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Volumn 24, Issue 4, 2000, Pages 507-529

Carbohydrate and energy-yielding metabolism in non-conventional yeasts

Author keywords

Carbohydrate metabolism; Catabolite repression; Non conventional yeast; Respiration; Tricarboxylic acid cycle

Indexed keywords

CANDIDA; CARBOHYDRATE METABOLISM; CELL RESPIRATION; CITRIC ACID CYCLE; ENERGY METABOLISM; FERMENTATION; GENETIC VARIABILITY; GLUCONEOGENESIS; GLYCOLYSIS; KLUYVEROMYCES; NONHUMAN; PENTOSE PHOSPHATE CYCLE; PICHIA; REVIEW; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES; YARROWIA; YEAST;

EID: 0342472225     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(00)00037-1     Document Type: Review
Times cited : (193)

References (273)
  • 1
    • 0009986107 scopus 로고
    • Identification and clustering of lactic acid bacteria and yeasts from wheat sourdoughs of central Italy
    • Gobetti I., Corsetti A., Rossi J., La Rosa F., De Vincenzi S. Identification and clustering of lactic acid bacteria and yeasts from wheat sourdoughs of central Italy. Ital. J. Food. Sci. 6:1994;85-94.
    • (1994) Ital. J. Food. Sci. , vol.6 , pp. 85-94
    • Gobetti, I.1    Corsetti, A.2    Rossi, J.3    La Rosa, F.4    De Vincenzi, S.5
  • 2
    • 0029822554 scopus 로고    scopus 로고
    • Characterization of the yeast population from traditional corn and rye bread doughs
    • Almeida M.J., Pais C.J. Characterization of the yeast population from traditional corn and rye bread doughs. Lett. Appl. Microbiol. 23:1996;154-158.
    • (1996) Lett. Appl. Microbiol. , vol.23 , pp. 154-158
    • Almeida, M.J.1    Pais, C.J.2
  • 4
    • 0013936130 scopus 로고
    • The Crabtree effect: A regulatory system in yeast
    • De Deken R.H. The Crabtree effect: a regulatory system in yeast. J. Gen. Microbiol. 44:1966;149-156.
    • (1966) J. Gen. Microbiol. , vol.44 , pp. 149-156
    • De Deken, R.H.1
  • 5
    • 0019750424 scopus 로고
    • Regulation of glucose metabolism in growing yeast cells
    • Fiechter A. Regulation of glucose metabolism in growing yeast cells. Adv. Microb. Physiol. 22:1981;123-183.
    • (1981) Adv. Microb. Physiol. , vol.22 , pp. 123-183
    • Fiechter, A.1
  • 6
    • 0006900439 scopus 로고
    • Energy-yielding metabolism in yeasts
    • (Rose, A.H. and Harrison, J.S., Eds.), Academic Press, London
    • Sols, A., Gancedo, C. and De la Fuente, G. (1971) Energy-yielding metabolism in yeasts. In: The Yeasts (Rose, A.H. and Harrison, J.S., Eds.), Vol. 2, pp. 271-308. Academic Press, London.
    • (1971) In: The Yeasts , vol.2 , pp. 271-308
    • Sols, A.1    Gancedo, C.2    De La Fuente, G.3
  • 7
    • 0001776017 scopus 로고
    • Carbohydrate metabolism
    • (Strathern, J.N., Jones, E.W. and Broach, J.R., Eds.), Cold Spring Harbor Laboratory, Cold Spring Harbor
    • Fraenkel, D.G. (1982) Carbohydrate metabolism. In: The Molecular Biology of the Yeast Saccharomyces (Strathern, J.N., Jones, E.W. and Broach, J.R., Eds.), Vol. 1, pp. 1-37. Cold Spring Harbor Laboratory, Cold Spring Harbor.
    • (1982) In: The Molecular Biology of the Yeast Saccharomyces , vol.1 , pp. 1-37
    • Fraenkel, D.G.1
  • 8
    • 0000676550 scopus 로고
    • Energy yielding metabolism
    • (Rose, A.H. and Harrison, J.S., Eds.), 2nd edn., Academic Press, London
    • Gancedo, C. and Serrano, R. (1989) Energy yielding metabolism. In: The Yeasts (Rose, A.H. and Harrison, J.S., Eds.), 2nd edn., Vol. 3, pp. 205-260. Academic Press, London.
    • (1989) In: The Yeasts , vol.3 , pp. 205-260
    • Gancedo, C.1    Serrano, R.2
  • 11
  • 12
    • 0343370910 scopus 로고
    • Carbohydrate metabolism
    • Sols A. Carbohydrate metabolism. Annu. Rev. Biochem. 30:1961;213-238.
    • (1961) Annu. Rev. Biochem. , vol.30 , pp. 213-238
    • Sols, A.1
  • 13
    • 0030953385 scopus 로고    scopus 로고
    • The molecular genetics of hexose transport in yeasts
    • Boles E., Hollenberg C.P. The molecular genetics of hexose transport in yeasts. FEMS Microbiol. Rev. 21:1997;85-111.
    • (1997) FEMS Microbiol. Rev. , vol.21 , pp. 85-111
    • Boles, E.1    Hollenberg, C.P.2
  • 14
    • 0032865543 scopus 로고    scopus 로고
    • Function and regulation of yeast hexose transporters
    • Özcan S., Johnston M. Function and regulation of yeast hexose transporters. Microbiol. Mol. Biol. Rev. 63:1999;554-569.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 554-569
    • Özcan, S.1    Johnston, M.2
  • 17
    • 0026780836 scopus 로고
    • Glucose transport in the yeast Kluyveromyces lactis. I. Properties of an inducible low-affinity glucose transporter gene
    • Wesolowski-Louvel M., Goffrini P., Ferrero I., Fukuhara H. Glucose transport in the yeast Kluyveromyces lactis. I. Properties of an inducible low-affinity glucose transporter gene. Mol. Gen. Genet. 233:1992;89-96.
    • (1992) Mol. Gen. Genet. , vol.233 , pp. 89-96
    • Wesolowski-Louvel, M.1    Goffrini, P.2    Ferrero, I.3    Fukuhara, H.4
  • 18
    • 0030797933 scopus 로고    scopus 로고
    • Influence of mutations in hexose-transporter genes on glucose repression in Kluyveromyces lactis
    • Weirich J., Goffrini P., Kuger P., Ferrero I., Breunig K. Influence of mutations in hexose-transporter genes on glucose repression in Kluyveromyces lactis. Eur. J. Biochem. 249:1997;248-257.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 248-257
    • Weirich, J.1    Goffrini, P.2    Kuger, P.3    Ferrero, I.4    Breunig, K.5
  • 19
    • 0026719343 scopus 로고
    • Glucose transport in the yeast Kluyveromyces lactis. II. Transcriptional regulation of the glucose transporter gene RAG1
    • Chen X.J., Wesolowski-Louvel M., Fukuhara H. Glucose transport in the yeast Kluyveromyces lactis. II. Transcriptional regulation of the glucose transporter gene RAG1. Mol. Gen. Genet. 233:1992;97-105.
    • (1992) Mol. Gen. Genet. , vol.233 , pp. 97-105
    • Chen, X.J.1    Wesolowski-Louvel, M.2    Fukuhara, H.3
  • 20
    • 0025821220 scopus 로고
    • A phosphoglucose isomerase gene is involved in the Rag phenotype of the yeast Kluyveromyces lactis
    • Goffrini P., Wesolowski-Louvel M., Ferrero I. A phosphoglucose isomerase gene is involved in the Rag phenotype of the yeast Kluyveromyces lactis. Mol. Gen. Genet. 228:1991;401-409.
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 401-409
    • Goffrini, P.1    Wesolowski-Louvel, M.2    Ferrero, I.3
  • 21
    • 0024285095 scopus 로고
    • The RAG2 gene of the yeast Kluyveromyces lactis codes for a putative phosphoglucose isomerase
    • Wesolowski-Louvel M., Goffrini P., Ferrero I. The RAG2 gene of the yeast Kluyveromyces lactis codes for a putative phosphoglucose isomerase. Nucleic Acids Res. 16:1988;8714.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 8714
    • Wesolowski-Louvel, M.1    Goffrini, P.2    Ferrero, I.3
  • 22
    • 0027280268 scopus 로고
    • The hexokinase gene is required for transcriptional regulation of the glucose transporter gene RAG1 in Kluyveromyces lactis
    • Prior C., Mamessier P., Fukuhara H., Chen X.J., Wésolowski-Louvel M. The hexokinase gene is required for transcriptional regulation of the glucose transporter gene RAG1 in Kluyveromyces lactis. Mol. Cell. Biol. 13:1993;3882-3889.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3882-3889
    • Prior, C.1    Mamessier, P.2    Fukuhara, H.3    Chen, X.J.4    Wésolowski-Louvel, M.5
  • 23
    • 0031026141 scopus 로고    scopus 로고
    • The Kluyveromyces lactis equivalent of casein kinase I is required for the transcription of the gene encoding the low-affinity glucose permease
    • Blaisonneau J., Fukuhara H., Wesolowski-Louvel M. The Kluyveromyces lactis equivalent of casein kinase I is required for the transcription of the gene encoding the low-affinity glucose permease. Mol. Gen. Genet. 253:1997;469-477.
    • (1997) Mol. Gen. Genet. , vol.253 , pp. 469-477
    • Blaisonneau, J.1    Fukuhara, H.2    Wesolowski-Louvel, M.3
  • 26
    • 0031036063 scopus 로고    scopus 로고
    • Mechanism of glucose and maltose transport in plasma-membrane vesicles from the yeast Candida utilis
    • van den Broek P.J.A., van Gompel A.E., Luttik M.A.H., Pronk J.T., van Leeuwen C.M. Mechanism of glucose and maltose transport in plasma-membrane vesicles from the yeast Candida utilis. Biochem. J. 321:1997;487-495.
    • (1997) Biochem. J. , vol.321 , pp. 487-495
    • Van Den Broek, P.J.A.1    Van Gompel, A.E.2    Luttik, M.A.H.3    Pronk, J.T.4    Van Leeuwen, C.M.5
  • 27
    • 0032961329 scopus 로고    scopus 로고
    • Cloning and characterization of three genes (SUT1-3) encoding glucose transporters of the yeast Pichia stipitis
    • Weierstall T., Hollenberg C.P., Boles E. Cloning and characterization of three genes (SUT1-3) encoding glucose transporters of the yeast Pichia stipitis. Mol. Microbiol. 31:1999;871-883.
    • (1999) Mol. Microbiol. , vol.31 , pp. 871-883
    • Weierstall, T.1    Hollenberg, C.P.2    Boles, E.3
  • 28
    • 0024638420 scopus 로고
    • Comparison of glucose uptake kinetics in different yeasts
    • Does A.L., Bisson L.F. Comparison of glucose uptake kinetics in different yeasts. J. Bacteriol. 171:1989;1303-1308.
    • (1989) J. Bacteriol. , vol.171 , pp. 1303-1308
    • Does, A.L.1    Bisson, L.F.2
  • 29
    • 0001267868 scopus 로고
    • Aerobic and anaerobic uptake of sugars in Schizosaccharomyces pombe
    • Höfer M., Nassar F.R. Aerobic and anaerobic uptake of sugars in Schizosaccharomyces pombe. J. Gen. Microbiol. 133:1987;2163-2172.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 2163-2172
    • Höfer, M.1    Nassar, F.R.2
  • 31
    • 0031936791 scopus 로고    scopus 로고
    • Std1, a gene involved in glucose transport in Schizosaccharomyces pombe
    • Mehta S.V., Patil V.B., Velmurugan S., Lobo Z., Maitra P.K. std1, a gene involved in glucose transport in Schizosaccharomyces pombe. J. Bacteriol. 180:1998;674-679.
    • (1998) J. Bacteriol. , vol.180 , pp. 674-679
    • Mehta, S.V.1    Patil, V.B.2    Velmurugan, S.3    Lobo, Z.4    Maitra, P.K.5
  • 32
    • 0023353293 scopus 로고
    • Isolation and characterization of mutants of Kluyveromyces lactis defective in lactose transport
    • Riley M.I., Srekrishna K., Bhairi S., Dickson R.C. Isolation and characterization of mutants of Kluyveromyces lactis defective in lactose transport. Mol. Gen. Genet. 208:1987;145-151.
    • (1987) Mol. Gen. Genet. , vol.208 , pp. 145-151
    • Riley, M.I.1    Srekrishna, K.2    Bhairi, S.3    Dickson, R.C.4
  • 33
    • 0026592624 scopus 로고
    • D-Gluconate is an alternative growth substrate for cultivation of Schizosaccharomyces pombe mutants
    • Hoever M., Milbradt B., Höfer M. D-Gluconate is an alternative growth substrate for cultivation of Schizosaccharomyces pombe mutants. Arch. Microbiol. 157:1992;191-193.
    • (1992) Arch. Microbiol. , vol.157 , pp. 191-193
    • Hoever, M.1    Milbradt, B.2    Höfer, M.3
  • 34
    • 0030810379 scopus 로고    scopus 로고
    • + gene product
    • + gene product. J. Cell. Sci. 110:1997;2599-2608.
    • (1997) J. Cell. Sci. , vol.110 , pp. 2599-2608
    • Caspari, T.1
  • 35
    • 0030597182 scopus 로고    scopus 로고
    • + symporter of Schizosaccharomyces pombe cells is down-regulated by D-glucose and exogenous cAMP
    • + symporter of Schizosaccharomyces pombe cells is down-regulated by D-glucose and exogenous cAMP. FEBS Lett. 395:1996;272-276.
    • (1996) FEBS Lett. , vol.395 , pp. 272-276
    • Caspari, T.1    Urlinger, S.2
  • 36
    • 0033028545 scopus 로고    scopus 로고
    • Glucose repression of the Kluyveromyces lactis invertase gene KlINV1 does not require Mig1p
    • Georis I., Cassart J.P., Breunig K.D., Vandenhaute J. Glucose repression of the Kluyveromyces lactis invertase gene KlINV1 does not require Mig1p. Mol. Gen. Genet. 261:1999;862-870.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 862-870
    • Georis, I.1    Cassart, J.P.2    Breunig, K.D.3    Vandenhaute, J.4
  • 37
    • 0032582030 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the gene encoding invertase (INV1) from the yeast Candida utilis
    • Chávez F.P., Pons T., Delgado J.M., Rodríguez L. Cloning and sequence analysis of the gene encoding invertase (INV1) from the yeast Candida utilis. Yeast. 14:1998;1223-1232.
    • (1998) Yeast , vol.14 , pp. 1223-1232
    • Chávez, F.P.1    Pons, T.2    Delgado, J.M.3    Rodríguez, L.4
  • 39
    • 0027196481 scopus 로고
    • Role of maltase in the utilization of sucrose by Candida albicans
    • Williamson P.R., Huber M.A., Bennett J.E. Role of maltase in the utilization of sucrose by Candida albicans. Biochem. J. 291:1993;765-771.
    • (1993) Biochem. J. , vol.291 , pp. 765-771
    • Williamson, P.R.1    Huber, M.A.2    Bennett, J.E.3
  • 40
    • 0026673556 scopus 로고
    • Cloning and characterization of a Candida albicans maltase gene involved in sucrose utilization
    • Geber A., Williamson P.R., Rex J.H., Sweemey E.C., Bennett J.E. Cloning and characterization of a Candida albicans maltase gene involved in sucrose utilization. J. Bacteriol. 174:1992;6992-6996.
    • (1992) J. Bacteriol. , vol.174 , pp. 6992-6996
    • Geber, A.1    Williamson, P.R.2    Rex, J.H.3    Sweemey, E.C.4    Bennett, J.E.5
  • 41
    • 0020505047 scopus 로고
    • Characterization of lactose transport in Kluyveromyces lactis
    • Dickson R.C., Barr K. Characterization of lactose transport in Kluyveromyces lactis. J. Bacteriol. 154:1983;1245-1251.
    • (1983) J. Bacteriol. , vol.154 , pp. 1245-1251
    • Dickson, R.C.1    Barr, K.2
  • 42
    • 0022372049 scopus 로고
    • Construction of strains of Saccharomyces cerevisiae that grow on lactose
    • Sreekrishna K., Dickson R.C. Construction of strains of Saccharomyces cerevisiae that grow on lactose. Proc. Natl. Acad. Sci. USA. 82:1985;7909-7913.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7909-7913
    • Sreekrishna, K.1    Dickson, R.C.2
  • 43
    • 0022038375 scopus 로고
    • A positive regulatory element is involved in the induction of the beta-galactosidase gene from Kluyveromyces lactis
    • Das S., Breunig K.D., Hollenberg C.P. A positive regulatory element is involved in the induction of the beta-galactosidase gene from Kluyveromyces lactis. EMBO J. 4:1985;793-798.
    • (1985) EMBO J. , vol.4 , pp. 793-798
    • Das, S.1    Breunig, K.D.2    Hollenberg, C.P.3
  • 45
    • 0028797325 scopus 로고
    • Transcriptional regulation of the Saccharomyces cerevisiae HXK1, HXK2 and GLK1 genes
    • Herrero P., Galindez J., Ruiz N., Martinez-Campa C., Moreno F. Transcriptional regulation of the Saccharomyces cerevisiae HXK1, HXK2 and GLK1 genes. Yeast. 11:1995;137-144.
    • (1995) Yeast , vol.11 , pp. 137-144
    • Herrero, P.1    Galindez, J.2    Ruiz, N.3    Martinez-Campa, C.4    Moreno, F.5
  • 46
    • 0017576189 scopus 로고
    • Glucose-phosphorylating enzymes of Candida yeasts and their regulation in vivo
    • Hirai M., Ohtani E., Tanaka A., Fukui S. Glucose-phosphorylating enzymes of Candida yeasts and their regulation in vivo. Biochim. Biophys. Acta. 480:1977;357-366.
    • (1977) Biochim. Biophys. Acta , vol.480 , pp. 357-366
    • Hirai, M.1    Ohtani, E.2    Tanaka, A.3    Fukui, S.4
  • 47
    • 0032697881 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene HXK1 encoding the hexokinase from Yarrowia lipolytica
    • Petit T., Gancedo C. Molecular cloning and characterization of the gene HXK1 encoding the hexokinase from Yarrowia lipolytica. Yeast. 15:1999;1573-1584.
    • (1999) Yeast , vol.15 , pp. 1573-1584
    • Petit, T.1    Gancedo, C.2
  • 48
    • 0343930747 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: Biochemical and molecular characterization of both hexokinases
    • Petit T., Blázquez M.A., Gancedo C. Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: biochemical and molecular characterization of both hexokinases. FEBS Lett. 378:1996;185-189.
    • (1996) FEBS Lett. , vol.378 , pp. 185-189
    • Petit, T.1    Blázquez, M.A.2    Gancedo, C.3
  • 50
    • 0032578633 scopus 로고    scopus 로고
    • 213/Asn in the hexokinase 1 gene from Schizosaccharomyces pombe increases its affinity for glucose
    • 213/Asn in the hexokinase 1 gene from Schizosaccharomyces pombe increases its affinity for glucose. Biochem. Biophys. Res. Commun. 251:1998;714-719.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 714-719
    • Petit, T.1    Herrero, P.2    Gancedo, C.3
  • 51
    • 0027305174 scopus 로고
    • Trehalose-6-phosphate, a new regulator of yeast glycolysis that inhibits hexokinases
    • Blázquez M.A., Lagunas R., Gancedo C., Gancedo J.M. Trehalose-6-phosphate, a new regulator of yeast glycolysis that inhibits hexokinases. FEBS Lett. 329:1993;51-54.
    • (1993) FEBS Lett. , vol.329 , pp. 51-54
    • Blázquez, M.A.1    Lagunas, R.2    Gancedo, C.3    Gancedo, J.M.4
  • 52
    • 0028024214 scopus 로고
    • Use of Yarrowia lipolytica hexokinase for the quantitative determination of trehalose-6-phosphate
    • Blázquez M.A., Gancedo J.M., Gancedo C. Use of Yarrowia lipolytica hexokinase for the quantitative determination of trehalose-6-phosphate. FEMS Microbiol. Lett. 121:1994;223-228.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 223-228
    • Blázquez, M.A.1    Gancedo, J.M.2    Gancedo, C.3
  • 53
    • 0015125608 scopus 로고
    • Glucose and fructose metabolism in a phosphoglucoseisomerase less mutant of Saccharomyces cerevisiae
    • Maitra P.K. Glucose and fructose metabolism in a phosphoglucoseisomerase less mutant of Saccharomyces cerevisiae. J. Bacteriol. 107:1971;759-769.
    • (1971) J. Bacteriol. , vol.107 , pp. 759-769
    • Maitra, P.K.1
  • 54
    • 0342679075 scopus 로고    scopus 로고
    • Reoxidation of the NADPH produced by the pentose phosphate pathway is necessary for the utilization of glucose by Kluyveromyces lactis rag2 mutants
    • González Siso M.I., Freire Picos M.A., Cerdán M.E. Reoxidation of the NADPH produced by the pentose phosphate pathway is necessary for the utilization of glucose by Kluyveromyces lactis rag2 mutants. FEBS Lett. 387:1996;7-10.
    • (1996) FEBS Lett. , vol.387 , pp. 7-10
    • González Siso, M.I.1    Freire Picos, M.A.2    Cerdán, M.E.3
  • 55
    • 0019751252 scopus 로고
    • Multimodulation of enzyme activity
    • Sols A. Multimodulation of enzyme activity. Curr. Top. Cell. Regul. 19:1981;77-101.
    • (1981) Curr. Top. Cell. Regul. , vol.19 , pp. 77-101
    • Sols, A.1
  • 56
    • 0024694679 scopus 로고
    • Overproduction of glycolytic enzymes in yeast
    • Schaaff, I., Heinischm, J., Zimmermann, F.K. (1989) Overproduction of glycolytic enzymes in yeast. Yeast 5, 285-290.
    • (1989) Yeast , vol.5 , pp. 285-290
    • Schaaff, I.1    Heinischm, J.2    Zimmermann, F.K.3
  • 57
    • 0022595650 scopus 로고
    • Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast
    • Heinisch J. Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast. Mol. Gen. Genet. 202:1986;75-82.
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 75-82
    • Heinisch, J.1
  • 58
    • 0018527496 scopus 로고
    • Molecular democracy: Who shares the controls?
    • Kacser H., Burns J.A. Molecular democracy: who shares the controls? Biochem. Soc. Trans. 7:1979;1149-1160.
    • (1979) Biochem. Soc. Trans. , vol.7 , pp. 1149-1160
    • Kacser, H.1    Burns, J.A.2
  • 59
    • 0030838251 scopus 로고    scopus 로고
    • Purification and characterization of phosphofructokinase from the yeast Kluyveromyces lactis
    • Bar J., Schellenberger W., Kopperschläger G. Purification and characterization of phosphofructokinase from the yeast Kluyveromyces lactis. Yeast. 13:1997;1309-1317.
    • (1997) Yeast , vol.13 , pp. 1309-1317
    • Bar, J.1    Schellenberger, W.2    Kopperschläger, G.3
  • 61
    • 0020481613 scopus 로고
    • Mutant studies of yeast phosphofructokinase
    • Clifton D., Fraenkel D.G. Mutant studies of yeast phosphofructokinase. Biochemistry. 21:1982;1935-1942.
    • (1982) Biochemistry , vol.21 , pp. 1935-1942
    • Clifton, D.1    Fraenkel, D.G.2
  • 62
    • 0027368793 scopus 로고
    • Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence that glucose can be metabolized through the pentose phosphate pathway
    • Jacoby J., Hollenberg P., Heinisch J.J. Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence that glucose can be metabolized through the pentose phosphate pathway. Mol. Microbiol. 10:1993;867-876.
    • (1993) Mol. Microbiol. , vol.10 , pp. 867-876
    • Jacoby, J.1    Hollenberg, P.2    Heinisch, J.J.3
  • 63
    • 0033557828 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of phosphofructokinase from the opportunistic pathogenic yeast Candida albicans
    • Lorberg A., Kirchrath L., Ernst J.F., Heinisch J.J. Genetic and biochemical characterization of phosphofructokinase from the opportunistic pathogenic yeast Candida albicans. Eur. J. Biochem. 260:1999;217-226.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 217-226
    • Lorberg, A.1    Kirchrath, L.2    Ernst, J.F.3    Heinisch, J.J.4
  • 64
    • 0030883562 scopus 로고    scopus 로고
    • Glucose-induced microautophagy in Pichia pastoris requires the alpha-subunit of phosphofructokinase
    • Yuan W., Tuttle D.L., Shi Y.J., Ralph G.S., Dunn W.A. Glucose-induced microautophagy in Pichia pastoris requires the alpha-subunit of phosphofructokinase. J. Cell. Sci. 110:1997;1935-1945.
    • (1997) J. Cell. Sci. , vol.110 , pp. 1935-1945
    • Yuan, W.1    Tuttle, D.L.2    Shi, Y.J.3    Ralph, G.S.4    Dunn, W.A.5
  • 66
    • 0028006491 scopus 로고
    • Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of the class II fructose-1, 6-bisphosphate aldolase gene
    • Mutoh N., Hayashi Y. Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of the class II fructose-1, 6-bisphosphate aldolase gene. Biochim. Biophys. Acta. 1183:1994;550-552.
    • (1994) Biochim. Biophys. Acta , vol.1183 , pp. 550-552
    • Mutoh, N.1    Hayashi, Y.2
  • 67
    • 0013894154 scopus 로고
    • Fructose 1, 6-diphosphate aldolase of Candida utilis: Purification and properties
    • Kowal J., Cremona T., Horecker B.L. Fructose 1, 6-diphosphate aldolase of Candida utilis: purification and properties. Arch. Biochem. Biophys. 114:1966;13-23.
    • (1966) Arch. Biochem. Biophys. , vol.114 , pp. 13-23
    • Kowal, J.1    Cremona, T.2    Horecker, B.L.3
  • 68
    • 0022312921 scopus 로고
    • Transcription of the triose-phosphate-isomerase gene of Schizosaccharomyces pombe initiates from a start point different from that in Saccharomyces cerevisiae
    • Russell P.R. Transcription of the triose-phosphate-isomerase gene of Schizosaccharomyces pombe initiates from a start point different from that in Saccharomyces cerevisiae. Gene. 40:1985;125-130.
    • (1985) Gene , vol.40 , pp. 125-130
    • Russell, P.R.1
  • 69
    • 0032875841 scopus 로고    scopus 로고
    • Isolation, nucleotide sequence, and physiological relevance of the gene encoding triose phosphate isomerase from Kluyveromyces lactis
    • Compagno C., Boschi F., Daleffe A., Porro D., Ranzi B.M. Isolation, nucleotide sequence, and physiological relevance of the gene encoding triose phosphate isomerase from Kluyveromyces lactis. Appl. Environ. Microbiol. 65:1999;4216-4219.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4216-4219
    • Compagno, C.1    Boschi, F.2    Daleffe, A.3    Porro, D.4    Ranzi, B.M.5
  • 70
    • 0022385984 scopus 로고
    • Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenases genes
    • McAlister L., Holland M.J. Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenases genes. J. Biol. Chem. 260:1985;15019-15027.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15019-15027
    • McAlister, L.1    Holland, M.J.2
  • 71
    • 0025314813 scopus 로고
    • Kluyveromyces lactis glyceraldehyde-3-phosphate dehydrogenase and alcohol dehydrogenase-1 genes are linked and divergently transcribed
    • Shuster J.R. Kluyveromyces lactis glyceraldehyde-3-phosphate dehydrogenase and alcohol dehydrogenase-1 genes are linked and divergently transcribed. Nucleic Acids Res. 18:1990;4271.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4271
    • Shuster, J.R.1
  • 72
    • 0029052878 scopus 로고
    • Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene family from Kluyveromyces marxianus. Polymerase chain reaction-single-strand conformation polymorphism as a tool for the study of multigenic families
    • Fernandes P.A., Sena-Esteves M., Moradas-Ferreira P. Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene family from Kluyveromyces marxianus. Polymerase chain reaction-single-strand conformation polymorphism as a tool for the study of multigenic families. Yeast. 11:1995;725-733.
    • (1995) Yeast , vol.11 , pp. 725-733
    • Fernandes, P.A.1    Sena-Esteves, M.2    Moradas-Ferreira, P.3
  • 73
    • 0032819504 scopus 로고    scopus 로고
    • Purification of a biologically active recombinant glyceraldehyde-3-phosphate dehydrogenase from Candida albicans
    • Villamon E., Gozalbo D., Martínez J.P., Gil M.L. Purification of a biologically active recombinant glyceraldehyde-3-phosphate dehydrogenase from Candida albicans. FEMS Microbiol. Lett. 179:1999;61-65.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 61-65
    • Villamon, E.1    Gozalbo, D.2    Martínez, J.P.3    Gil, M.L.4
  • 74
    • 0033056208 scopus 로고    scopus 로고
    • Clinical strains of Candida albicans express the surface antigen glyceraldehyde-3-phosphate dehydrogenase in vitro and in infected tissues
    • Gil M.L., Villamon E., Monteagudo C., Gozalbo D., Martínez J.P. Clinical strains of Candida albicans express the surface antigen glyceraldehyde-3-phosphate dehydrogenase in vitro and in infected tissues. FEMS Immunol. Med. Microbiol. 23:1999;229-234.
    • (1999) FEMS Immunol. Med. Microbiol. , vol.23 , pp. 229-234
    • Gil, M.L.1    Villamon, E.2    Monteagudo, C.3    Gozalbo, D.4    Martínez, J.P.5
  • 75
    • 0031579445 scopus 로고    scopus 로고
    • Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter
    • Waterham H.R., Digan M.E., Koutz P.J., Lair S.V., Cregg J.M. Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter. Gene. 186:1997;37-44.
    • (1997) Gene , vol.186 , pp. 37-44
    • Waterham, H.R.1    Digan, M.E.2    Koutz, P.J.3    Lair, S.V.4    Cregg, J.M.5
  • 77
    • 0025058445 scopus 로고
    • The primary structure of the 3-phosphoglycerate kinase (PGK) gene from Kluyveromyces lactis
    • Fournier A., Fleer R., Yeh P., Mayaux J.F. The primary structure of the 3-phosphoglycerate kinase (PGK) gene from Kluyveromyces lactis. Nucleic Acids Res. 18:1990;365.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 365
    • Fournier, A.1    Fleer, R.2    Yeh, P.3    Mayaux, J.F.4
  • 78
    • 0028354515 scopus 로고
    • Expression of an endogenous and a heterologous gene in Candida maltosa by using a promoter of a newly isolated phosphoglycerate kinase (PGK) gene
    • Masuda Y., Park S.M., Ohkuma M., Ohta A., Takagi M. Expression of an endogenous and a heterologous gene in Candida maltosa by using a promoter of a newly isolated phosphoglycerate kinase (PGK) gene. Curr. Genet. 25:1994;412-417.
    • (1994) Curr. Genet. , vol.25 , pp. 412-417
    • Masuda, Y.1    Park, S.M.2    Ohkuma, M.3    Ohta, A.4    Takagi, M.5
  • 79
    • 1842301085 scopus 로고    scopus 로고
    • 3-Phosphoglycerate kinase: A glycolytic enzyme protein present in the cell wall of Candida albicans
    • Alloussh H.M., Lopez-Ribot J.L., Masten B.J., Chaffin W.L. 3-Phosphoglycerate kinase: a glycolytic enzyme protein present in the cell wall of Candida albicans. Microbiology. 143:1997;321-330.
    • (1997) Microbiology , vol.143 , pp. 321-330
    • Alloussh, H.M.1    Lopez-Ribot, J.L.2    Masten, B.J.3    Chaffin, W.L.4
  • 80
    • 0030115596 scopus 로고    scopus 로고
    • The 3-phosphoglycerate kinase gene of the yeast Yarrowia lipolytica de-represses on gluconeogenic substrates
    • Le Dall M., Nicaud J., Treton B.Y., Gaillardin C.M. The 3-phosphoglycerate kinase gene of the yeast Yarrowia lipolytica de-represses on gluconeogenic substrates. Curr. Genet. 29:1996;446-456.
    • (1996) Curr. Genet. , vol.29 , pp. 446-456
    • Le Dall, M.1    Nicaud, J.2    Treton, B.Y.3    Gaillardin, C.M.4
  • 82
    • 0027955469 scopus 로고
    • The amino acid sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe
    • Nairn J., Price N.J., Fothergill-Gilmore L.A., Walker G.A., Fothergill J.E., Dunbar B. The amino acid sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe. Biochem. J. 297:1994;603-608.
    • (1994) Biochem. J. , vol.297 , pp. 603-608
    • Nairn, J.1    Price, N.J.2    Fothergill-Gilmore, L.A.3    Walker, G.A.4    Fothergill, J.E.5    Dunbar, B.6
  • 83
    • 0018084041 scopus 로고
    • Isolation and identification of yeast messenger nucleic acids coding for enolase, glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase
    • Holland M.J., Holland J.P. Isolation and identification of yeast messenger nucleic acids coding for enolase, glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase. Biochemistry. 17:1978;4900-4907.
    • (1978) Biochemistry , vol.17 , pp. 4900-4907
    • Holland, M.J.1    Holland, J.P.2
  • 84
    • 0020490759 scopus 로고
    • The targeted deletion of a yeast enolase structural gene
    • McAlister L., Holland M.J. The targeted deletion of a yeast enolase structural gene. J. Biol. Chem. 257:1982;7181-7188.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7181-7188
    • McAlister, L.1    Holland, M.J.2
  • 85
    • 0027167774 scopus 로고
    • Molecular cloning and characterization of the Candida albicans enolase gene
    • Mason A.B., Buckley H.R., Gorman J.A. Molecular cloning and characterization of the Candida albicans enolase gene. J. Bacteriol. 175:1993;2632-2639.
    • (1993) J. Bacteriol. , vol.175 , pp. 2632-2639
    • Mason, A.B.1    Buckley, H.R.2    Gorman, J.A.3
  • 86
    • 0028926766 scopus 로고
    • Genetic organization and mRNA expression of enolase genes of Candida albicans
    • Postlethwait P., Sundstrom P. Genetic organization and mRNA expression of enolase genes of Candida albicans. J. Bacteriol. 177:1995;1772-1779.
    • (1995) J. Bacteriol. , vol.177 , pp. 1772-1779
    • Postlethwait, P.1    Sundstrom, P.2
  • 87
    • 0028842193 scopus 로고
    • A cDNA from Schizosaccharomyces pombe encoding a putative enolase
    • Jackson J.C., Lopes J.M. A cDNA from Schizosaccharomyces pombe encoding a putative enolase. Gene. 154:1995;109-113.
    • (1995) Gene , vol.154 , pp. 109-113
    • Jackson, J.C.1    Lopes, J.M.2
  • 88
    • 0030971548 scopus 로고    scopus 로고
    • Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate
    • Boles E., Schulte F., Miosga T., Freidel K., Schluter E., Zimmermann F.K., Hollenberg C.P., Heinisch J.J. Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate. J. Bacteriol. 179:1997;2987-2993.
    • (1997) J. Bacteriol. , vol.179 , pp. 2987-2993
    • Boles, E.1    Schulte, F.2    Miosga, T.3    Freidel, K.4    Schluter, E.5    Zimmermann, F.K.6    Hollenberg, C.P.7    Heinisch, J.J.8
  • 89
    • 0028804016 scopus 로고
    • Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe: Implications for quaternary structure and regulation of the enzyme
    • Nairn J., Smith S., Allison P.J., Rigden D., Fothergill-More L.A., Price N.C. Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe: implications for quaternary structure and regulation of the enzyme. FEMS Microbiol. Lett. 134:1995;221-226.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 221-226
    • Nairn, J.1    Smith, S.2    Allison, P.J.3    Rigden, D.4    Fothergill-More, L.A.5    Price, N.C.6
  • 90
    • 0026641224 scopus 로고
    • The isolation and characterization of the pyruvate kinase encoding gene from the yeast Yarrowia lipolytica
    • Strick C.A., James L.C., O'Donnell M.M., Gollaher M.G., Franke A.E. The isolation and characterization of the pyruvate kinase encoding gene from the yeast Yarrowia lipolytica. Gene. 118:1992;65-72.
    • (1992) Gene , vol.118 , pp. 65-72
    • Strick, C.A.1    James, L.C.2    O'Donnell, M.M.3    Gollaher, M.G.4    Franke, A.E.5
  • 91
    • 0028212347 scopus 로고
    • The isolation and characterization of the pyruvate kinase-encoding gene from the yeast Yarrowia lipolytica
    • Strick C.A., James L.C., O'Donnell M.M., Gollaher M.G., Franke A.E. The isolation and characterization of the pyruvate kinase-encoding gene from the yeast Yarrowia lipolytica. Gene. 140:1994;141-143.
    • (1994) Gene , vol.140 , pp. 141-143
    • Strick, C.A.1    James, L.C.2    O'Donnell, M.M.3    Gollaher, M.G.4    Franke, A.E.5
  • 92
    • 0014054113 scopus 로고
    • Regulation of the concentration or activity of pyruvate kinase in yeasts and its relationship to gluconeogenesis
    • Gancedo J.M., Gancedo C., Sols A. Regulation of the concentration or activity of pyruvate kinase in yeasts and its relationship to gluconeogenesis. Biochem. J. 102:1967;23C-25C.
    • (1967) Biochem. J. , vol.102
    • Gancedo, J.M.1    Gancedo, C.2    Sols, A.3
  • 93
    • 0016687235 scopus 로고
    • Difference in pyruvate kinase regulation among three groups of yeasts
    • Hirai M., Tanaka A., Fukui S. Difference in pyruvate kinase regulation among three groups of yeasts. Biochim. Biophys. Acta. 391:1975;282-291.
    • (1975) Biochim. Biophys. Acta , vol.391 , pp. 282-291
    • Hirai, M.1    Tanaka, A.2    Fukui, S.3
  • 94
    • 0030448870 scopus 로고    scopus 로고
    • Pyruvate metabolism in Saccharomyces cerevisiae
    • Pronk J.T., Steensma H.Y., van Dijken J.P. Pyruvate metabolism in Saccharomyces cerevisiae. Yeast. 12:1996;1607-1633.
    • (1996) Yeast , vol.12 , pp. 1607-1633
    • Pronk, J.T.1    Steensma, H.Y.2    Van Dijken, J.P.3
  • 95
    • 0025111184 scopus 로고
    • Molecular cloning of the gene for the E1α subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae
    • Steensma H.Y., Holterman L., Dekker I., van Sluis C.A., Wenzel T.J. Molecular cloning of the gene for the E1α subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae. Eur. J. Biochem. 191:1990;769-774.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 769-774
    • Steensma, H.Y.1    Holterman, L.2    Dekker, I.3    Van Sluis, C.A.4    Wenzel, T.J.5
  • 96
    • 0024418681 scopus 로고
    • Nucleotide and deduced amino acid sequence of the alpha subunit of yeast pyruvate dehydrogenase
    • Behal R.H., Browning K.S., Reed L.J. Nucleotide and deduced amino acid sequence of the alpha subunit of yeast pyruvate dehydrogenase. Biochem. Biophys. Res. Commun. 164:1989;941-946.
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 941-946
    • Behal, R.H.1    Browning, K.S.2    Reed, L.J.3
  • 97
    • 0027450063 scopus 로고
    • Characterization of the PDHβ1, the structural gene for the pyruvate dehydrogenase β subunit from Saccharomyces cerevisiae
    • Miran S.G., Lawson J.E., Reed L.J. Characterization of the PDHβ1, the structural gene for the pyruvate dehydrogenase β subunit from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 90:1993;1252-1256.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1252-1256
    • Miran, S.G.1    Lawson, J.E.2    Reed, L.J.3
  • 98
    • 0024095046 scopus 로고
    • Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae
    • Niu X.-D., Browning K.S., Behal R.H., Reed L.J. Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 85:1988;7546-7550.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7546-7550
    • Niu, X.-D.1    Browning, K.S.2    Behal, R.H.3    Reed, L.J.4
  • 99
    • 0024015337 scopus 로고
    • The nucleotide sequence of the LDP1 gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae: Comparison between eukaryotic and prokaryotic sequences for related enzymes and identification of potential upstream control sites
    • Ross J., Reid G.A., Dawes I.A. The nucleotide sequence of the LDP1 gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae: comparison between eukaryotic and prokaryotic sequences for related enzymes and identification of potential upstream control sites. J. Gen. Microbiol. 134:1988;1131-1139.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1131-1139
    • Ross, J.1    Reid, G.A.2    Dawes, I.A.3
  • 100
    • 0025887857 scopus 로고
    • Purification and functional characterization of the pyruvate (monocarboxylate) carrier from baker's yeast mitochondria (Saccharomyces cerevisiae)
    • Nalecz M.J., Nalecz K.A., Azzi A. Purification and functional characterization of the pyruvate (monocarboxylate) carrier from baker's yeast mitochondria (Saccharomyces cerevisiae). Biochim. Biophys. Acta. 1079:1991;87-95.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 87-95
    • Nalecz, M.J.1    Nalecz, K.A.2    Azzi, A.3
  • 101
    • 0032774716 scopus 로고    scopus 로고
    • Impaired growth on glucose of a pyruvate dehydrogenase-negative mutant of Kluyveromyces lactis is due to a limitation in mitochondrial acetyl-coenzyme A uptake
    • Zeeman A.M., Luttik M.A., Pronk J.T., van Dijken J.P., Steensma H.Y. Impaired growth on glucose of a pyruvate dehydrogenase-negative mutant of Kluyveromyces lactis is due to a limitation in mitochondrial acetyl-coenzyme A uptake. FEMS Microbiol. Lett. 177:1999;23-28.
    • (1999) FEMS Microbiol. Lett. , vol.177 , pp. 23-28
    • Zeeman, A.M.1    Luttik, M.A.2    Pronk, J.T.3    Van Dijken, J.P.4    Steensma, H.Y.5
  • 102
    • 0032211885 scopus 로고    scopus 로고
    • The RAG3 gene of Kluyveromyces lactis is involved in the transcriptional regulation of genes coding for enzymes implicated in pyruvate utilization and genes of the biosynthesis of thiamine pyrophosphate
    • Tizzani L., Meacock P., Frontali L., Wesolowski-Louvel M. The RAG3 gene of Kluyveromyces lactis is involved in the transcriptional regulation of genes coding for enzymes implicated in pyruvate utilization and genes of the biosynthesis of thiamine pyrophosphate. FEMS Microbiol. Lett. 168:1998;25-30.
    • (1998) FEMS Microbiol. Lett. , vol.168 , pp. 25-30
    • Tizzani, L.1    Meacock, P.2    Frontali, L.3    Wesolowski-Louvel, M.4
  • 103
    • 0027330910 scopus 로고
    • Characterisation of PDC2, a gene necessary for high level expression of pyruvate decarboxylase structural genes in Saccharomyces cerevisiae
    • Hohmann S. Characterisation of PDC2, a gene necessary for high level expression of pyruvate decarboxylase structural genes in Saccharomyces cerevisiae. Mol. Gen. Genet. 241:1993;657-666.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 657-666
    • Hohmann, S.1
  • 104
    • 0028982636 scopus 로고
    • Cloning and sequence of a gene encoding the pyruvate dehydrogenase E1 beta subunit of Schizosacchromyces pombe
    • Cavan G., MacDonald D. Cloning and sequence of a gene encoding the pyruvate dehydrogenase E1 beta subunit of Schizosacchromyces pombe. Gene. 152:1995;117-120.
    • (1995) Gene , vol.152 , pp. 117-120
    • Cavan, G.1    MacDonald, D.2
  • 105
    • 0028173004 scopus 로고
    • Mutations which reduce levels of pyruvate dehydrogenase in Schizosaccharomyces pombe cause a requirement for arginine or glutamine
    • Cavan G., MacDonald D. Mutations which reduce levels of pyruvate dehydrogenase in Schizosaccharomyces pombe cause a requirement for arginine or glutamine. FEMS Microbiol. Lett. 124:1994;361-365.
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 361-365
    • Cavan, G.1    MacDonald, D.2
  • 106
    • 0030097349 scopus 로고    scopus 로고
    • Peculiarities of the regulation of fermentation and respiration in the Crabtree-negative, xylose fermenting yeast Pichia stipitis
    • Passoth V., Zimmermann M., Klinner U. Peculiarities of the regulation of fermentation and respiration in the Crabtree-negative, xylose fermenting yeast Pichia stipitis. Appl. Biochem. Biotechnol. 57-58:1996;201-212.
    • (1996) Appl. Biochem. Biotechnol. , vol.5758 , pp. 201-212
    • Passoth, V.1    Zimmermann, M.2    Klinner, U.3
  • 108
    • 0030049641 scopus 로고    scopus 로고
    • The 'petite negative' yeast Kluyveromyces lactis has a single gene expressing pyruvate decarboxylase activity
    • Bianchi M.M., Tizzani L., Destruelle M., Frontali L., Wesolowski-Louvel M. The 'petite negative' yeast Kluyveromyces lactis has a single gene expressing pyruvate decarboxylase activity. Mol. Microbiol. 19:1996;27-36.
    • (1996) Mol. Microbiol. , vol.19 , pp. 27-36
    • Bianchi, M.M.1    Tizzani, L.2    Destruelle, M.3    Frontali, L.4    Wesolowski-Louvel, M.5
  • 109
    • 0030015216 scopus 로고    scopus 로고
    • RAG3 gene and transcriptional regulation of the pyruvate decarboxylase gene in Kluyveromyces lactis
    • Prior C., Tizzani L., Fukuhara H., Wesolowski-Louvel M. RAG3 gene and transcriptional regulation of the pyruvate decarboxylase gene in Kluyveromyces lactis. Mol. Microbiol. 20:1996;765-772.
    • (1996) Mol. Microbiol. , vol.20 , pp. 765-772
    • Prior, C.1    Tizzani, L.2    Fukuhara, H.3    Wesolowski-Louvel, M.4
  • 110
    • 0032897230 scopus 로고    scopus 로고
    • Identification of a gene encoding the pyruvate decarboxylase gene regulator CaPdc2p from Candida albicans
    • Kaiser B., Munder T., Saluz H.P., Kunkel W., Eck R. Identification of a gene encoding the pyruvate decarboxylase gene regulator CaPdc2p from Candida albicans. Yeast. 15:1999;585-591.
    • (1999) Yeast , vol.15 , pp. 585-591
    • Kaiser, B.1    Munder, T.2    Saluz, H.P.3    Kunkel, W.4    Eck, R.5
  • 111
    • 0031985532 scopus 로고    scopus 로고
    • Cloning and characterization of two pyruvate decarboxylase genes from Pichia stipitis CBS 6054
    • Lu P., Davis B.P., Jeffries T.W. Cloning and characterization of two pyruvate decarboxylase genes from Pichia stipitis CBS 6054. Appl. Environ. Microbiol. 64:1998;94-97.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 94-97
    • Lu, P.1    Davis, B.P.2    Jeffries, T.W.3
  • 113
    • 0029134555 scopus 로고
    • ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose
    • van den Berg M.A., Steensma H.Y. ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose. Eur. J. Biochem. 231:1995;704-713.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 704-713
    • Van Den Berg, M.A.1    Steensma, H.Y.2
  • 114
    • 0030784854 scopus 로고    scopus 로고
    • The ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic, Mg(2+)-activated acetaldehyde dehydrogenase
    • Meaden P.G., Dickinson F.M., Mifsud A., Tessier W., Westwater J., Bussey H., Midgley M. The ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic, Mg(2+)-activated acetaldehyde dehydrogenase. Yeast. 13:1997;1319-1327.
    • (1997) Yeast , vol.13 , pp. 1319-1327
    • Meaden, P.G.1    Dickinson, F.M.2    Mifsud, A.3    Tessier, W.4    Westwater, J.5    Bussey, H.6    Midgley, M.7
  • 116
    • 0040884299 scopus 로고    scopus 로고
    • Metabolic defects of mislocalized mitochondrial and peroxisomal citrate synthases in the yeast Saccharomyces cerevisiae
    • Velot C., Lebreton S., Morgunov I., Usher K.C., Srere P.A. Metabolic defects of mislocalized mitochondrial and peroxisomal citrate synthases in the yeast Saccharomyces cerevisiae. Biochemistry. 38:1999;16195-16204.
    • (1999) Biochemistry , vol.38 , pp. 16195-16204
    • Velot, C.1    Lebreton, S.2    Morgunov, I.3    Usher, K.C.4    Srere, P.A.5
  • 117
    • 0030994770 scopus 로고    scopus 로고
    • The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase
    • Jia Y.K., Becam A.M., Herbert C.J. The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase. Mol. Microbiol. 24:1997;53-59.
    • (1997) Mol. Microbiol. , vol.24 , pp. 53-59
    • Jia, Y.K.1    Becam, A.M.2    Herbert, C.J.3
  • 118
    • 0030875237 scopus 로고    scopus 로고
    • Characterization of the intron-containing citrate synthase gene from the alkanotrophic yeast Candida tropicalis: Cloning and expression in Saccharomyces cerevisiae
    • Ueda M., Sanuki S., Kawachi H., Shimizu K., Atomi H., Tanaka A. Characterization of the intron-containing citrate synthase gene from the alkanotrophic yeast Candida tropicalis: cloning and expression in Saccharomyces cerevisiae. Arch. Microbiol. 168:1997;8-15.
    • (1997) Arch. Microbiol. , vol.168 , pp. 8-15
    • Ueda, M.1    Sanuki, S.2    Kawachi, H.3    Shimizu, K.4    Atomi, H.5    Tanaka, A.6
  • 119
    • 0025336743 scopus 로고
    • Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) and evidence of a synergistic regulation of expression by glucose plus glutamate
    • Gangloff S.P., Marguet D., Lauquin G.J. Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) and evidence of a synergistic regulation of expression by glucose plus glutamate. Mol. Cell. Biol. 10:1990;3551-3561.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3551-3561
    • Gangloff, S.P.1    Marguet, D.2    Lauquin, G.J.3
  • 120
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • Foury F. Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. FEBS Lett. 456:1999;281-284.
    • (1999) FEBS Lett. , vol.456 , pp. 281-284
    • Foury, F.1
  • 121
    • 0026784538 scopus 로고
    • +)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae
    • +)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae. J. Biol. Chem. 267:1992;16417-16423.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16417-16423
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 122
    • 0025841651 scopus 로고
    • +)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae
    • +)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae. J. Biol. Chem. 266:1991;22199-22205.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22199-22205
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 123
    • 0029977440 scopus 로고    scopus 로고
    • Expression and gene disruption analysis of the isocitrate dehydrogenase family in yeast
    • Zhao W.N., McAlister-Henn L. Expression and gene disruption analysis of the isocitrate dehydrogenase family in yeast. Biochemistry. 35:1996;7873-7878.
    • (1996) Biochemistry , vol.35 , pp. 7873-7878
    • Zhao, W.N.1    McAlister-Henn, L.2
  • 125
    • 0027382996 scopus 로고
    • Enzyme defects in glutamate-requiring stains of Schizosaccharomyces pombe
    • Barel I., MacDonald D.W. Enzyme defects in glutamate-requiring stains of Schizosaccharomyces pombe. FEMS Microbiol. Lett. 113:1993;267-272.
    • (1993) FEMS Microbiol. Lett. , vol.113 , pp. 267-272
    • Barel, I.1    MacDonald, D.W.2
  • 126
    • 0026015230 scopus 로고
    • DNA sequences in chromosomes II and VII code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: Analysis of pyruvate carboxylase-deficient strains
    • Stucka R., Dequin S., Salmon J.M., Gancedo C. DNA sequences in chromosomes II and VII code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: analysis of pyruvate carboxylase-deficient strains. Mol. Gen. Genet. 229:1991;307-315.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 307-315
    • Stucka, R.1    Dequin, S.2    Salmon, J.M.3    Gancedo, C.4
  • 128
    • 0024340089 scopus 로고
    • Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621
    • van Urk H., Schippe D., Breedveld G.J., Mak P.R., Scheffers W.A., van Dijken J.P. Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621. Biochim. Biophys. Acta. 992:1989;78-86.
    • (1989) Biochim. Biophys. Acta , vol.992 , pp. 78-86
    • Van Urk, H.1    Schippe, D.2    Breedveld, G.J.3    Mak, P.R.4    Scheffers, W.A.5    Van Dijken, J.P.6
  • 129
    • 0031779254 scopus 로고    scopus 로고
    • Isolation of the Pichia pastoris PYC1 gene encoding pyruvate carboxylase and identification of a suppressor of the pyc phenotype
    • Menéndez J., Delgado J., Gancedo C. Isolation of the Pichia pastoris PYC1 gene encoding pyruvate carboxylase and identification of a suppressor of the pyc phenotype. Yeast. 14:1998;647-654.
    • (1998) Yeast , vol.14 , pp. 647-654
    • Menéndez, J.1    Delgado, J.2    Gancedo, C.3
  • 131
  • 132
    • 0014559421 scopus 로고
    • Studies on the regulation and localization of the glyoxylate cycle enzymes in S. cerevisiae
    • Duntze W., Neumann D., Gancedo J.M., Atzpodien W., Holzer H. Studies on the regulation and localization of the glyoxylate cycle enzymes in S. cerevisiae. Eur. J. Biochem. 10:1968;83-89.
    • (1968) Eur. J. Biochem. , vol.10 , pp. 83-89
    • Duntze, W.1    Neumann, D.2    Gancedo, J.M.3    Atzpodien, W.4    Holzer, H.5
  • 133
    • 0025046371 scopus 로고
    • Association of glyoxylate and beta-oxidation enzymes with peroxisomes of Saccharomyces cerevisiae
    • McCammon M.T., Veenhuis M., Trapp S.B., Goodman J.M. Association of glyoxylate and beta-oxidation enzymes with peroxisomes of Saccharomyces cerevisiae. J. Bacteriol. 172:1990;5816-5827.
    • (1990) J. Bacteriol. , vol.172 , pp. 5816-5827
    • McCammon, M.T.1    Veenhuis, M.2    Trapp, S.B.3    Goodman, J.M.4
  • 134
    • 0025061158 scopus 로고
    • Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: Gene analysis and characterization
    • Atomi H., Ueda M., Hikida M., Hishida T., Teranishi Y., Tanaka A. Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization. J. Biochem. 107:1990;262-266.
    • (1990) J. Biochem. , vol.107 , pp. 262-266
    • Atomi, H.1    Ueda, M.2    Hikida, M.3    Hishida, T.4    Teranishi, Y.5    Tanaka, A.6
  • 135
    • 0027495624 scopus 로고
    • Cloning of the isocitrate lyase gene (ICL1) fromYarrowia lipolytica and characterization of the deduced protein
    • Barth G., Scheuber T. Cloning of the isocitrate lyase gene (ICL1) fromYarrowia lipolytica and characterization of the deduced protein. Mol. Gen. Genet. 241:1993;422-430.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 422-430
    • Barth, G.1    Scheuber, T.2
  • 136
    • 0029122796 scopus 로고
    • A novel promoter, derived from the isocitrate lyase gene of Candida tropicalis, inducible with acetate in Saccharomyces cerevisiae
    • Umemura K., Atomi H., Kanai T., Teranishi Y., Ueda M., Tanaka A. A novel promoter, derived from the isocitrate lyase gene of Candida tropicalis, inducible with acetate in Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 43:1995;489-492.
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 489-492
    • Umemura, K.1    Atomi, H.2    Kanai, T.3    Teranishi, Y.4    Ueda, M.5    Tanaka, A.6
  • 137
    • 0019301961 scopus 로고
    • Role and control of isocitrate lyase in Candida lipolytica
    • Matsuoka M., Ueda M., Aiba S. Role and control of isocitrate lyase in Candida lipolytica. J. Bacteriol. 144:1980;692-697.
    • (1980) J. Bacteriol. , vol.144 , pp. 692-697
    • Matsuoka, M.1    Ueda, M.2    Aiba, S.3
  • 138
    • 0022607777 scopus 로고
    • Purification of peroxisomal malate synthase from alkane-grown Candida tropicalis and some properties of the purified enzyme
    • Okada H., Ueda M., Tanaka A. Purification of peroxisomal malate synthase from alkane-grown Candida tropicalis and some properties of the purified enzyme. Arch. Microbiol. 144:1986;137-141.
    • (1986) Arch. Microbiol. , vol.144 , pp. 137-141
    • Okada, H.1    Ueda, M.2    Tanaka, A.3
  • 139
    • 0026348232 scopus 로고
    • Presence of two transcribed malate synthase genes in an n-alkane-utilizing yeast, Candida tropicalis
    • Hikida M., Atomi H., Fukuda Y., Aoki A., Hishida T., Teranishi Y., Ueda M., Tanaka A. Presence of two transcribed malate synthase genes in an n-alkane-utilizing yeast, Candida tropicalis. J. Biochem. 110:1991;909-914.
    • (1991) J. Biochem. , vol.110 , pp. 909-914
    • Hikida, M.1    Atomi, H.2    Fukuda, Y.3    Aoki, A.4    Hishida, T.5    Teranishi, Y.6    Ueda, M.7    Tanaka, A.8
  • 140
    • 0025425245 scopus 로고
    • Cloning and sequencing of the malate synthase gene from Hansenula polymorpha
    • Bruinenberg P.G., Blaauw M., Kazemier B., Ab G. Cloning and sequencing of the malate synthase gene from Hansenula polymorpha. Yeast. 6:1990;245-254.
    • (1990) Yeast , vol.6 , pp. 245-254
    • Bruinenberg, P.G.1    Blaauw, M.2    Kazemier, B.3    Ab, G.4
  • 141
    • 0026469802 scopus 로고
    • Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism of S. cerevisiae
    • Hartig A., Simon M.M., Schuster T., Daugherty J.R., Yoo H.S., Cooper T.G. Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism of S. cerevisiae. Nucleic Acids Res. 20:1992;5677-5686.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5677-5686
    • Hartig, A.1    Simon, M.M.2    Schuster, T.3    Daugherty, J.R.4    Yoo, H.S.5    Cooper, T.G.6
  • 142
    • 0016154761 scopus 로고
    • Regulatory and physicochemical properties of two isoenzymes of malate dehydrogenase from Schizosaccharomyces pombe
    • Flury U., Heer B., Fiechter A. Regulatory and physicochemical properties of two isoenzymes of malate dehydrogenase from Schizosaccharomyces pombe. Biochim. Biophys. Acta. 341:1974;465-483.
    • (1974) Biochim. Biophys. Acta , vol.341 , pp. 465-483
    • Flury, U.1    Heer, B.2    Fiechter, A.3
  • 143
    • 0021763550 scopus 로고
    • Catabolite repression in yeasts is not associated with low levels of cAMP
    • Eraso P., Gancedo J.M. Catabolite repression in yeasts is not associated with low levels of cAMP. Eur. J. Biochem. 141:1984;195-198.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 195-198
    • Eraso, P.1    Gancedo, J.M.2
  • 144
    • 0031878085 scopus 로고    scopus 로고
    • Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae
    • Small W.C., McAlister-Henn H. Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J. Bacteriol. 180:1998;4051-4055.
    • (1998) J. Bacteriol. , vol.180 , pp. 4051-4055
    • Small, W.C.1    McAlister-Henn, H.2
  • 145
    • 0032544505 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH
    • Luttik M.A.H., Overkamp K.M., Kötter P., de Vries S., van Dijken J.P., Pronk J.T. The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J. Biol. Chem. 273:1998;24259-24534.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24259-24534
    • Luttik, M.A.H.1    Overkamp, K.M.2    Kötter, P.3    De Vries, S.4    Van Dijken, J.P.5    Pronk, J.T.6
  • 146
    • 0032812743 scopus 로고    scopus 로고
    • A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica
    • Kerschner S.J., Okun J.G., Brandt U. A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica. J. Cell Sci. 112:1999;2347-2354.
    • (1999) J. Cell Sci. , vol.112 , pp. 2347-2354
    • Kerschner, S.J.1    Okun, J.G.2    Brandt, U.3
  • 147
    • 0026089901 scopus 로고
    • Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH-ubiquinone oxidoreductase of mitochondira from Saccharomyces cerevisiae
    • Marres C.A.M., de Vries S., Grivell L.A. Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH-ubiquinone oxidoreductase of mitochondira from Saccharomyces cerevisiae. Eur. J. Biochem. 195:1991;857-862.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 857-862
    • Marres, C.A.M.1    De Vries, S.2    Grivell, L.A.3
  • 148
    • 2642671097 scopus 로고    scopus 로고
    • The importance of the glycerol-3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae
    • Larsson C., Pahlman I.L., Ansell R., Rigoulet M., Adler L., Gustafsson L. The importance of the glycerol-3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae. Yeast. 14:1998;347-358.
    • (1998) Yeast , vol.14 , pp. 347-358
    • Larsson, C.1    Pahlman, I.L.2    Ansell, R.3    Rigoulet, M.4    Adler, L.5    Gustafsson, L.6
  • 149
    • 0023561970 scopus 로고
    • The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism
    • de Vries S., Marres C.A. The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim. Biophys. Acta. 895:1987;205-239.
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 205-239
    • De Vries, S.1    Marres, C.A.2
  • 150
    • 0028179124 scopus 로고
    • NADH:ubiquinone oxidoreductase in obligate aerobic yeasts
    • Buschges R., Bahrenberg G., Zimmermann M., Wolf K. NADH:ubiquinone oxidoreductase in obligate aerobic yeasts. Yeast. 10:1994;475-479.
    • (1994) Yeast , vol.10 , pp. 475-479
    • Buschges, R.1    Bahrenberg, G.2    Zimmermann, M.3    Wolf, K.4
  • 151
    • 0022633030 scopus 로고
    • Sequences required for delivery and localization of the ADP/ATP translocator to the mitochondrial inner membrane
    • Adrian G.S., McCammon M.T., Montgomery D.L., Douglas M.G. Sequences required for delivery and localization of the ADP/ATP translocator to the mitochondrial inner membrane. Mol. Cell. Biol. 6:1986;626-634.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 626-634
    • Adrian, G.S.1    McCammon, M.T.2    Montgomery, D.L.3    Douglas, M.G.4
  • 152
    • 0024288852 scopus 로고
    • Separate genes encode functionally equivalent carrier proteins in Saccharomyces cerevisiae
    • Lawson J.E., Douglas M.G. Separate genes encode functionally equivalent carrier proteins in Saccharomyces cerevisiae. J. Biol. Chem. 263:1988;14812-14818.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14812-14818
    • Lawson, J.E.1    Douglas, M.G.2
  • 153
    • 0025282180 scopus 로고
    • A third ADP/ATP translocator gene in yeast
    • Kolarov J., Kolarova N., Nelson N. A third ADP/ATP translocator gene in yeast. J. Biol. Chem. 265:1990;12711-12716.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12711-12716
    • Kolarov, J.1    Kolarova, N.2    Nelson, N.3
  • 154
    • 0026689334 scopus 로고
    • Yeast ADP/ATP carrier (AAC) proteins exhibit similar enzymatic properties but their deletion produces different phenotypes
    • Drgon T., Sabova L., Gavurnikova G., Kolarov J. Yeast ADP/ATP carrier (AAC) proteins exhibit similar enzymatic properties but their deletion produces different phenotypes. FEBS Lett. 304:1992;277-280.
    • (1992) FEBS Lett. , vol.304 , pp. 277-280
    • Drgon, T.1    Sabova, L.2    Gavurnikova, G.3    Kolarov, J.4
  • 155
    • 0028899628 scopus 로고
    • A Kluyveromyces lactis gene homologue to AAC2 complements the Saccharomyces cerevisiae op1 mutation
    • Viola A.M., Galeotti C.L., Goffrini P., Ficarelli A., Ferrero I. A Kluyveromyces lactis gene homologue to AAC2 complements the Saccharomyces cerevisiae op1 mutation. Curr. Genet. 27:1995;229-233.
    • (1995) Curr. Genet. , vol.27 , pp. 229-233
    • Viola, A.M.1    Galeotti, C.L.2    Goffrini, P.3    Ficarelli, A.4    Ferrero, I.5
  • 156
    • 0345425098 scopus 로고    scopus 로고
    • Isolation and expression of the gene encoding mitochondrial ADP/ATP carrier (AAC) from the pathogenic yeast Candida parapsilosis
    • Nebohacova M., Mentel M., Nosek J., Kolarov J. Isolation and expression of the gene encoding mitochondrial ADP/ATP carrier (AAC) from the pathogenic yeast Candida parapsilosis. Yeast. 15:1999;1237-1242.
    • (1999) Yeast , vol.15 , pp. 1237-1242
    • Nebohacova, M.1    Mentel, M.2    Nosek, J.3    Kolarov, J.4
  • 157
    • 0342936502 scopus 로고    scopus 로고
    • Cloning of the gene encoding the mitochondrial adenine nucleotide carrier of Schizosaccharomyces pombe by functional complementation in Saccharomyces cerevisiae
    • Couzin N., Trezeguet V., Le Saux A., Lauquin G.J. Cloning of the gene encoding the mitochondrial adenine nucleotide carrier of Schizosaccharomyces pombe by functional complementation in Saccharomyces cerevisiae. Gene. 171:1996;113-117.
    • (1996) Gene , vol.171 , pp. 113-117
    • Couzin, N.1    Trezeguet, V.2    Le Saux, A.3    Lauquin, G.J.4
  • 158
    • 0032867936 scopus 로고    scopus 로고
    • A Klaac null mutant of Kluyveromyces lactis is complemented by a single copy of the Saccharomyces cerevisiae AAC1 gene
    • Viola A.M., Lodi T., Ferrero I. A Klaac null mutant of Kluyveromyces lactis is complemented by a single copy of the Saccharomyces cerevisiae AAC1 gene. Curr. Genet. 36:1999;29-36.
    • (1999) Curr. Genet. , vol.36 , pp. 29-36
    • Viola, A.M.1    Lodi, T.2    Ferrero, I.3
  • 159
    • 18544398274 scopus 로고    scopus 로고
    • Expression of the ADP/ATP carrier encoding genes in aerobic yeasts; Phenotype of an ADP/ATP carrier deletion mutant of Schizosaccharomyces pombe
    • Trezeguet V., Zeman I., David C., Lauquin G.J., Kolarov J. Expression of the ADP/ATP carrier encoding genes in aerobic yeasts; phenotype of an ADP/ATP carrier deletion mutant of Schizosaccharomyces pombe. Biochim. Biophys. Acta. 1410:1999;229-236.
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 229-236
    • Trezeguet, V.1    Zeman, I.2    David, C.3    Lauquin, G.J.4    Kolarov, J.5
  • 161
    • 0014984252 scopus 로고
    • Specific inhibition of the cyanide-insensitive respiratory pathway in plant mitochondria by hydroxamic acids
    • Schonbaum G.R., Bonner W.D., Storey B.T., Bahr J.T. Specific inhibition of the cyanide-insensitive respiratory pathway in plant mitochondria by hydroxamic acids. Plant. Physiol. 47:1971;124-128.
    • (1971) Plant. Physiol. , vol.47 , pp. 124-128
    • Schonbaum, G.R.1    Bonner, W.D.2    Storey, B.T.3    Bahr, J.T.4
  • 162
    • 0016431422 scopus 로고
    • Cyanide insensitive respiration. An alternative mitochondrial pathway
    • Henry M.F., Nyns E.J. Cyanide insensitive respiration. An alternative mitochondrial pathway. Sub-Cell. Biochem. 4:1975;1-65.
    • (1975) Sub-Cell. Biochem. , vol.4 , pp. 1-65
    • Henry, M.F.1    Nyns, E.J.2
  • 164
    • 0019856574 scopus 로고
    • The respiration pathways of wild-type and petite mutants of Kluyveromyces lactis
    • Heritage J., Tribe M.A., Whittaker P.A. The respiration pathways of wild-type and petite mutants of Kluyveromyces lactis. Microbios. 30:1981;37-45.
    • (1981) Microbios , vol.30 , pp. 37-45
    • Heritage, J.1    Tribe, M.A.2    Whittaker, P.A.3
  • 165
    • 0025355108 scopus 로고
    • A 36 kDa mitochondrial protein is responsible for cyanide resistant respiration in Hansenula anomala
    • Minagawa N., Sakajo S., Komiyama T., Yoshimoto A. A 36 kDa mitochondrial protein is responsible for cyanide resistant respiration in Hansenula anomala. FEBS Lett. 264:1990;149-152.
    • (1990) FEBS Lett. , vol.264 , pp. 149-152
    • Minagawa, N.1    Sakajo, S.2    Komiyama, T.3    Yoshimoto, A.4
  • 166
    • 0001589213 scopus 로고
    • Sulfur compounds induce alternative oxidation in Hansenula anomala
    • Minagawa N., Sakajo S., Yoshimoto A. Sulfur compounds induce alternative oxidation in Hansenula anomala. Agric. Biol. Chem. 61:1991;1573-1574.
    • (1991) Agric. Biol. Chem. , vol.61 , pp. 1573-1574
    • Minagawa, N.1    Sakajo, S.2    Yoshimoto, A.3
  • 167
    • 0025880440 scopus 로고
    • Molecular cloning of cDNA from antimycinA-inducible mRNA and its role in cyanide-resistant respiration in Hansenula anomala
    • Sakajo S., Minagawa N., Komiyama T., Yoshimoto A. Molecular cloning of cDNA from antimycinA-inducible mRNA and its role in cyanide-resistant respiration in Hansenula anomala. Biochim. Biophys. Acta. 1090:1991;102-108.
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 102-108
    • Sakajo, S.1    Minagawa, N.2    Komiyama, T.3    Yoshimoto, A.4
  • 168
    • 0032988014 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of alternative oxidase in Candida albicans
    • Huh W.K., Kang S.O. Molecular cloning and functional expression of alternative oxidase in Candida albicans. J. Bacteriol. 181:1999;4098-4102.
    • (1999) J. Bacteriol. , vol.181 , pp. 4098-4102
    • Huh, W.K.1    Kang, S.O.2
  • 170
    • 0033173845 scopus 로고    scopus 로고
    • Development and activation of cyanide-resistant respiration in the yeast Yarrowia lipolytica
    • Medentsev A.G., Akimenko V.K. Development and activation of cyanide-resistant respiration in the yeast Yarrowia lipolytica. Biochemistry (Moscow). 64:1999;945-951.
    • (1999) Biochemistry (Moscow) , vol.64 , pp. 945-951
    • Medentsev, A.G.1    Akimenko, V.K.2
  • 171
    • 0029041836 scopus 로고
    • Existence of cyanide insensitive respiration in the yeast Pichia stipitis and its possible influence on product formation during xylose utilization
    • Jeppsson H., Alexander N.J., Hahn-Hagerdal B.C. Existence of cyanide insensitive respiration in the yeast Pichia stipitis and its possible influence on product formation during xylose utilization. Appl. Env. Microb. 61:1995;2596-2600.
    • (1995) Appl. Env. Microb. , vol.61 , pp. 2596-2600
    • Jeppsson, H.1    Alexander, N.J.2    Hahn-Hagerdal, B.C.3
  • 172
    • 0030055355 scopus 로고    scopus 로고
    • Targeting the plant alternative oxidase protein to Schizosaccharomyces pombe mitochondria confers cyanide-insensitive respiration
    • Albury M.S., Dudley P., Watts F.Z., Moore A.L. Targeting the plant alternative oxidase protein to Schizosaccharomyces pombe mitochondria confers cyanide-insensitive respiration. J. Biol. Chem. 271:1996;17062-17066.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17062-17066
    • Albury, M.S.1    Dudley, P.2    Watts, F.Z.3    Moore, A.L.4
  • 173
    • 0033525704 scopus 로고    scopus 로고
    • Functional expression of the plant alternative oxidase affects growth of the yeast Schizosaccharomyces pombe
    • Affourtit C., Albury M.S., Krab K., Moore A.L. Functional expression of the plant alternative oxidase affects growth of the yeast Schizosaccharomyces pombe. J. Biol. Chem. 274:1999;6212-6218.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6212-6218
    • Affourtit, C.1    Albury, M.S.2    Krab, K.3    Moore, A.L.4
  • 174
    • 0001335898 scopus 로고
    • Contribution of the pentose phosphate pathway to glucose metabolism in Saccharomyces cerevisiae: A critical analysis on the use of labelled glucose
    • Gancedo J.M., Lagunas R. Contribution of the pentose phosphate pathway to glucose metabolism in Saccharomyces cerevisiae: a critical analysis on the use of labelled glucose. Plant. Sci. Lett. 1:1973;193-200.
    • (1973) Plant. Sci. Lett. , vol.1 , pp. 193-200
    • Gancedo, J.M.1    Lagunas, R.2
  • 175
    • 0020626034 scopus 로고
    • An enzymic analysis of NADPH production and consumption in Candida utilis
    • Bruinenberg P.M., van Dijken J.P., Scheffers W.A. An enzymic analysis of NADPH production and consumption in Candida utilis. J. Gen. Microbiol. 129:1983;965-971.
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 965-971
    • Bruinenberg, P.M.1    Van Dijken, J.P.2    Scheffers, W.A.3
  • 176
    • 0032458781 scopus 로고    scopus 로고
    • Purification and kinetic characterizaton of hexokinase and glucose-6-phosphate dehydrogenase from Schizosaccharomyces pombe
    • Tsai C.S., Chen Q. Purification and kinetic characterizaton of hexokinase
    • (1998) Biochem. Cell. Biol. , vol.76 , pp. 107-113
    • Tsai, C.S.1    Chen, Q.2
  • 177
    • 0016420647 scopus 로고
    • Glucose-6-phosphate dehydrogenase from Candida utilis
    • Domagk G.F., Chilla R. Glucose-6-phosphate dehydrogenase from Candida utilis. Methods Enzymol. 41:1975;205-208.
    • (1975) Methods Enzymol. , vol.41 , pp. 205-208
    • Domagk, G.F.1    Chilla, R.2
  • 178
    • 0027497702 scopus 로고
    • Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure
    • Jeffery J., Persson B., Wood I., Bergman T., Jeffery R., Jornvall H. Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure. Eur. J. Biochem. 212:1993;41-49.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 41-49
    • Jeffery, J.1    Persson, B.2    Wood, I.3    Bergman, T.4    Jeffery, R.5    Jornvall, H.6
  • 179
    • 0026096914 scopus 로고
    • Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur
    • Thomas D., Cherest H., Surdin-Kerjan Y. Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur. EMBO J. 10:1991;547-553.
    • (1991) EMBO J. , vol.10 , pp. 547-553
    • Thomas, D.1    Cherest, H.2    Surdin-Kerjan, Y.3
  • 180
    • 0000923421 scopus 로고
    • Identification of a gluconolactonase
    • Brodie A.F., Lipmann F. Identification of a gluconolactonase. J. Biol. Chem. 212:1955;677-685.
    • (1955) J. Biol. Chem. , vol.212 , pp. 677-685
    • Brodie, A.F.1    Lipmann, F.2
  • 181
    • 0027062698 scopus 로고
    • Isolation and characterization of the gene encoding gluconolactonase from Zymomonas mobilis
    • Kanagasundaram V., Scopes R. Isolation and characterization of the gene encoding gluconolactonase from Zymomonas mobilis. Biochim. Biophys. Acta. 1171:1992;198-200.
    • (1992) Biochim. Biophys. Acta , vol.1171 , pp. 198-200
    • Kanagasundaram, V.1    Scopes, R.2
  • 182
    • 0032573079 scopus 로고    scopus 로고
    • Lactone-ring-cleaving enzyme: Genetic analysis, novel RNA editing, and evolutionary implications
    • Kobayashi M., Shinohara M., Sakoh C., Kataoka M., Shimizu S. Lactone-ring-cleaving enzyme: genetic analysis, novel RNA editing, and evolutionary implications. Proc. Natl. Acad. Sci. USA. 95:1998;12787-12792.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12787-12792
    • Kobayashi, M.1    Shinohara, M.2    Sakoh, C.3    Kataoka, M.4    Shimizu, S.5
  • 183
    • 0028809157 scopus 로고
    • Kinetic studies of gluconate pathway enzymes from Schizosaccharomyces pombe
    • Tsai C.S., Shi J.L., Ye H.G. Kinetic studies of gluconate pathway enzymes from Schizosaccharomyces pombe. Arch. Biochem. Biophys. 316:1995;163-168.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 163-168
    • Tsai, C.S.1    Shi, J.L.2    Ye, H.G.3
  • 184
    • 0032468799 scopus 로고    scopus 로고
    • Purification and kinetic characterization of 6-phosphogluconate dehydrogenase from Schizosaccharomyces pombe
    • Tsai C.S., Chen Q. Purification and kinetic characterization of 6-phosphogluconate dehydrogenase from Schizosaccharomyces pombe. Biochem. Cell. Biol. 76:1998;637-644.
    • (1998) Biochem. Cell. Biol. , vol.76 , pp. 637-644
    • Tsai, C.S.1    Chen, Q.2
  • 185
    • 0016415481 scopus 로고
    • 6-Phosphogluconate dehydrogenase from Candida utilis
    • Rippa M., Signorini M. 6-Phosphogluconate dehydrogenase from Candida utilis. Methods Enzymol. 41:1975;237-240.
    • (1975) Methods Enzymol. , vol.41 , pp. 237-240
    • Rippa, M.1    Signorini, M.2
  • 186
    • 0020069233 scopus 로고
    • Pentose phosphate pathway mutants of yeast
    • Lobo Z., Maitra P.K. Pentose phosphate pathway mutants of yeast. Mol. Gen. Genet. 185:1982;367-368.
    • (1982) Mol. Gen. Genet. , vol.185 , pp. 367-368
    • Lobo, Z.1    Maitra, P.K.2
  • 187
    • 0016422117 scopus 로고
    • D-Ribose-5-phosphate isomerase from Candida utilis
    • Domagk G.F., Doering K.M. D-Ribose-5-phosphate isomerase from Candida utilis. Methods Enzymol. 41:1975;427-429.
    • (1975) Methods Enzymol. , vol.41 , pp. 427-429
    • Domagk, G.F.1    Doering, K.M.2
  • 188
    • 0017145042 scopus 로고
    • Purification, properties and structure of ribose-5-phosphate ketol isomerase from Candida utilis
    • Horitsu H., Sasaki I., Kikuchi T., Suzuki H., Sumida M., Tomoyeda M. Purification, properties and structure of ribose-5-phosphate ketol isomerase from Candida utilis. Agric. Biol. Chem. 40:1976;257-264.
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 257-264
    • Horitsu, H.1    Sasaki, I.2    Kikuchi, T.3    Suzuki, H.4    Sumida, M.5    Tomoyeda, M.6
  • 189
    • 0019881194 scopus 로고
    • The preparation of transketolase free from D-ribulose-5-phosphate-3-epimerase
    • Wood T. The preparation of transketolase free from D-ribulose-5-phosphate-3-epimerase. Biochim. Biophys. Acta. 659:1981;233-243.
    • (1981) Biochim. Biophys. Acta , vol.659 , pp. 233-243
    • Wood, T.1
  • 190
    • 0031039891 scopus 로고    scopus 로고
    • Analysis of a transketolase gene from Kluyveromyces lactis reveals that the yeast enzymes are more related to transketolases of prokaryotic origins than to those of higher eukaryotes
    • Jakoby J.J., Heinisch J.J. Analysis of a transketolase gene from Kluyveromyces lactis reveals that the yeast enzymes are more related to transketolases of prokaryotic origins than to those of higher eukaryotes. Curr. Genet. 31:1997;15-21.
    • (1997) Curr. Genet. , vol.31 , pp. 15-21
    • Jakoby, J.J.1    Heinisch, J.J.2
  • 191
    • 0028029844 scopus 로고
    • Isolation and characterization of the Pichia stipitis transketolase gene and expression in a xylose-utilising Saccharomyces cerevisiae transformant
    • Metzger M.H., Hollenberg C.P. Isolation and characterization of the Pichia stipitis transketolase gene and expression in a xylose-utilising Saccharomyces cerevisiae transformant. Appl. Microbiol. Biotechnol. 42:1994;319-325.
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 319-325
    • Metzger, M.H.1    Hollenberg, C.P.2
  • 194
    • 0342514615 scopus 로고    scopus 로고
    • D-Xylose metabolism by Candida intermedia: Isolation and characterisation of two forms of aldose reductase with different coenzyme specificities
    • Mayr P., Bruggler K., Kulbe K.D., Nidetzky B. D-Xylose metabolism by Candida intermedia: isolation and characterisation of two forms of aldose reductase with different coenzyme specificities. J. Chromatogr. B Biomed. Sci. Appl. 14:2000;195-202.
    • (2000) J. Chromatogr. B Biomed. Sci. Appl. , vol.14 , pp. 195-202
    • Mayr, P.1    Bruggler, K.2    Kulbe, K.D.3    Nidetzky, B.4
  • 195
    • 0029160251 scopus 로고
    • Isolation and characterization of the gene encoding xylose reductase from Kluyveromyces lactis
    • Billard P., Menart S., Fleer R., Bolotin-Fukuhara M. Isolation and characterization of the gene encoding xylose reductase from Kluyveromyces lactis. Gene. 162:1995;93-97.
    • (1995) Gene , vol.162 , pp. 93-97
    • Billard, P.1    Menart, S.2    Fleer, R.3    Bolotin-Fukuhara, M.4
  • 196
    • 0027395082 scopus 로고
    • Xylose fermentation by Saccharomyces cerevisiae
    • Kötter P., Ciriacy M. Xylose fermentation by Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 38:1993;776-783.
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 776-783
    • Kötter, P.1    Ciriacy, M.2
  • 197
    • 0032945807 scopus 로고    scopus 로고
    • Xylitol production using recombinant Saccharomyces cerevisiae containing multiple xylose reductase genes at chromosomal delta-sequences
    • Kim Y.S., Kim S.Y., Kim J.H., Kim S.C. Xylitol production using recombinant Saccharomyces cerevisiae containing multiple xylose reductase genes at chromosomal delta-sequences. J. Biotechnol. 67:1999;159-171.
    • (1999) J. Biotechnol. , vol.67 , pp. 159-171
    • Kim, Y.S.1    Kim, S.Y.2    Kim, J.H.3    Kim, S.C.4
  • 198
    • 0025139414 scopus 로고
    • Purification, characterization, and amino terminal sequence of xylose reductase from Candida shehatae
    • Ho N.W., Lin F.P., Huang S., Andrews P.C., Tsao G.T. Purification, characterization, and amino terminal sequence of xylose reductase from Candida shehatae. Enzyme Microb. Technol. 12:1990;33-39.
    • (1990) Enzyme Microb. Technol. , vol.12 , pp. 33-39
    • Ho, N.W.1    Lin, F.P.2    Huang, S.3    Andrews, P.C.4    Tsao, G.T.5
  • 199
    • 0030881429 scopus 로고    scopus 로고
    • NAD(P)H-dependent aldolase reductase from the xylose assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme
    • Neuhauser W., Haltrich D., Kulbe K.D., Nidetzky B. NAD(P)H-dependent aldolase reductase from the xylose assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. Biochem. J. 326:1997;683-692.
    • (1997) Biochem. J. , vol.326 , pp. 683-692
    • Neuhauser, W.1    Haltrich, D.2    Kulbe, K.D.3    Nidetzky, B.4
  • 200
    • 0031892213 scopus 로고    scopus 로고
    • Cloning and expression of Candida guilliermondii xylose reductase gene (xyl1) in Pichia pastoris
    • Handumrongkul C., Ma D.P., Silva J.L. Cloning and expression of Candida guilliermondii xylose reductase gene (xyl1) in Pichia pastoris. Appl. Microbiol. Biotechnol. 49:1998;399-404.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 399-404
    • Handumrongkul, C.1    Ma, D.P.2    Silva, J.L.3
  • 201
    • 17544401301 scopus 로고    scopus 로고
    • Isolation and characterization of the MIG1 gene from Candida albicans and effect of its disruption on catabolite repression
    • Zaragoza O., Rodríguez C., Gancedo C. Isolation and characterization of the MIG1 gene from Candida albicans and effect of its disruption on catabolite repression. J. Bacteriol. 182:2000;320-326.
    • (2000) J. Bacteriol. , vol.182 , pp. 320-326
    • Zaragoza, O.1    Rodríguez, C.2    Gancedo, C.3
  • 202
    • 0032769768 scopus 로고    scopus 로고
    • Evidence that the gene YLR070c of Saccharomyces cerevisiae encodes a xylitol dehydrogenase
    • Richard P., Toivari M.H., Penttila M. Evidence that the gene YLR070c of Saccharomyces cerevisiae encodes a xylitol dehydrogenase. FEBS Lett. 457:1999;135-138.
    • (1999) FEBS Lett. , vol.457 , pp. 135-138
    • Richard, P.1    Toivari, M.H.2    Penttila, M.3
  • 203
    • 0030772483 scopus 로고    scopus 로고
    • Expression of different levels of enzymes from the Pichia stipitis XYL1 and XYL2 genes in Saccharomyces cerevisiae and its effects on product formation during xylose utilisation
    • Waldfrisson M., Anderlund M., Bao X., Hahn-Hägerdal B. Expression of different levels of enzymes from the Pichia stipitis XYL1 and XYL2 genes in Saccharomyces cerevisiae and its effects on product formation during xylose utilisation. Appl. Microbiol. Technol. 48:1997;218-224.
    • (1997) Appl. Microbiol. Technol. , vol.48 , pp. 218-224
    • Waldfrisson, M.1    Anderlund, M.2    Bao, X.3    Hahn-Hägerdal, B.4
  • 204
    • 0020697117 scopus 로고
    • MRNA levels for the fermentative alcohol dehydrogenase of Saccharomyces cerevisiae decrease upon growth on a nonfermentable carbon source
    • Denis C.L., Ferguson J., Young E.T. mRNA levels for the fermentative alcohol dehydrogenase of Saccharomyces cerevisiae decrease upon growth on a nonfermentable carbon source. J. Biol. Chem. 258:1983;1165-1171.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1165-1171
    • Denis, C.L.1    Ferguson, J.2    Young, E.T.3
  • 206
    • 0014105807 scopus 로고
    • Mutants partially deficient in alcohol dehydrogenase in Schizosaccharomyces pombe
    • Megnet R. Mutants partially deficient in alcohol dehydrogenase in Schizosaccharomyces pombe. Arch. Biochem. Biophys. 121:1967;194-201.
    • (1967) Arch. Biochem. Biophys. , vol.121 , pp. 194-201
    • Megnet, R.1
  • 207
    • 0020663608 scopus 로고
    • The primary structure of the alcohol dehydrogenase gene from the fission yeast Schizosaccharomyces pombe
    • Russell P., Hall B.D. The primary structure of the alcohol dehydrogenase gene from the fission yeast Schizosaccharomyces pombe. J. Biol. Chem. 258:1983;143-149.
    • (1983) J. Biol. Chem. , vol.258 , pp. 143-149
    • Russell, P.1    Hall, B.D.2
  • 208
    • 0030987011 scopus 로고    scopus 로고
    • Structural and biochemical studies of alcohol dehydrogenase isozymes from Kluyveromyces lactis
    • Bozzi A., Saliola M., Falcone C., Bossa F., Martini F. Structural and biochemical studies of alcohol dehydrogenase isozymes from Kluyveromyces lactis. Biochim. Biophys. Acta. 1339:1997;133-142.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 133-142
    • Bozzi, A.1    Saliola, M.2    Falcone, C.3    Bossa, F.4    Martini, F.5
  • 209
    • 0026648824 scopus 로고
    • Ethanol-induced and glucose-insensitive alcohol dehydrogenase activity in the yeast Kluyveromyces lactis
    • Mazzoni C., Saliola M., Falcone C. Ethanol-induced and glucose-insensitive alcohol dehydrogenase activity in the yeast Kluyveromyces lactis. Mol. Microbiol. 6:1992;2279-2286.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2279-2286
    • Mazzoni, C.1    Saliola, M.2    Falcone, C.3
  • 210
    • 0029584856 scopus 로고
    • Two mitochondrial alcohol dehydrogenase activities of Kluyveromyces lactis are differently expressed during respiration and fermentation
    • Saliola M., Falcone C. Two mitochondrial alcohol dehydrogenase activities of Kluyveromyces lactis are differently expressed during respiration and fermentation. Mol. Gen. Genet. 249:1995;665-672.
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 665-672
    • Saliola, M.1    Falcone, C.2
  • 211
    • 0030025373 scopus 로고    scopus 로고
    • Structure and regulation of the Candida albicans ADH1 gene encoding an immunogenic alcohol dehydrogenase
    • Bertram G., Swoboda R.K., Gooday G.W., Gow N.A., Brown A.J. Structure and regulation of the Candida albicans ADH1 gene encoding an immunogenic alcohol dehydrogenase. Yeast. 12:1996;115-127.
    • (1996) Yeast , vol.12 , pp. 115-127
    • Bertram, G.1    Swoboda, R.K.2    Gooday, G.W.3    Gow, N.A.4    Brown, A.J.5
  • 212
    • 0031968382 scopus 로고    scopus 로고
    • Pichia stipitis genes for alcohol dehydrogenase with fermentative and respiratory functions
    • Cho J.Y., Jeffries T.W. Pichia stipitis genes for alcohol dehydrogenase with fermentative and respiratory functions. Appl. Environ. Microbiol. 64:1998;1350-1358.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1350-1358
    • Cho, J.Y.1    Jeffries, T.W.2
  • 213
    • 0031690601 scopus 로고    scopus 로고
    • Molecular cloning of alcohol dehydrogenase genes of the yeast Pichia stipitis and identification of the fermentative ADH
    • Passoth V., Schafer B., Liebel B., Weierstall T., Klinner U. Molecular cloning of alcohol dehydrogenase genes of the yeast Pichia stipitis and identification of the fermentative ADH. Yeast. 14:1998;1311-1325.
    • (1998) Yeast , vol.14 , pp. 1311-1325
    • Passoth, V.1    Schafer, B.2    Liebel, B.3    Weierstall, T.4    Klinner, U.5
  • 214
    • 0018734895 scopus 로고
    • +-dependent alcohol dehydrogenases in Saccharomycopsis lipolytica
    • +-dependent alcohol dehydrogenases in Saccharomycopsis lipolytica. Z. Allg. Mikrobiol. 19:1979;381-390.
    • (1979) Z. Allg. Mikrobiol. , vol.19 , pp. 381-390
    • Barth, G.1    Kunkel, W.2
  • 215
    • 0032784969 scopus 로고    scopus 로고
    • A proposal for nomenclature of aldehyde deydrogenases in Saccharomyces cerevisiae and characterization of the stress-inducible ALD2 and ALD3 genes
    • Navarro-Aviño J.P., Prasad R., Miralles V.J., Benito R.M., Serrano R. A proposal for nomenclature of aldehyde deydrogenases in Saccharomyces cerevisiae and characterization of the stress-inducible ALD2 and ALD3 genes. Yeast. 15:1999;829-842.
    • (1999) Yeast , vol.15 , pp. 829-842
    • Navarro-Aviño, J.P.1    Prasad, R.2    Miralles, V.J.3    Benito, R.M.4    Serrano, R.5
  • 217
    • 0027062806 scopus 로고
    • Cloning and disruption of a gene required for growth on acetate but not on ethanol: The acetyl-coenzyme A synthetase gene of Saccharomyces cerevisiae
    • De Virgilio C., Bürckert N., Barth G., Neuhaus J.M., Boller T., Wiemken A. Cloning and disruption of a gene required for growth on acetate but not on ethanol: the acetyl-coenzyme A synthetase gene of Saccharomyces cerevisiae. Yeast. 8:1992;1043-1051.
    • (1992) Yeast , vol.8 , pp. 1043-1051
    • De Virgilio, C.1    Bürckert, N.2    Barth, G.3    Neuhaus, J.M.4    Boller, T.5    Wiemken, A.6
  • 218
    • 0029802611 scopus 로고    scopus 로고
    • The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation
    • van den Berg M.A., de Jong-Gubbels P., Kortland C.J., van Dijken J.P., Pronk J.T., Steensma H.Y. The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation. J. Biol. Chem. 271:1996;28953-28959.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28953-28959
    • Van Den Berg, M.A.1    De Jong-Gubbels, P.2    Kortland, C.J.3    Van Dijken, J.P.4    Pronk, J.T.5    Steensma, H.Y.6
  • 219
    • 0026534662 scopus 로고
    • Characterization of mutants of the yeast Yarrowia lipolytica defective in acetyl-coenzyme A synthetase
    • Kujau M., Weber H., Barth G. Characterization of mutants of the yeast Yarrowia lipolytica defective in acetyl-coenzyme A synthetase. Yeast. 8:1992;193-203.
    • (1992) Yeast , vol.8 , pp. 193-203
    • Kujau, M.1    Weber, H.2    Barth, G.3
  • 220
    • 0024442219 scopus 로고
    • Acetate assimilation by the fission yeast Schizosaccharomyces pombe
    • Tsai C.S., Mitton K.P., Johnson B.F. Acetate assimilation by the fission yeast Schizosaccharomyces pombe. Biochem. Cell. Biol. 67:1989;464-467.
    • (1989) Biochem. Cell. Biol. , vol.67 , pp. 464-467
    • Tsai, C.S.1    Mitton, K.P.2    Johnson, B.F.3
  • 221
    • 0025194333 scopus 로고
    • Ethanol formation in adh0 mutants reveals the existence of a novel acetaldehyde-reducing activity in Saccharomyces cerevisiae
    • Drewke C., Thielen J., Ciriacy M. Ethanol formation in adh0 mutants reveals the existence of a novel acetaldehyde-reducing activity in Saccharomyces cerevisiae. J. Bacteriol. 172:1990;3909-3917.
    • (1990) J. Bacteriol. , vol.172 , pp. 3909-3917
    • Drewke, C.1    Thielen, J.2    Ciriacy, M.3
  • 222
    • 0027992610 scopus 로고
    • Glucose metabolism and ethanol production in adh multiple and null mutants of Kluyveromyces lactis
    • Saliola M., Bellardi S., Marta I., Falcone C. Glucose metabolism and ethanol production in adh multiple and null mutants of Kluyveromyces lactis. Yeast. 10:1994;1133-1140.
    • (1994) Yeast , vol.10 , pp. 1133-1140
    • Saliola, M.1    Bellardi, S.2    Marta, I.3    Falcone, C.4
  • 223
    • 0030908893 scopus 로고    scopus 로고
    • The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation
    • Ansell R., Granath K., Hohmann S., Thevelein J.M., Adler L. The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation. EMBO J. 16:1997;2179-2187.
    • (1997) EMBO J. , vol.16 , pp. 2179-2187
    • Ansell, R.1    Granath, K.2    Hohmann, S.3    Thevelein, J.M.4    Adler, L.5
  • 224
    • 0029583970 scopus 로고
    • Osmoregulation of fission yeast: Cloning of two distinct genes encoding glycerol-3-phosphate dehydrogenase, one of which is responsible for osmotolerance for growth
    • Ohmiya R., Yamada H., Nakashima K., Aiba H., Mizuno T. Osmoregulation of fission yeast: cloning of two distinct genes encoding glycerol-3-phosphate dehydrogenase, one of which is responsible for osmotolerance for growth. Mol. Microbiol. 18:1995;963-973.
    • (1995) Mol. Microbiol. , vol.18 , pp. 963-973
    • Ohmiya, R.1    Yamada, H.2    Nakashima, K.3    Aiba, H.4    Mizuno, T.5
  • 225
    • 0030150653 scopus 로고    scopus 로고
    • Construction and characterization of a deletion mutant of gpd2 that encodes an isozyme of NADH-dependent glycerol-3-phosphate dehydrogenase in fission yeast
    • Yamada H., Ohmiya R., Aiba H., Mizuno T. Construction and characterization of a deletion mutant of gpd2 that encodes an isozyme of NADH-dependent glycerol-3-phosphate dehydrogenase in fission yeast. Biosci. Biotechnol. Biochem. 60:1996;918-920.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 918-920
    • Yamada, H.1    Ohmiya, R.2    Aiba, H.3    Mizuno, T.4
  • 226
    • 0029920291 scopus 로고    scopus 로고
    • Purification and characterization of two isoenzymes of DL-glycerol-3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of Gpp2p expression by the osmosensing mitogen-activated protein kinase signal transduction pathway
    • Norbeck J., Pahlman A.K., Akhtar N., Blomberg A., Adler L. Purification and characterization of two isoenzymes of DL-glycerol-3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of Gpp2p expression by the osmosensing mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 271:1996;13875-13881.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13875-13881
    • Norbeck, J.1    Pahlman, A.K.2    Akhtar, N.3    Blomberg, A.4    Adler, L.5
  • 227
    • 0014305533 scopus 로고
    • Glycerol metabolism in yeasts. Pathways of utilization and production
    • Gancedo C., Gancedo J.M., Sols A. Glycerol metabolism in yeasts. Pathways of utilization and production. Eur. J. Biochem. 5:1968;165-172.
    • (1968) Eur. J. Biochem. , vol.5 , pp. 165-172
    • Gancedo, C.1    Gancedo, J.M.2    Sols, A.3
  • 228
    • 0017381201 scopus 로고
    • Isolation and characterization of Saccharomyces cerevisiae mutants defective in glycerol catabolism
    • Sprague G.F., Cronan J.E. Isolation and characterization of Saccharomyces cerevisiae mutants defective in glycerol catabolism. J. Bacteriol. 129:1977;1335-1342.
    • (1977) J. Bacteriol. , vol.129 , pp. 1335-1342
    • Sprague, G.F.1    Cronan, J.E.2
  • 229
    • 0019926193 scopus 로고
    • Glycerol utilization by Schizosaccharomyces pombe: Phosphorylation of dihidroxyacetone by a specific kinase as the second step
    • May J.W., Marshall J.H., Sloan J. Glycerol utilization by Schizosaccharomyces pombe: phosphorylation of dihidroxyacetone by a specific kinase as the second step. J. Gen. Microbiol. 128:1982;1763-1766.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 1763-1766
    • May, J.W.1    Marshall, J.H.2    Sloan, J.3
  • 230
    • 0023050095 scopus 로고
    • Isolation and characterization of mutants from Schizosaccharomyces pombe defective in glycerol catabolism
    • Gancedo C., Llobell A., Ribas J.C., Luchi F. Isolation and characterization of mutants from Schizosaccharomyces pombe defective in glycerol catabolism. Eur. J. Biochem. 159:1986;171-174.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 171-174
    • Gancedo, C.1    Llobell, A.2    Ribas, J.C.3    Luchi, F.4
  • 231
    • 0031041461 scopus 로고    scopus 로고
    • Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway
    • Norbeck J., Blomberg A. Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway. J. Biol. Chem. 272:1997;5544-5554.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5544-5554
    • Norbeck, J.1    Blomberg, A.2
  • 232
    • 0028947362 scopus 로고
    • Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress
    • Luyten K., Albertyn J., Skibbe W.F., Prior B.A., Ramos J., Thevelein J.M., Hohmann S. Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress. EMBO J. 14:1995;1360-1371.
    • (1995) EMBO J. , vol.14 , pp. 1360-1371
    • Luyten, K.1    Albertyn, J.2    Skibbe, W.F.3    Prior, B.A.4    Ramos, J.5    Thevelein, J.M.6    Hohmann, S.7
  • 234
    • 0028835866 scopus 로고
    • + symport in the halotolerant yeast Pichia sorbitophila
    • + symport in the halotolerant yeast Pichia sorbitophila. Yeast. 11:1995;111-119.
    • (1995) Yeast , vol.11 , pp. 111-119
    • Lages, F.1    Lucas, C.2
  • 235
    • 0032884517 scopus 로고    scopus 로고
    • Active glycerol uptake is a mechanism underlying halotolerance in yeasts: A study of 42 species
    • Lages F., Silva-Graça M., Lucas C. Active glycerol uptake is a mechanism underlying halotolerance in yeasts: a study of 42 species. Microbiology. 145:1999;2577-2585.
    • (1999) Microbiology , vol.145 , pp. 2577-2585
    • Lages, F.1    Silva-Graça, M.2    Lucas, C.3
  • 236
    • 0021832049 scopus 로고
    • Isolation of the fructose-1,6-bisphosphatase gene of the yeast Schizosaccharomyces pombe. Evidence for transcriptional regulation
    • Vassarotti A., Friessen J.D. Isolation of the fructose-1,6-bisphosphatase gene of the yeast Schizosaccharomyces pombe. Evidence for transcriptional regulation. J. Biol. Chem. 260:1985;6348-6353.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6348-6353
    • Vassarotti, A.1    Friessen, J.D.2
  • 238
    • 0015132126 scopus 로고
    • Fructose 1,6-diphosphatase and sedoheptulose 1,7-diphosphatase from Candida utilis: Purification and properties
    • Traniello S., Calcagno M., Pontremoli S. Fructose 1,6-diphosphatase and sedoheptulose 1,7-diphosphatase from Candida utilis: purification and properties. Arch. Biochem. Biophys. 146:1971;603-610.
    • (1971) Arch. Biochem. Biophys. , vol.146 , pp. 603-610
    • Traniello, S.1    Calcagno, M.2    Pontremoli, S.3
  • 239
    • 0025859184 scopus 로고
    • Glucose repression of transcription of theSchizosaccharomyces pombe fbp1 gene occurs by a cAMP signaling pathway
    • Hoffman C.S., Winston F. Glucose repression of transcription of theSchizosaccharomyces pombe fbp1 gene occurs by a cAMP signaling pathway. Genes Dev. 5:1991;561-571.
    • (1991) Genes Dev. , vol.5 , pp. 561-571
    • Hoffman, C.S.1    Winston, F.2
  • 240
  • 241
    • 0024388313 scopus 로고
    • Isolation and characterization of the gene encoding phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae
    • Valdés-Hevia M.D., de la Guerra R., Gancedo C. Isolation and characterization of the gene encoding phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae. FEBS Lett. 258:1989;313-316.
    • (1989) FEBS Lett. , vol.258 , pp. 313-316
    • Valdés-Hevia, M.D.1    De La Guerra, R.2    Gancedo, C.3
  • 242
    • 0031816542 scopus 로고    scopus 로고
    • Isolation and nucleotide sequence of the gene encoding phosphoenolpyruvate carboxykinase from Kluyveromyces lactis
    • Kitamoto H.K., Ohmono S., Imura Y. Isolation and nucleotide sequence of the gene encoding phosphoenolpyruvate carboxykinase from Kluyveromyces lactis. Yeast. 14:1998;963-967.
    • (1998) Yeast , vol.14 , pp. 963-967
    • Kitamoto, H.K.1    Ohmono, S.2    Imura, Y.3
  • 243
    • 0030970379 scopus 로고    scopus 로고
    • Sequence and promoter regulation of the PCK1 gene encoding phosphoenolpyruvate carboxykinase of the fungal pathogen Candida albicans
    • Leuker C.E., Sonneborn A., Delbruck S., Ernst J.F. Sequence and promoter regulation of the PCK1 gene encoding phosphoenolpyruvate carboxykinase of the fungal pathogen Candida albicans. Gene. 192:1997;235-240.
    • (1997) Gene , vol.192 , pp. 235-240
    • Leuker, C.E.1    Sonneborn, A.2    Delbruck, S.3    Ernst, J.F.4
  • 244
    • 0017389356 scopus 로고
    • Location of three key enzymes of gluconeogenesis in baker's yeast
    • Haarasilta S., Taskinen L. Location of three key enzymes of gluconeogenesis in baker's yeast. Arch. Microbiol. 113:1977;159-161.
    • (1977) Arch. Microbiol. , vol.113 , pp. 159-161
    • Haarasilta, S.1    Taskinen, L.2
  • 245
    • 0017178572 scopus 로고
    • Inactivation by glucose of phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae
    • Gancedo C., Schwerzmann K. Inactivation by glucose of phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae. Arch. Microbiol. 109:1976;221-225.
    • (1976) Arch. Microbiol. , vol.109 , pp. 221-225
    • Gancedo, C.1    Schwerzmann, K.2
  • 246
    • 0022906124 scopus 로고
    • Malate transport in Schizosaccharomyces pombe
    • Osothsilp C., Subden R.E. Malate transport in Schizosaccharomyces pombe. J. Bacteriol. 168:1986;1439-1443.
    • (1986) J. Bacteriol. , vol.168 , pp. 1439-1443
    • Osothsilp, C.1    Subden, R.E.2
  • 247
    • 0019947312 scopus 로고
    • The anaerobic metabolism of malate of Saccharomyces bailii and the partial purification and characterization of malic enzyme
    • Kuczynski J.T., Radler F. The anaerobic metabolism of malate of Saccharomyces bailii and the partial purification and characterization of malic enzyme. Arch. Microbiol. 131:1982;266-270.
    • (1982) Arch. Microbiol. , vol.131 , pp. 266-270
    • Kuczynski, J.T.1    Radler, F.2
  • 248
    • 0021718609 scopus 로고
    • The glucose-dependent transport of L-malate in Zygosaccharomyces bailii
    • Baranowski K., Radler F. The glucose-dependent transport of L-malate in Zygosaccharomyces bailii. Antonie Van Leeuwenhoek. 50:1984;329-340.
    • (1984) Antonie Van Leeuwenhoek , vol.50 , pp. 329-340
    • Baranowski, K.1    Radler, F.2
  • 249
    • 0033538071 scopus 로고    scopus 로고
    • Transcriptional regulation of the Schizosaccharomyces pombe malic enzyme gene, mae2
    • Viljoen M., Volschenk H., Young R.A., van Vuuren H.J. Transcriptional regulation of the Schizosaccharomyces pombe malic enzyme gene, mae2. J. Biol. Chem. 274:1999;9969-9975.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9969-9975
    • Viljoen, M.1    Volschenk, H.2    Young, R.A.3    Van Vuuren, H.J.4
  • 250
    • 0032455440 scopus 로고    scopus 로고
    • Identification and characterization of MAE1, the Saccharomyces cerevisiae structural gene encoding mitochondrial malic enzyme
    • Boles E., de Jong-Gubbels P., Pronk J.T. Identification and characterization of MAE1, the Saccharomyces cerevisiae structural gene encoding mitochondrial malic enzyme. J. Bacteriol. 180:1998;2875-2882.
    • (1998) J. Bacteriol. , vol.180 , pp. 2875-2882
    • Boles, E.1    De Jong-Gubbels, P.2    Pronk, J.T.3
  • 251
    • 0031810672 scopus 로고    scopus 로고
    • Yeast carbon catabolite repression
    • Gancedo J.M. Yeast carbon catabolite repression. Microbiol. Mol. Biol. Rev. 62:1998;334-361.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 334-361
    • Gancedo, J.M.1
  • 252
    • 0032931613 scopus 로고    scopus 로고
    • Cyclic AMP can decrease expression of genes subject to catabolite repression in Saccharomyces cerevisiae
    • Zaragoza O., Lindley C., Gancedo J.M. Cyclic AMP can decrease expression of genes subject to catabolite repression in Saccharomyces cerevisiae. J. Bacteriol. 181:1999;2640-2642.
    • (1999) J. Bacteriol. , vol.181 , pp. 2640-2642
    • Zaragoza, O.1    Lindley, C.2    Gancedo, J.M.3
  • 253
    • 0018969294 scopus 로고
    • Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast
    • Entian K.D. Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Mol. Gen. Genet. 178:1980;633-637.
    • (1980) Mol. Gen. Genet. , vol.178 , pp. 633-637
    • Entian, K.D.1
  • 254
    • 0343371823 scopus 로고    scopus 로고
    • The inactivation of hexokinase activity does not prevent glucose repression in Candida utilis
    • Espinel A.E., Gomez-Toribio V., Peinado J.M. The inactivation of hexokinase activity does not prevent glucose repression in Candida utilis. FEMS Microbiol. Lett. 135:1996;327-332.
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 327-332
    • Espinel, A.E.1    Gomez-Toribio, V.2    Peinado, J.M.3
  • 255
    • 0029942696 scopus 로고    scopus 로고
    • FOG1 and FOG2 genes, required for the transcriptional activation of glucose-repressible genes of Kluyveromyces lactis are homologous to GAL83 and SNF1 of Saccharomyces cerevisiae
    • Goffrini P., Ficarelli A., Donini C., Lodi T., Puglisi P.P., Ferrero I. FOG1 and FOG2 genes, required for the transcriptional activation of glucose-repressible genes of Kluyveromyces lactis are homologous to GAL83 and SNF1 of Saccharomyces cerevisiae. Curr. Genet. 29:1996;316-326.
    • (1996) Curr. Genet. , vol.29 , pp. 316-326
    • Goffrini, P.1    Ficarelli, A.2    Donini, C.3    Lodi, T.4    Puglisi, P.P.5    Ferrero, I.6
  • 256
    • 0030782385 scopus 로고    scopus 로고
    • A gene homologous to Saccharomyces cerevisiae SNF1 appears to be essential for the viability of Candida albicans
    • Petter R., Chang Y.C., Kwon-Chung K.J. A gene homologous to Saccharomyces cerevisiae SNF1 appears to be essential for the viability of Candida albicans. Infect. Immun. 65:1997;4909-4917.
    • (1997) Infect. Immun. , vol.65 , pp. 4909-4917
    • Petter, R.1    Chang, Y.C.2    Kwon-Chung, K.J.3
  • 257
    • 0032886019 scopus 로고    scopus 로고
    • Expression of the SNF1 gene from Candida tropicalis is required for growth on various carbon sources, including glucose
    • Kanai T., Ogawa K., Ueda M., Tanaka A. Expression of the SNF1 gene from Candida tropicalis is required for growth on various carbon sources, including glucose. Arch. Microbiol. 172:1999;256-263.
    • (1999) Arch. Microbiol. , vol.172 , pp. 256-263
    • Kanai, T.1    Ogawa, K.2    Ueda, M.3    Tanaka, A.4
  • 258
    • 0029828850 scopus 로고    scopus 로고
    • Disruption of the SNF1 gene abolishes trehalose utilization in the pathogenic yeast Candida glabrata
    • Petter R., Kwon-Chung K.J. Disruption of the SNF1 gene abolishes trehalose utilization in the pathogenic yeast Candida glabrata. Infect. Immun. 64:1996;5269-5273.
    • (1996) Infect. Immun. , vol.64 , pp. 5269-5273
    • Petter, R.1    Kwon-Chung, K.J.2
  • 259
    • 0028293916 scopus 로고
    • Importance of a flanking AT-rich region in target site recognition by the GC box containing zinc finger protein Mig1
    • Lundin M., Nehlin J.O., Ronne H. Importance of a flanking AT-rich region in target site recognition by the GC box containing zinc finger protein Mig1. Mol. Cell. Biol. 14:1994;1979-1985.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1979-1985
    • Lundin, M.1    Nehlin, J.O.2    Ronne, H.3
  • 260
    • 0028340797 scopus 로고
    • Functional dissection of the yeast Cyc8-Tup1 transcriptional co-repressor complex
    • Tzamarias D., Struhl K. Functional dissection of the yeast Cyc8-Tup1 transcriptional co-repressor complex. Nature. 369:1994;758-760.
    • (1994) Nature , vol.369 , pp. 758-760
    • Tzamarias, D.1    Struhl, K.2
  • 261
    • 0030611091 scopus 로고    scopus 로고
    • Glucose represses the lactose-galactose regulon in Kluyveromyces lactis through a SNF1 and MIG1 dependent pathway that modulates galactokinase (GAL1) expression
    • Dong J., Dickson R.C. Glucose represses the lactose-galactose regulon in Kluyveromyces lactis through a SNF1 and MIG1 dependent pathway that modulates galactokinase (GAL1) expression. Nucleic Acids Res. 25:1997;3657-3664.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3657-3664
    • Dong, J.1    Dickson, R.C.2
  • 262
    • 0033513583 scopus 로고    scopus 로고
    • Conservation of histone binding and transcriptional repressor functions in a Schizosaccharomyces pombe Tup1p homolog
    • Mukai Y., Matsuo E., Roth S.Y., Harashima S. Conservation of histone binding and transcriptional repressor functions in a Schizosaccharomyces pombe Tup1p homolog. Mol. Cell. Biol. 19:1999;8461-8468.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8461-8468
    • Mukai, Y.1    Matsuo, E.2    Roth, S.Y.3    Harashima, S.4
  • 263
    • 0030824249 scopus 로고    scopus 로고
    • Control of filament formation in Candida albicans by the transcriptional repressor TUP1
    • Braun B.R., Johnson A.D. Control of filament formation in Candida albicans by the transcriptional repressor TUP1. Science. 277:1997;105-108.
    • (1997) Science , vol.277 , pp. 105-108
    • Braun, B.R.1    Johnson, A.D.2
  • 264
    • 0033982453 scopus 로고    scopus 로고
    • +-ATPase in fungi and plants
    • +-ATPase in fungi and plants. Biochim. Biophys. Acta. 1469:2000;31-42.
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 31-42
    • Portillo, F.1
  • 265
    • 0018078517 scopus 로고
    • Solubilization by lysolecithin and purification of the plasma membrane ATPase of the yeast Schizosaccharomyces pombe
    • Dufour J.P., Goffeau A. Solubilization by lysolecithin and purification of the plasma membrane ATPase of the yeast Schizosaccharomyces pombe. J. Biol. Chem. 253:1978;7026-7032.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7026-7032
    • Dufour, J.P.1    Goffeau, A.2
  • 266
    • 0023610618 scopus 로고
    • Mutation of a conserved glycine residue modifies the vanadate sensitivity of the plasma membrane. H+-ATPase from Schizosaccharomyces pombe
    • Ghislain M., Schlesser A., Goffeau A. Mutation of a conserved glycine residue modifies the vanadate sensitivity of the plasma membrane. H+-ATPase from Schizosaccharomyces pombe. J. Biol. Chem. 262:1987;17549-17555.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17549-17555
    • Ghislain, M.1    Schlesser, A.2    Goffeau, A.3
  • 267
    • 0026731689 scopus 로고
    • Altered plasma membrane H(+)-ATPase from the Dio-9-resistant pma1-2 mutant of Schizosaccharomyces pombe
    • Ghislain M., De Sadeleer M., Goffeau A. Altered plasma membrane H(+)-ATPase from the Dio-9-resistant pma1-2 mutant of Schizosaccharomyces pombe. Eur. J. Biochem. 209:1992;275-279.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 275-279
    • Ghislain, M.1    De Sadeleer, M.2    Goffeau, A.3
  • 271
    • 0027177656 scopus 로고
    • +)-ATPase during yeast growth and germ tube formation
    • +)-ATPase during yeast growth and germ tube formation. J. Bacteriol. 175:1993;5566-5574.
    • (1993) J. Bacteriol. , vol.175 , pp. 5566-5574
    • Monk, B.C.1    Niimi, M.2    Sheperd, M.G.3
  • 272
    • 0006065895 scopus 로고
    • Eenheid en verscheidenheid in de stofwisseling der microben
    • Kluyver A.J. Eenheid en verscheidenheid in de stofwisseling der microben. Chem. Weekblad. 21:1924;266-277.
    • (1924) Chem. Weekblad , vol.21 , pp. 266-277
    • Kluyver, A.J.1
  • 273
    • 0031832290 scopus 로고    scopus 로고
    • Genetically engineered Saccharomyces yeast capable of effective cofermentation of glucose and xylose
    • Ho N.W.Y., Chen Z., Brainard A.P. Genetically engineered Saccharomyces yeast capable of effective cofermentation of glucose and xylose. Appl. Environm. Microbiol. 64:1998;1852-1859.
    • (1998) Appl. Environm. Microbiol. , vol.64 , pp. 1852-1859
    • Ho, N.W.Y.1    Chen, Z.2    Brainard, A.P.3


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