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Volumn 186, Issue 17, 2004, Pages 5799-5807

Genetic evidence identifying the true gluconeogenic fructose-1,6- bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE BISPHOSPHATASE; INOSITOL MONOPHOSPHATASE; PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 4344692495     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.17.5799-5807.2004     Document Type: Article
Times cited : (81)

References (44)
  • 1
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1
    • in press
    • Atomi, H., T. Fukui, T. Kanai, M. Morikawa, and T. Imanaka. Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea, in press.
    • Archaea
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 2
    • 0034636139 scopus 로고    scopus 로고
    • Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: Comparison with bacterial and archaeal inositol monophosphatases
    • Chen, L., and M. F. Roberts. 2000. Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases. Biochemistry 39:4145-4153.
    • (2000) Biochemistry , vol.39 , pp. 4145-4153
    • Chen, L.1    Roberts, M.F.2
  • 3
    • 0031858558 scopus 로고    scopus 로고
    • Biosynthesis of di-myo-inositol-1,1′-phosphate, a novel osmolyte in hyperthermophilic archaea
    • Chen, L., E. T. Spiliotis, and M. F. Roberts. 1998. Biosynthesis of di-myo-inositol-1,1′-phosphate, a novel osmolyte in hyperthermophilic archaea. J. Bacteriol. 180:3785-3792.
    • (1998) J. Bacteriol. , vol.180 , pp. 3785-3792
    • Chen, L.1    Spiliotis, E.T.2    Roberts, M.F.3
  • 4
    • 0027966149 scopus 로고
    • Occurrence and role of di-myo-inositol-1,1′-phosphate in Methanococcus igneus
    • Ciulla, R. A., S. Burggraf, K. O. Stetter, and M. F. Roberts. 1994. Occurrence and role of di-myo-inositol-1,1′-phosphate in Methanococcus igneus. Appl. Environ. Microbiol. 60:3660-3664.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3660-3664
    • Ciulla, R.A.1    Burggraf, S.2    Stetter, K.O.3    Roberts, M.F.4
  • 5
    • 0033802606 scopus 로고    scopus 로고
    • Purification and characterization of glpX-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli
    • Donahue, J. L., J. L. Bownas, W. G. Niehaus, and T. J. Larson. 2000. Purification and characterization of glpX-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli. J. Bacteriol. 182:5624-5627.
    • (2000) J. Bacteriol. , vol.182 , pp. 5624-5627
    • Donahue, J.L.1    Bownas, J.L.2    Niehaus, W.G.3    Larson, T.J.4
  • 6
    • 0014085165 scopus 로고
    • Genetic mapping of mutations affecting phosphoglucose isomerase and fructose diphosphatase in Escherichia coli
    • Fraenkel, D. G. 1967. Genetic mapping of mutations affecting phosphoglucose isomerase and fructose diphosphatase in Escherichia coli. J. Bacteriol. 93:1582-1587.
    • (1967) J. Bacteriol. , vol.93 , pp. 1582-1587
    • Fraenkel, D.G.1
  • 7
    • 0013805504 scopus 로고
    • Fructose-1,6-diphosphatase and acid hexose phosphatase of Escherichia coli
    • Fraenkel, D. G., and B. L. Horecker. 1965. Fructose-1,6-diphosphatase and acid hexose phosphatase of Escherichia coli. J. Bacteriol. 90:837-842.
    • (1965) J. Bacteriol. , vol.90 , pp. 837-842
    • Fraenkel, D.G.1    Horecker, B.L.2
  • 8
    • 0021058627 scopus 로고
    • Enzymes of gluconeogenesis in the autotroph Methanobacterium thermoautotrophicum
    • Fuchs, G., H. Winter, I. Steiner, and E. Stupperich. 1983. Enzymes of gluconeogenesis in the autotroph Methanobacterium thermoautotrophicum. Arch. Microbiol. 136:160-162.
    • (1983) Arch. Microbiol. , vol.136 , pp. 160-162
    • Fuchs, G.1    Winter, H.2    Steiner, I.3    Stupperich, E.4
  • 9
    • 0018364199 scopus 로고
    • Purification and properties of fructose-1,6-bisphosphatase of Bacillus subtilis
    • Fujita, Y., and E. Freese. 1979. Purification and properties of fructose-1,6-bisphosphatase of Bacillus subtilis. J. Biol. Chem. 254:5340-5349.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5340-5349
    • Fujita, Y.1    Freese, E.2
  • 10
    • 0019424164 scopus 로고
    • Isolation and properties of a Bacillus subtilis mutant unable to produce fructose-bisphosphatase
    • Fujita, Y., and E. Freese. 1981. Isolation and properties of a Bacillus subtilis mutant unable to produce fructose-bisphosphatase. J. Bacteriol. 145:760-767.
    • (1981) J. Bacteriol. , vol.145 , pp. 760-767
    • Fujita, Y.1    Freese, E.2
  • 11
    • 0031858032 scopus 로고    scopus 로고
    • Identification and expression of the Bacillus subtilis fructose-1,6-bisphosphatase gene (fbp)
    • Fujita, Y., K. Yoshida, Y. Miwa, N. Yanai, E. Nagakawa, and Y. Kasahara. 1998. Identification and expression of the Bacillus subtilis fructose-1,6-bisphosphatase gene (fbp). J. Bacteriol. 180:4309-4313.
    • (1998) J. Bacteriol. , vol.180 , pp. 4309-4313
    • Fujita, Y.1    Yoshida, K.2    Miwa, Y.3    Yanai, N.4    Nagakawa, E.5    Kasahara, Y.6
  • 12
    • 2642650376 scopus 로고
    • Reciprocal effects of carbon sources on the levels of an AMP-sensitive fructose-1,6-diphosphatase and phosphofructokinase in yeast
    • Gancedo, C., M. L. Salas, A. Giner, and A. Sols. 1965. Reciprocal effects of carbon sources on the levels of an AMP-sensitive fructose-1,6-diphosphatase and phosphofructokinase in yeast. Biochem. Biophys. Res. Commun. 20:15-20.
    • (1965) Biochem. Biophys. Res. Commun. , vol.20 , pp. 15-20
    • Gancedo, C.1    Salas, M.L.2    Giner, A.3    Sols, A.4
  • 13
    • 0031810672 scopus 로고    scopus 로고
    • Yeast carbon catabolite repression
    • Gancedo, J. M. 1998. Yeast carbon catabolite repression. Microbiol. Mol. Biol. Rev. 62:334-361.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 334-361
    • Gancedo, J.M.1
  • 14
    • 0020362744 scopus 로고
    • Kinetic differences between two interconvertible forms of fructose-1,6-bisphosphatase from Saccharomyces cerevisiae
    • Gancedo, J. M., M. J. Mazón, and C. Gancedo. 1982. Kinetic differences between two interconvertible forms of fructose-1,6-bisphosphatase from Saccharomyces cerevisiae. Arch. Biochem. Biophys. 218:478-482.
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 478-482
    • Gancedo, J.M.1    Mazón, M.J.2    Gancedo, C.3
  • 15
    • 0029008560 scopus 로고
    • Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of Escherichia coli
    • Inada, T., and Y. Nakamura. 1995. Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of Escherichia coli. Biochimie 77:294-302.
    • (1995) Biochimie , vol.77 , pp. 294-302
    • Inada, T.1    Nakamura, Y.2
  • 16
    • 0030055702 scopus 로고    scopus 로고
    • Autogenous control of the suhB gene expression of Escherichia coli
    • Inada, T., and Y. Nakamura. 1996. Autogenous control of the suhB gene expression of Escherichia coli. Biochimie 78:209-212.
    • (1996) Biochimie , vol.78 , pp. 209-212
    • Inada, T.1    Nakamura, Y.2
  • 17
    • 0013946834 scopus 로고
    • A new micromethod for the colorimetric determination of inorganic phosphate
    • Itaya, K., and M. Ui. 1966. A new micromethod for the colorimetric determination of inorganic phosphate. Clin. Chim. Acta 14:361-366.
    • (1966) Clin. Chim. Acta , vol.14 , pp. 361-366
    • Itaya, K.1    Ui, M.2
  • 19
    • 0027944043 scopus 로고
    • Development of a continuous coupled enzymatic assay for myo-inositol monophosphatase
    • Kwok, F., and S. C. L. Lo. 1994. Development of a continuous coupled enzymatic assay for myo-inositol monophosphatase. J. Biochem. Biophys. Methods 29:173-178.
    • (1994) J. Biochem. Biophys. Methods , vol.29 , pp. 173-178
    • Kwok, F.1    Lo, S.C.L.2
  • 20
    • 0031662628 scopus 로고    scopus 로고
    • Effects of temperature, salinity, and medium composition on compatible solute accumulation by Thermococcus spp
    • Lamosa, P., L. O. Martins, M. S. Da Costa, and H. Santos. 1998. Effects of temperature, salinity, and medium composition on compatible solute accumulation by Thermococcus spp. Appl. Environ. Microbiol. 64:3591-3598.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3591-3598
    • Lamosa, P.1    Martins, L.O.2    Da Costa, M.S.3    Santos, H.4
  • 21
    • 0018870829 scopus 로고
    • Rapid reversible inactivation of fructose-1,6-bisphosphatase in Saccharomyces cerevisiae by glucose
    • Lenz, A. G., and H. Holzer. 1980. Rapid reversible inactivation of fructose-1,6-bisphosphatase in Saccharomyces cerevisiae by glucose. FEBS Lett. 109: 271-274.
    • (1980) FEBS Lett. , vol.109 , pp. 271-274
    • Lenz, A.G.1    Holzer, H.2
  • 22
    • 0037383069 scopus 로고    scopus 로고
    • Potential genomic determinants of hyperthermophily
    • Makarova, K. S., Y. I. Wolf, and E. V. Koonin. 2003. Potential genomic determinants of hyperthermophily. Trends Genet. 19:172-176.
    • (2003) Trends Genet. , vol.19 , pp. 172-176
    • Makarova, K.S.1    Wolf, Y.I.2    Koonin, E.V.3
  • 23
    • 0028981456 scopus 로고
    • Accumulation of mannosylglycerate and di-myo-inositol-phosphate by Pyrococcus furiosus in response to salinity and temperature
    • Martins, L. O., and H. Santos. 1995. Accumulation of mannosylglycerate and di-myo-inositol-phosphate by Pyrococcus furiosus in response to salinity and temperature. Appl. Environ. Microbiol. 61:3299-3303.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3299-3303
    • Martins, L.O.1    Santos, H.2
  • 24
    • 0029838122 scopus 로고    scopus 로고
    • New compatible solutes related to di-myo-inositol-phosphate in members of the order Thermotogates
    • Martins, L. O., L. S. Carreto, M. S. Da Costa, and H. Santos. 1996. New compatible solutes related to di-myo-inositol-phosphate in members of the order Thermotogates. J. Bacteriol. 178:5644-5651.
    • (1996) J. Bacteriol. , vol.178 , pp. 5644-5651
    • Martins, L.O.1    Carreto, L.S.2    Da Costa, M.S.3    Santos, H.4
  • 25
    • 0028800519 scopus 로고
    • Inositol monophosphatase activity from the Escherichia coli suhB gene product
    • Matsuhisa, A., N. Suzuki, T. Noda, and K. Shiba. 1995. Inositol monophosphatase activity from the Escherichia coli suhB gene product. J. Bacteriol. 177:200-205.
    • (1995) J. Bacteriol. , vol.177 , pp. 200-205
    • Matsuhisa, A.1    Suzuki, N.2    Noda, T.3    Shiba, K.4
  • 26
    • 0027946790 scopus 로고
    • Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp
    • Morikawa, M., Y. Izawa, N. Rashid, T. Hoaki, and T. Imanaka. 1994. Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp. Appl. Environ. Microbiol. 60: 4559-4566.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4559-4566
    • Morikawa, M.1    Izawa, Y.2    Rashid, N.3    Hoaki, T.4    Imanaka, T.5
  • 27
    • 0037066717 scopus 로고    scopus 로고
    • Global expression profiling of acetate-grown Escherichia coli
    • Oh, M. K., L. Rohlin, K. C. Kao, and J. C. Liao. 2002. Global expression profiling of acetate-grown Escherichia coli. J. Biol. Chem. 277:13175-13183.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13175-13183
    • Oh, M.K.1    Rohlin, L.2    Kao, K.C.3    Liao, J.C.4
  • 28
    • 0025914685 scopus 로고
    • Hepatic gluconeogenesis/glycolysis: Regulation and structure/function relationships of substrate cycle enzymes
    • Pilkis, S. J., and T. H. Claus. 1991. Hepatic gluconeogenesis/glycolysis: regulation and structure/function relationships of substrate cycle enzymes. Annu. Rev. Nutr. 11:465-515.
    • (1991) Annu. Rev. Nutr. , vol.11 , pp. 465-515
    • Pilkis, S.J.1    Claus, T.H.2
  • 29
    • 0037163028 scopus 로고    scopus 로고
    • A novel candidate for the true fructose-1,6-bisphosphatase in archaea
    • Rashid, N., H. Imanaka, T. Kanai, T. Fukui, H. Atomi, and T. Imanaka. 2002. A novel candidate for the true fructose-1,6-bisphosphatase in archaea. J. Biol. Chem. 277:30649-30655.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30649-30655
    • Rashid, N.1    Imanaka, H.2    Kanai, T.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 30
    • 0038709277 scopus 로고    scopus 로고
    • Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: A genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways
    • Regelmann, J., T. Schüle, F. S. Josupeit, J. Horak, M. Rose, K. D. Entian, M. Thumm, and D. H. Wolf. 2003. Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol. Biol. Cell 14:1652-1663.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1652-1663
    • Regelmann, J.1    Schüle, T.2    Josupeit, F.S.3    Horak, J.4    Rose, M.5    Entian, K.D.6    Thumm, M.7    Wolf, D.H.8
  • 31
    • 0141921885 scopus 로고    scopus 로고
    • Fructose-1,6-bisphosphatase from Corynebacterium glutamicum: Expression and deletion of the fbp gene and biochemical characterization of the enzyme
    • Rittmann, D., S. Schaffer, V. F. Wendisch, and H. Sahm. 2003. Fructose-1,6-bisphosphatase from Corynebacterium glutamicum: expression and deletion of the fbp gene and biochemical characterization of the enzyme. Arch. Microbiol. 180:285-292.
    • (2003) Arch. Microbiol. , vol.180 , pp. 285-292
    • Rittmann, D.1    Schaffer, S.2    Wendisch, V.F.3    Sahm, H.4
  • 33
    • 0037215528 scopus 로고    scopus 로고
    • Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermacoccus kodakaraensis KOD1
    • Sato, T., T. Fukui, H. Atomi, and T. Imanaka. 2003. Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermacoccus kodakaraensis KOD1. J. Bacteriol. 185:210-220.
    • (2003) J. Bacteriol. , vol.185 , pp. 210-220
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 34
    • 0027418935 scopus 로고
    • Gluconeogenesis from pyruvate in the hyperthermophilic archaeon Pyrococcus furiosus: Involvement of reactions of the Embden-Meyerhof pathway
    • Schäfer, T., and P. Schönheit. 1993. Gluconeogenesis from pyruvate in the hyperthermophilic archaeon Pyrococcus furiosus: involvement of reactions of the Embden-Meyerhof pathway. Arch. Microbiol. 159:354-363.
    • (1993) Arch. Microbiol. , vol.159 , pp. 354-363
    • Schäfer, T.1    Schönheit, P.2
  • 35
    • 0026766429 scopus 로고
    • Di-myo-inositol-1,1′-phosphate: A new inositol phosphate isolated from Pyrococcus woesei
    • Scholz, S., J. Sonnenbichler, W. Schäfer, and R. Hensel. 1992. Di-myo-inositol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Lett. 306:239-242.
    • (1992) FEBS Lett. , vol.306 , pp. 239-242
    • Scholz, S.1    Sonnenbichler, J.2    Schäfer, W.3    Hensel, R.4
  • 36
    • 0032211886 scopus 로고    scopus 로고
    • The biosynthesis pathway of di-myo-inositol-1,1′-phosphate in Pyrococcus woesei
    • Scholz, S., S. Wolff, and R. Hensel. 1998. The biosynthesis pathway of di-myo-inositol-1,1′-phosphate in Pyrococcus woesei. FEMS Microbiol. Lett. 168:37-42.
    • (1998) FEMS Microbiol. Lett. , vol.168 , pp. 37-42
    • Scholz, S.1    Wolff, S.2    Hensel, R.3
  • 37
    • 0343570543 scopus 로고    scopus 로고
    • Ubc8p functions in catabolite degradation of fructose-1,6-bisphosphatase in yeast
    • Schüle, T., M. Rose, K. D. Entian, M. Thumm, and D. H. Wolf. 2000. Ubc8p functions in catabolite degradation of fructose-1,6-bisphosphatase in yeast. EMBO J. 19:2161-2167.
    • (2000) EMBO J. , vol.19 , pp. 2161-2167
    • Schüle, T.1    Rose, M.2    Entian, K.D.3    Thumm, M.4    Wolf, D.H.5
  • 38
    • 0021166268 scopus 로고
    • Fructose bisphosphatase of Escherichia coli: Cloning of the structural gene (fbp) and preparation of a chromosomal deletion
    • Sedivy, J. M., F. Daldal, and D. G. Fraenkel. 1984. Fructose bisphosphatase of Escherichia coli: cloning of the structural gene (fbp) and preparation of a chromosomal deletion. J. Bacteriol. 158:1048-1053.
    • (1984) J. Bacteriol. , vol.158 , pp. 1048-1053
    • Sedivy, J.M.1    Daldal, F.2    Fraenkel, D.G.3
  • 39
    • 0022368298 scopus 로고
    • Fructose bisphosphatase of Saccharomyces cerevisiae: Cloning, disruption and regulation of the FBPI structural gene
    • Sedivy, J. M., and D. G. Fraenkel. 1985. Fructose bisphosphatase of Saccharomyces cerevisiae: cloning, disruption and regulation of the FBPI structural gene. J. Mol. Biol. 186:307-319.
    • (1985) J. Mol. Biol. , vol.186 , pp. 307-319
    • Sedivy, J.M.1    Fraenkel, D.G.2
  • 40
    • 0021720662 scopus 로고
    • Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli
    • Shiba, K., K. Ito, and T. Yura. 1984. Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli. J. Bacteriol. 160:696-701.
    • (1984) J. Bacteriol. , vol.160 , pp. 696-701
    • Shiba, K.1    Ito, K.2    Yura, T.3
  • 41
    • 0033756225 scopus 로고    scopus 로고
    • MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase
    • Stec, B., H. Yang, K. A. Johnson, L. Chen, and M. F. Roberts. 2000. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat. Struct. Biol. 7:1046-1050.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1046-1050
    • Stec, B.1    Yang, H.2    Johnson, K.A.3    Chen, L.4    Roberts, M.F.5
  • 42
    • 0036275509 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus
    • Verhees, C. H., J. Akerboom, E. Schiltz, W. M. de Vos, and J. van der Oost. 2002. Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus. J. Bacteriol. 184:3401-3405.
    • (2002) J. Bacteriol. , vol.184 , pp. 3401-3405
    • Verhees, C.H.1    Akerboom, J.2    Schiltz, E.3    De Vos, W.M.4    Van Der Oost, J.5
  • 43
    • 0025320802 scopus 로고
    • 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli
    • 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli. J. Bacteriol. 172:2124-2130.
    • (1990) J. Bacteriol. , vol.172 , pp. 2124-2130
    • Yano, R.1    Nagai, H.2    Shiba, K.3    Yura, T.4
  • 44
    • 0028029482 scopus 로고
    • Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase
    • Zhang, Y., J. Y. Liang, S. Huang, and W. N. Lipscomb. 1994. Toward a mechanism for the allosteric transition of pig kidney fructose-1,6- bisphosphatase. J. Mol. Biol. 244:609-624.
    • (1994) J. Mol. Biol. , vol.244 , pp. 609-624
    • Zhang, Y.1    Liang, J.Y.2    Huang, S.3    Lipscomb, W.N.4


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