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Volumn 151, Issue 5, 2005, Pages 1409-1419

Allosteric NADP-glutamate dehyrogenase from aspergilli: Purification, characterization and implications for metabolic regulation at the carbon-nitrogen interface

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; CARBENOID; CARBON; DICARBOXYLIC ACID DERIVATIVE; DYE; GLUTAMATE DEHYDROGENASE (NADP); GLUTAMIC ACID; GLUTARIC ACID DERIVATIVE; NITROGEN; PHTHALIC ACID DERIVATIVE; PYRIDINE DERIVATIVE; TRICARBOXYLIC ACID;

EID: 19044375664     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.27751-0     Document Type: Article
Times cited : (43)

References (52)
  • 1
    • 0020838730 scopus 로고
    • Affinity chromatographic purification of glutamate dehydrogenase of Aspergillus ochraceus
    • Agrawal, A. K. & Rao, V. K. M. (1983). Affinity chromatographic purification of glutamate dehydrogenase of Aspergillus ochraceus. Indian J Exp Biol 21, 553-556.
    • (1983) Indian J. Exp. Biol. , vol.21 , pp. 553-556
    • Agrawal, A.K.1    Rao, V.K.M.2
  • 2
    • 19044388640 scopus 로고
    • A rapid and easy method for the purification of the Neurospora crassa NADP-specific glutamate dehydrogenase
    • Aguirre, J. & Hansberg, W. (1988). A rapid and easy method for the purification of the Neurospora crassa NADP-specific glutamate dehydrogenase. Fungal Genet Newsl 35, 5-6.
    • (1988) Fungal Genet. Newsl. , vol.35 , pp. 5-6
    • Aguirre, J.1    Hansberg, W.2
  • 5
    • 0344073999 scopus 로고    scopus 로고
    • Mycotechnology: The role of fungi in biotechnology
    • Bennett, J. W. (1998). Mycotechnology: the role of fungi in biotechnology. J Biotechnol 66, 101-107.
    • (1998) J. Biotechnol. , vol.66 , pp. 101-107
    • Bennett, J.W.1
  • 6
    • 0015902622 scopus 로고
    • Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora. I. Isolation, subunits, amino acid composition, sulfhydryl groups, and identification of a lysine residue reactive with pyridoxal phosphate and N-ethylmaleimide
    • Blumenthal, K. M. & Smith, E. L. (1973). Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora. I. Isolation, subunits, amino acid composition, sulfhydryl groups, and identification of a lysine residue reactive with pyridoxal phosphate and N-ethylmaleimide. J Biol Chem 248, 6002-6008.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6002-6008
    • Blumenthal, K.M.1    Smith, E.L.2
  • 7
    • 0030464821 scopus 로고    scopus 로고
    • NADP-specific glutamate dehydrogenase of Penicillium chrysogenum has a homohexamer structure
    • Bogati, M. S., Posci, I., Maticsek, J., Boross, P., Tozser, J. & Szentirmai, A. (1996). NADP-specific glutamate dehydrogenase of Penicillium chrysogenum has a homohexamer structure. J Basic Microbiol 36, 371-375.
    • (1996) J. Basic Microbiol. , vol.36 , pp. 371-375
    • Bogati, M.S.1    Posci, I.2    Maticsek, J.3    Boross, P.4    Tozser, J.5    Szentirmai, A.6
  • 8
    • 0015527130 scopus 로고
    • Affinity chromatography of phosphofructokinase using Cibacron blue F3G-A
    • Bohme, H.-J., Kopperschlager, G., Schulz, J. & Hofmann, E. (1972). Affinity chromatography of phosphofructokinase using Cibacron blue F3G-A. J Chromatogr 69, 209-214.
    • (1972) J. Chromatogr. , vol.69 , pp. 209-214
    • Bohme, H.-J.1    Kopperschlager, G.2    Schulz, J.3    Hofmann, E.4
  • 9
    • 84989682257 scopus 로고
    • Purification and properties of NADP-dependent glutamate dehydrogenase from Sphaerostilbe repens
    • Botton, B. & Msatef, Y. (1983). Purification and properties of NADP-dependent glutamate dehydrogenase from Sphaerostilbe repens. Physiol Plant 59, 428-444.
    • (1983) Physiol. Plant , vol.59 , pp. 428-444
    • Botton, B.1    Msatef, Y.2
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
  • 12
    • 0031817133 scopus 로고    scopus 로고
    • Characterization and nitrogen-source regulation at the transcriptional level of the gdhA gene of Aspergillus awamori encoding an NADP-dependent glutamate dehydrogenase
    • Cardoza, R. E., Moralejo, F. J., Gutierrez, S., Casqueiro, J., Fierro, F. & Martin, J. F. (1998). Characterization and nitrogen-source regulation at the transcriptional level of the gdhA gene of Aspergillus awamori encoding an NADP-dependent glutamate dehydrogenase. Curr Genet 34, 50-59.
    • (1998) Curr. Genet. , vol.34 , pp. 50-59
    • Cardoza, R.E.1    Moralejo, F.J.2    Gutierrez, S.3    Casqueiro, J.4    Fierro, F.5    Martin, J.F.6
  • 13
    • 0006541738 scopus 로고
    • L-Glutamic acid dehydrogenase: Structural requirements for substrate competition: Effect of thyroxine
    • Caughey, W. S., Smiley, J. D. & Hellerman, L. (1956). L-Glutamic acid dehydrogenase: structural requirements for substrate competition: effect of thyroxine. J Biol Chem 224, 591-607.
    • (1956) J. Biol. Chem. , vol.224 , pp. 591-607
    • Caughey, W.S.1    Smiley, J.D.2    Hellerman, L.3
  • 14
    • 17644369410 scopus 로고    scopus 로고
    • Integrated regulation of the nitrogen-carbon interface
    • Edited by J. Winderickx & P. M. Taylor. Berlin & Heidelberg: Springer
    • Cooper, T. G. (2004). Integrated regulation of the nitrogen-carbon interface. In Topics in Current Genetics, vol. 7, pp. 225-257. Edited by J. Winderickx & P. M. Taylor. Berlin & Heidelberg: Springer.
    • (2004) Topics in Current Genetics , vol.7 , pp. 225-257
    • Cooper, T.G.1
  • 15
    • 0345438400 scopus 로고
    • The inhibition of glutamate dehydrogenase by derivatives of isophthalic acid
    • Cunliffe, D., Leason, M., Parkin, D. & Lea, P. (1983). The inhibition of glutamate dehydrogenase by derivatives of isophthalic acid. Phytochemistry 22, 1357-1360.
    • (1983) Phytochemistry , vol.22 , pp. 1357-1360
    • Cunliffe, D.1    Leason, M.2    Parkin, D.3    Lea, P.4
  • 16
    • 0035941209 scopus 로고    scopus 로고
    • NADP-glutamate dehydrogenase isoenzymes of Saccharomyces cerevisiae. Purification, kinetic properties, and physiological roles
    • DeLuna, A., Avendano, A., Riego, L. & Gonzalez, A. (2001). NADP-glutamate dehydrogenase isoenzymes of Saccharomyces cerevisiae. Purification, kinetic properties, and physiological roles. J Biol Chem 276, 43775-43783.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43775-43783
    • DeLuna, A.1    Avendano, A.2    Riego, L.3    Gonzalez, A.4
  • 17
    • 0035892653 scopus 로고    scopus 로고
    • Analysis of conformationally restricted alpha-ketoglutarate analogues as substrates of dehydrogenases and aminotransferases
    • Denton, T. T., Thompson, C. M. & Cooper, J. L. (2001). Analysis of conformationally restricted alpha-ketoglutarate analogues as substrates of dehydrogenases and aminotransferases. Anal Biochem 298, 265-274.
    • (2001) Anal. Biochem. , vol.298 , pp. 265-274
    • Denton, T.T.1    Thompson, C.M.2    Cooper, J.L.3
  • 18
    • 0032850367 scopus 로고    scopus 로고
    • The NADP-dependent glutamate dehydrogenase gene from Penicillium chrysogenum and the construction of expression vectors for filamentous fungi
    • Diez, B., Mellado, E., Rodriguez, M., Bernasconi, E. & Barredo, J. L. (1999). The NADP-dependent glutamate dehydrogenase gene from Penicillium chrysogenum and the construction of expression vectors for filamentous fungi. Appl Microbiol Biotechnol 52, 196-207.
    • (1999) Appl. Microbiol. Biotechnol. , vol.52 , pp. 196-207
    • Diez, B.1    Mellado, E.2    Rodriguez, M.3    Bernasconi, E.4    Barredo, J.L.5
  • 19
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis, K. J. & Morrison, J. F. (1982). Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol 87, 405-426.
    • (1982) Methods Enzymol. , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 20
    • 85025308811 scopus 로고
    • Genetically determined multiple forms of glutamic dehydrogenase in Neurospora crassa
    • Fincham, J. R. S. (1962). Genetically determined multiple forms of glutamic dehydrogenase in Neurospora crassa. J Mol Biol 4, 257-274.
    • (1962) J. Mol. Biol. , vol.4 , pp. 257-274
    • Fincham, J.R.S.1
  • 21
    • 0033846090 scopus 로고    scopus 로고
    • The Neurospora am gene and NADP-specific glutamate dehydrogenase: Mutational sequence changes and functional effects - More mutants and a summary
    • Fincham, J. R. S., Kinsey, J. A., Fuentes, A. M., Cummings, N. J. & Connerton, I. F. (2000). The Neurospora am gene and NADP-specific glutamate dehydrogenase: mutational sequence changes and functional effects - more mutants and a summary. Genet Res 76, 1-10.
    • (2000) Genet. Res. , vol.76 , pp. 1-10
    • Fincham, J.R.S.1    Kinsey, J.A.2    Fuentes, A.M.3    Cummings, N.J.4    Connerton, I.F.5
  • 22
    • 0035929374 scopus 로고    scopus 로고
    • Stabilization of noncovalent intermediates in enzymatically catalyzed reactions
    • Fisher, H. F., Maniscalco, S. J. & Tally, J. (2001). Stabilization of noncovalent intermediates in enzymatically catalyzed reactions. Biochem Biophys Res Commun 287, 343-347.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 343-347
    • Fisher, H.F.1    Maniscalco, S.J.2    Tally, J.3
  • 23
    • 0026654155 scopus 로고
    • Staining for enzymatic activity after gel electrophoresis, I
    • Gabriel, O. & Gersten, D. M. (1992). Staining for enzymatic activity after gel electrophoresis, I. and Biochem 203, 1-21.
    • (1992) Anal. Biochem. , vol.203 , pp. 1-21
    • Gabriel, O.1    Gersten, D.M.2
  • 24
    • 0000572386 scopus 로고
    • The effect of feedback inhibitor, CTP, on subunit interactions in aspartate transcarbamylase
    • Gerhart, J. C. & Pardee, A. B. (1963). The effect of feedback inhibitor, CTP, on subunit interactions in aspartate transcarbamylase. Cold Spring Harbor Symp Quant Biol 28, 491-496.
    • (1963) Cold Spring Harbor Symp. Quant. Biol. , vol.28 , pp. 491-496
    • Gerhart, J.C.1    Pardee, A.B.2
  • 25
    • 0024336791 scopus 로고
    • Nucleotide sequence and regulation of expression of the Aspergillus nidulans gdhA gene encoding NADP dependent glutamate dehydrogenase
    • Hawkins, A. R., Gurr, S. J., Montague, P. & Kinghorn, J. R. (1989). Nucleotide sequence and regulation of expression of the Aspergillus nidulans gdhA gene encoding NADP dependent glutamate dehydrogenase. Mol Gen Genet 218, 105-111.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 105-111
    • Hawkins, A.R.1    Gurr, S.J.2    Montague, P.3    Kinghorn, J.R.4
  • 26
    • 0024337652 scopus 로고
    • Ammonium assimilation by Candida albicans and other yeasts: Evidence for activity of glutamate synthase
    • Holmes, A. R., Collings, A., Farnden, K. J. F. & Shepherd, M. G. (1989). Ammonium assimilation by Candida albicans and other yeasts: evidence for activity of glutamate synthase. J Gen Microbiol 135, 1423-1430.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1423-1430
    • Holmes, A.R.1    Collings, A.2    Farnden, K.J.F.3    Shepherd, M.G.4
  • 27
    • 0027333040 scopus 로고
    • L-Glutamate dehydrogenases: Distribution, properties and mechanism
    • Hudson, R. C. & Daniel, R. M. (1993). L-Glutamate dehydrogenases: distribution, properties and mechanism. Comp Biochem Physiol 106B, 767-792.
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 767-792
    • Hudson, R.C.1    Daniel, R.M.2
  • 28
    • 0015899509 scopus 로고
    • NAD and NADP L-glutamate dehydrogenase activity and ammonium regulation in Aspergillus nidulans
    • Kinghorn, J. R. & Pateman, J. A. (1973). NAD and NADP L-glutamate dehydrogenase activity and ammonium regulation in Aspergillus nidulans. J Gen Microbiol 78, 39-46.
    • (1973) J. Gen. Microbiol. , vol.78 , pp. 39-46
    • Kinghorn, J.R.1    Pateman, J.A.2
  • 29
    • 0034607152 scopus 로고    scopus 로고
    • Metabolic fate of glutamate and evaluation of flux through the 4-aminobutyrate (GABA) shunt in Aspergillus niger
    • Kumar, S., Punekar, N. S., SatyaNarayan, V. & Venkatesh, K. V. (2000). Metabolic fate of glutamate and evaluation of flux through the 4-aminobutyrate (GABA) shunt in Aspergillus niger. Biotechnol Bioeng 67, 575-584.
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 575-584
    • Kumar, S.1    Punekar, N.S.2    SatyaNarayan, V.3    Venkatesh, K.V.4
  • 30
    • 0023236539 scopus 로고
    • The involvement of glutamine synthetase/glutamate synthase in ammonia assimilation by Aspergillus nidulans
    • Kusnan, M. B., Berger, M. G. & Fock, H. P. (1987). The involvement of glutamine synthetase/glutamate synthase in ammonia assimilation by Aspergillus nidulans. J Gen Microbiol 133, 1235-1242.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 1235-1242
    • Kusnan, M.B.1    Berger, M.G.2    Fock, H.P.3
  • 32
    • 0036897415 scopus 로고    scopus 로고
    • Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum
    • MacRae, I. J., Segel, I. H. & Fisher, A. J. (2002). Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum. Nat Struct Biol 9, 945-949.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 945-949
    • MacRae, I.J.1    Segel, I.H.2    Fisher, A.J.3
  • 33
    • 84982615390 scopus 로고
    • Nitrogen assimilation in mycorrhizas. Purification and properties of the nicotinamide dinucleotide phosphate-specific glutamate dehydrogenase of the ectomycorrhizal fungus Cenococcum geophilum Fr
    • Martin, F., Msatef, Y. & Botton, B. (1983). Nitrogen assimilation in mycorrhizas. Purification and properties of the nicotinamide dinucleotide phosphate-specific glutamate dehydrogenase of the ectomycorrhizal fungus Cenococcum geophilum Fr. New Phytol 93, 415-422.
    • (1983) New Phytol. , vol.93 , pp. 415-422
    • Martin, F.1    Msatef, Y.2    Botton, B.3
  • 34
    • 84986946650 scopus 로고
    • The involvement of glutamate dehydrogenase and glutamine synthetase in ammonia assimilation by the rapidly growing ectomycorrhizal ascomycete Cenococcum geophylum
    • Martin, F., Stewart, G. R., Genetet, I. & Mourot, B. (1988). The involvement of glutamate dehydrogenase and glutamine synthetase in ammonia assimilation by the rapidly growing ectomycorrhizal ascomycete Cenococcum geophylum. New Phytol 110, 541-550.
    • (1988) New Phytol. , vol.110 , pp. 541-550
    • Martin, F.1    Stewart, G.R.2    Genetet, I.3    Mourot, B.4
  • 35
    • 0032600814 scopus 로고    scopus 로고
    • Response of the central metabolism in Corynebacterium glutamicum to the use of an NADH-dependent glutamate dehydrogenase
    • Marx, A., Eikmanns, B. J., Sahm, H., de Graaf, A. A. & Eggeling, L. (1999). Response of the central metabolism in Corynebacterium glutamicum to the use of an NADH-dependent glutamate dehydrogenase. Metab Eng 1, 35-48.
    • (1999) Metab. Eng. , vol.1 , pp. 35-48
    • Marx, A.1    Eikmanns, B.J.2    Sahm, H.3    de Graaf, A.A.4    Eggeling, L.5
  • 36
    • 0030794656 scopus 로고    scopus 로고
    • Genetic regulation of nitrogen metabolism in the fungi
    • Marzluf, G. A. (1997). Genetic regulation of nitrogen metabolism in the fungi. Microbiol Mol Biol Rev 61, 17-32.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 17-32
    • Marzluf, G.A.1
  • 37
    • 0021909170 scopus 로고
    • Presence and regulation of the alpha-ketoglutarate dehydrogenase multienzyme complex in the filamentous fungus Aspergillus niger
    • Meixner-Monori, B., Kubicek, C. P., Habison, A., Kubicek-Pranz, E. M. & Röhr, M. (1985). Presence and regulation of the alpha-ketoglutarate dehydrogenase multienzyme complex in the filamentous fungus Aspergillus niger. J Bacteriol 161, 265-271.
    • (1985) J. Bacteriol. , vol.161 , pp. 265-271
    • Meixner-Monori, B.1    Kubicek, C.P.2    Habison, A.3    Kubicek-Pranz, E.M.4    Röhr, M.5
  • 38
    • 0025101830 scopus 로고
    • Glutamine metabolism and cycling in Neurospora crassa
    • Mora, J. (1990). Glutamine metabolism and cycling in Neurospora crassa. Microbiol Rev 54, 293-304.
    • (1990) Microbiol. Rev. , vol.54 , pp. 293-304
    • Mora, J.1
  • 39
    • 0035819980 scopus 로고    scopus 로고
    • An NMR and ab initio quantum chemical study of acid-base equilibria for conformationally constrained acidic alpha-amino acids in aqueous solution
    • Nielsen, P. A., Jaroszewski, J. W., Norrby, P.-O. & Liljefors, T. (2001). An NMR and ab initio quantum chemical study of acid-base equilibria for conformationally constrained acidic alpha-amino acids in aqueous solution. J Am Chem Soc 123, 2003-2006.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2003-2006
    • Nielsen, P.A.1    Jaroszewski, J.W.2    Norrby, P.-O.3    Liljefors, T.4
  • 40
    • 0033929520 scopus 로고    scopus 로고
    • Optimization of ethanol production in Saccharomyces cerevisiae by metabolic engineering of the ammonia assimilation
    • Nissen, T. L., Kielland-Brandt, M. C., Nielsen, J. & Villadsen, J. (2000). Optimization of ethanol production in Saccharomyces cerevisiae by metabolic engineering of the ammonia assimilation. Metab Eng 2, 69-77.
    • (2000) Metab. Eng. , vol.2 , pp. 69-77
    • Nissen, T.L.1    Kielland-Brandt, M.C.2    Nielsen, J.3    Villadsen, J.4
  • 41
    • 0032931265 scopus 로고    scopus 로고
    • Identification of enzymes and quantification of metabolic fluxes in the wild type and in a recombinant Aspergillus oryzae strain
    • Pedersen, H., Carlsen, M. & Nielsen, J. (1999). Identification of enzymes and quantification of metabolic fluxes in the wild type and in a recombinant Aspergillus oryzae strain. Appl Environ Microbiol 165, 11-19.
    • (1999) Appl. Environ. Microbiol. , vol.165 , pp. 11-19
    • Pedersen, H.1    Carlsen, M.2    Nielsen, J.3
  • 42
    • 0028025206 scopus 로고
    • Biochemical and genetical studies of NADP-specific glutamate dehydrogenase in the fission yeast Schizosaccharomyces pombe
    • Perysinakis, A., Kinghorn, J. R. & Drainas, C. (1994). Biochemical and genetical studies of NADP-specific glutamate dehydrogenase in the fission yeast Schizosaccharomyces pombe. Curr Genet 26, 315-320.
    • (1994) Curr. Genet. , vol.26 , pp. 315-320
    • Perysinakis, A.1    Kinghorn, J.R.2    Drainas, C.3
  • 43
    • 0008245499 scopus 로고    scopus 로고
    • Production of organic acids by fungi
    • Edited by H. D. Osiewacz. Berlin & Heidelberg: Springer
    • Ruijter, G. J. G., Kubicek, C. P. & Visser, J. (2002). Production of organic acids by fungi. In The Mycota. X. Industrial Applications, pp. 213-230. Edited by H. D. Osiewacz. Berlin & Heidelberg: Springer.
    • (2002) The Mycota. X. Industrial Applications , pp. 213-230
    • Ruijter, G.J.G.1    Kubicek, C.P.2    Visser, J.3
  • 44
    • 0025916758 scopus 로고
    • The involvement of glutamate dehydrogenase and glutamine synthetase/glutamate synthase in ammonia assimilation by the basidiomycete fungus Strophia semiglobata
    • Schwartz, T., Kusnan, M. B. & Fock, H. P. (1991). The involvement of glutamate dehydrogenase and glutamine synthetase/glutamate synthase in ammonia assimilation by the basidiomycete fungus Strophia semiglobata. J Gen Microbiol 137, 2253-2258.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2253-2258
    • Schwartz, T.1    Kusnan, M.B.2    Fock, H.P.3
  • 46
    • 0023840718 scopus 로고
    • Mechanism of formation of bound alpha-iminoglutarate from alpha-ketoglutarate in the glutamate dehydrogenase reaction. A chemical basis for ammonia recognition
    • Srinivasan, R., Viswanathan, T. S. & Fisher, H. F. (1988). Mechanism of formation of bound alpha-iminoglutarate from alpha-ketoglutarate in the glutamate dehydrogenase reaction. A chemical basis for ammonia recognition. J Biol Chem 263, 2304-2308.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2304-2308
    • Srinivasan, R.1    Viswanathan, T.S.2    Fisher, H.F.3
  • 47
    • 0024969299 scopus 로고
    • Purification and characterization of NAD-glutamate dehydrogenase from Aspergillus nidulans
    • Stevens, L., Duncan, D. & Robertson, P. (1989). Purification and characterization of NAD-glutamate dehydrogenase from Aspergillus nidulans. FEMS Microbiol Lett 57, 173-178.
    • (1989) FEMS Microbiol. Lett. , vol.57 , pp. 173-178
    • Stevens, L.1    Duncan, D.2    Robertson, P.3
  • 49
    • 0033955802 scopus 로고    scopus 로고
    • The role of ammonia metabolism in nitrogen catabolite repression in Saccharomyces cerevisiae
    • ter Schure, E. G., van Riel, N. A. W. & Verrips, C. T. (2000). The role of ammonia metabolism in nitrogen catabolite repression in Saccharomyces cerevisiae. FEMS Microbiol Rev 24, 67-83.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 67-83
    • ter Schure, E.G.1    van Riel, N.A.W.2    Verrips, C.T.3
  • 50
    • 0016326178 scopus 로고
    • Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora. I. Purification and molecular properties
    • Veronese, F. M., Nyc, J. F., Degani, Y., Brown, D. M. & Smith, E. L. (1974). Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora. I. Purification and molecular properties. J Biol Chem 249, 7922-7928.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7922-7928
    • Veronese, F.M.1    Nyc, J.F.2    Degani, Y.3    Brown, D.M.4    Smith, E.L.5
  • 51
  • 52
    • 0034886321 scopus 로고    scopus 로고
    • Biotechnological production of itaconic acid
    • Willeke, T. & Vorlop, K. D. (2001). Biotechnological production of itaconic acid. Appl Microbiol Biotechnol 56, 289-295.
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 289-295
    • Willeke, T.1    Vorlop, K.D.2


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