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Volumn 55, Issue 4, 1999, Pages 617-638

Glutamate synthase: A complex iron-sulfur flavoprotein

Author keywords

Amidotransferases; Ammonia assimilation; Electron transfer; Flavoprotein; Glutamate synthase; Iron sulfur clusters; Nitrogen metabolism; Oxidoreductases

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; FERREDOXIN; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; GLUTAMATE SYNTHASE; GLUTAMIC ACID; GLUTAMINE; IRON SULFUR PROTEIN; PYRIDINE NUCLEOTIDE;

EID: 0032951727     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050319     Document Type: Review
Times cited : (101)

References (66)
  • 2
    • 0022272463 scopus 로고
    • Glutamate synthase from Escherichia coli, Klebsiella aerogenes and Saccharomyces cerevisiae
    • Meister A. (1985) Glutamate synthase from Escherichia coli, Klebsiella aerogenes and Saccharomyces cerevisiae. Methods Enzymol. 113: 327-337
    • (1985) Methods Enzymol. , vol.113 , pp. 327-337
    • Meister, A.1
  • 3
  • 6
    • 0026097297 scopus 로고
    • Ferredoxin-dependent chloroplast enzymes
    • Knaff D. B. and Hirasawa M. (1991) Ferredoxin-dependent chloroplast enzymes. Biochim. Biophys. Acta 1056: 93-125
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 93-125
    • Knaff, D.B.1    Hirasawa, M.2
  • 7
    • 0032007276 scopus 로고    scopus 로고
    • Glutamate synthase and nitrogen assimilation
    • Temple S. J., Vance C. P. and Gantt J. S. (1998) Glutamate synthase and nitrogen assimilation. Trends Plant Sci. 3: 51-56
    • (1998) Trends Plant Sci. , vol.3 , pp. 51-56
    • Temple, S.J.1    Vance, C.P.2    Gantt, J.S.3
  • 8
    • 0026560269 scopus 로고
    • Purification and characterization of the ferredoxin-glutamate synthase from the unicellular cyanobacterium Synechococcus sp. PCC 6301
    • Marques S., Florencio F. J. and Candau P. (1992) Purification and characterization of the ferredoxin-glutamate synthase from the unicellular cyanobacterium Synechococcus sp. PCC 6301. Eur. J. Biochem. 206: 69-77
    • (1992) Eur. J. Biochem. , vol.206 , pp. 69-77
    • Marques, S.1    Florencio, F.J.2    Candau, P.3
  • 9
    • 0029889726 scopus 로고    scopus 로고
    • Oxidation-reduction and transient kinetic studies of spinach ferredoxin-dependent glutamate synthase
    • Hirasawa M., Hurley J. K., Salamon Z., Tollin G. and Knaff D. B. (1996) Oxidation-reduction and transient kinetic studies of spinach ferredoxin-dependent glutamate synthase. Arch. Biochim. Biophys. 330: 209-215
    • (1996) Arch. Biochim. Biophys. , vol.330 , pp. 209-215
    • Hirasawa, M.1    Hurley, J.K.2    Salamon, Z.3    Tollin, G.4    Knaff, D.B.5
  • 10
    • 0000322050 scopus 로고
    • Purification and characterization of NADH-glutamate synthase from Alfalfa root nodules
    • Anderson M. P., Vance C. P., Heichel G. H. and Miller S. S. (1989) Purification and characterization of NADH-glutamate synthase from Alfalfa root nodules. Plant Physiol. 90: 351-358
    • (1989) Plant Physiol. , vol.90 , pp. 351-358
    • Anderson, M.P.1    Vance, C.P.2    Heichel, G.H.3    Miller, S.S.4
  • 11
    • 0028925047 scopus 로고
    • Saccharomyces cerevisiae has a single glutamate synthase gene coding for a plant-like high molecular weight polypeptide
    • Cogoni C., Valenzuela L., Gonzalez-Halphen D., Olivera H., Macino G., Ballario P. et al. (1995) Saccharomyces cerevisiae has a single glutamate synthase gene coding for a plant-like high molecular weight polypeptide. J. Bacteriol. 177: 792-798
    • (1995) J. Bacteriol. , vol.177 , pp. 792-798
    • Cogoni, C.1    Valenzuela, L.2    Gonzalez-Halphen, D.3    Olivera, H.4    Macino, G.5    Ballario, P.6
  • 12
    • 0032127173 scopus 로고    scopus 로고
    • Purification and characterization of NADH-dependent glutamate synthase from the silkworm fat body (Bombyx mori)
    • Hirayama C., Saito H., Konno K. and Shinbo H. (1998) Purification and characterization of NADH-dependent glutamate synthase from the silkworm fat body (Bombyx mori). Insect Biochem. Mol. Biol. 28: 473-482
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 473-482
    • Hirayama, C.1    Saito, H.2    Konno, K.3    Shinbo, H.4
  • 13
    • 0001669793 scopus 로고
    • Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine, and D-alanine
    • Neidhart F. C. (ed.), ASM Press, Washington, DC
    • Reitzer L. J. and Magasanik B. (1987) Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine, and D-alanine. In: E. coli and S. typhimurium: Cellular and Molecular Biology, pp. 302-320, Neidhart F. C. (ed.), ASM Press, Washington, DC
    • (1987) E. Coli and S. Typhimurium: Cellular and Molecular Biology , pp. 302-320
    • Reitzer, L.J.1    Magasanik, B.2
  • 14
    • 0000060736 scopus 로고    scopus 로고
    • Ammonia assimilation and the biosynthesis of glutamine, glutamute, aspartate, asparagine, L-alanine and D-alanine
    • Neidhart F. C. (ed.), ASM Press, Washington DC
    • Reitzer L. J. (1996) Ammonia assimilation and the biosynthesis of glutamine, glutamute, aspartate, asparagine, L-alanine and D-alanine. In: Escherichia coli and Salmonella: Cellular and Molecular Biology, pp. 391-407, Neidhart F. C. (ed.), ASM Press, Washington DC
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 391-407
    • Reitzer, L.J.1
  • 15
    • 0014774708 scopus 로고
    • Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route
    • Tempest D. W., Meers J. L. and Brown C. M. (1970) Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route. Biochem. J. 117: 405-407
    • (1970) Biochem. J. , vol.117 , pp. 405-407
    • Tempest, D.W.1    Meers, J.L.2    Brown, C.M.3
  • 16
    • 0019214015 scopus 로고
    • Kinetic mechanism of Escherichia coli glutamine synthetase
    • Meek T. D. and Villafranca J. J. (1980) Kinetic mechanism of Escherichia coli glutamine synthetase. Biochemistry 19: 5513-5519
    • (1980) Biochemistry , vol.19 , pp. 5513-5519
    • Meek, T.D.1    Villafranca, J.J.2
  • 17
    • 0026056062 scopus 로고
    • The kinetic mechanism of the reactions catalyzed by the glutamate synthase from Azospirillum brasilense
    • Vanoni M. A., Rescigno M., Nuzzi L., Zanetti G. and Curti B. (1991) The kinetic mechanism of the reactions catalyzed by the glutamate synthase from Azospirillum brasilense. Eur. J. Biochem. 202: 181-189
    • (1991) Eur. J. Biochem. , vol.202 , pp. 181-189
    • Vanoni, M.A.1    Rescigno, M.2    Nuzzi, L.3    Zanetti, G.4    Curti, B.5
  • 18
    • 0015186294 scopus 로고
    • The mechanism of ammonia assimilation in nitrogen fixing bacteria
    • Nagatani H., Shimizu M. and Valentine R. C. (1971) The mechanism of ammonia assimilation in nitrogen fixing bacteria. Arch. Mikrobiol. 79: 164-175
    • (1971) Arch. Mikrobiol. , vol.79 , pp. 164-175
    • Nagatani, H.1    Shimizu, M.2    Valentine, R.C.3
  • 19
    • 0019058201 scopus 로고
    • Evaluation of nitrogen fixation by bacteria in association with roots of tropical grasses
    • van Berkum P. and Bohlool B. B. (1980) Evaluation of nitrogen fixation by bacteria in association with roots of tropical grasses. Microbiol. Rev. 44: 491-517
    • (1980) Microbiol. Rev. , vol.44 , pp. 491-517
    • Van Berkum, P.1    Bohlool, B.B.2
  • 20
  • 23
    • 0026756915 scopus 로고
    • glt F, a member of the glt BDF operon of Escherichia coli, is involved in nitrogen-regulated gene expression
    • Castano I., Flores N., Valle F., Covarrubias A. A. and Bolivar F. (1992) glt F, a member of the glt BDF operon of Escherichia coli, is involved in nitrogen-regulated gene expression. Mol. Microbiol. 6: 2733-2741
    • (1992) Mol. Microbiol. , vol.6 , pp. 2733-2741
    • Castano, I.1    Flores, N.2    Valle, F.3    Covarrubias, A.A.4    Bolivar, F.5
  • 24
    • 0028111825 scopus 로고
    • The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli
    • Calvo J. M. and Matthews R. G. (1994) The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli. Microbiol. Rev. 58: 466-490
    • (1994) Microbiol. Rev. , vol.58 , pp. 466-490
    • Calvo, J.M.1    Matthews, R.G.2
  • 26
    • 0030851327 scopus 로고    scopus 로고
    • A nucleoprotein activation complex between the leucine-responsive regulatory protein and DNA upstream of the gltBDF operon in Escherichia coli
    • Wiese D. E., Ernsting B. R., Blumenthal R. M. and Matthews R. G. (1997) A nucleoprotein activation complex between the leucine-responsive regulatory protein and DNA upstream of the gltBDF operon in Escherichia coli. J. Mol. Biol. 270: 152-168
    • (1997) J. Mol. Biol. , vol.270 , pp. 152-168
    • Wiese, D.E.1    Ernsting, B.R.2    Blumenthal, R.M.3    Matthews, R.G.4
  • 27
    • 0029412081 scopus 로고
    • Sites required for GltC-dependent regulation of Bacillus subtilis glutamate synthase expression
    • Belitsky B. R., Janssen P. J. and Sonenshein A. L. (1995) Sites required for GltC-dependent regulation of Bacillus subtilis glutamate synthase expression. J. Bacteriol. 177: 5686-5695
    • (1995) J. Bacteriol. , vol.177 , pp. 5686-5695
    • Belitsky, B.R.1    Janssen, P.J.2    Sonenshein, A.L.3
  • 28
    • 0031039345 scopus 로고    scopus 로고
    • Altered transcription activation specificity of a mutant form of Bacillus subtilis GltR, a LysR family member
    • Belitsky B. R., Janssen P. J. and Sonenshein A. L. (1997) Altered transcription activation specificity of a mutant form of Bacillus subtilis GltR, a LysR family member. J. Bacteriol. 179: 1035-1043
    • (1997) J. Bacteriol. , vol.179 , pp. 1035-1043
    • Belitsky, B.R.1    Janssen, P.J.2    Sonenshein, A.L.3
  • 32
    • 0018236372 scopus 로고
    • Glutamate synthase: On the kinetic mechanism of the enzyme from Escherichia coli W
    • Rendina A. R. and Orme-Johnson W. H. (1978) Glutamate synthase: on the kinetic mechanism of the enzyme from Escherichia coli W. Biochemistry 17: 5388-5393
    • (1978) Biochemistry , vol.17 , pp. 5388-5393
    • Rendina, A.R.1    Orme-Johnson, W.H.2
  • 33
    • 0022599181 scopus 로고
    • Glutamate synthase from Bacillus subtilis
    • Matsuoka K. and Kimura K. (1986) Glutamate synthase from Bacillus subtilis. J. Biochem. 99: 1087-1100
    • (1986) J. Biochem. , vol.99 , pp. 1087-1100
    • Matsuoka, K.1    Kimura, K.2
  • 34
    • 0002434254 scopus 로고    scopus 로고
    • Flavin-dependent enzymes
    • Sinnot M. L. (ed.), Academic Press, Orlando, FL
    • Palfey B. A. and Massey V. (1998) Flavin-dependent enzymes. In: Comprehensive Biological Catalysis, vol. 3, pp. 83-154, Sinnot M. L. (ed.), Academic Press, Orlando, FL
    • (1998) Comprehensive Biological Catalysis , vol.3 , pp. 83-154
    • Palfey, B.A.1    Massey, V.2
  • 35
    • 0027944061 scopus 로고
    • Interdomain loops and conformational changes of glutamate synthase as detected by limited proteolysis
    • Vanoni M. A., Mazzoni A., Fumagalli P., Negri A., Zanetti G. and Curti B. (1994) Interdomain loops and conformational changes of glutamate synthase as detected by limited proteolysis. Eur. J. Biochem. 226: 505-515
    • (1994) Eur. J. Biochem. , vol.226 , pp. 505-515
    • Vanoni, M.A.1    Mazzoni, A.2    Fumagalli, P.3    Negri, A.4    Zanetti, G.5    Curti, B.6
  • 36
    • 0026659227 scopus 로고
    • Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospirillum brasilense by absorption, circular dichroism and electron paramagnetic resonance spectroscopies
    • Vanoni M. A., Edmondson D. E., Zanetti G. and Curti B. (1992) Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospirillum brasilense by absorption, circular dichroism and electron paramagnetic resonance spectroscopies. Biochemistry 31: 4613-4623
    • (1992) Biochemistry , vol.31 , pp. 4613-4623
    • Vanoni, M.A.1    Edmondson, D.E.2    Zanetti, G.3    Curti, B.4
  • 37
    • 0017378115 scopus 로고
    • On the mechanism of glutamine-dependent reductive amination of α-ketoglutarate catalysed by glutamate synthase
    • Geary L. E. and Meister A. (1977) On the mechanism of glutamine-dependent reductive amination of α-ketoglutarate catalysed by glutamate synthase. J. Biol. Chem. 252: 3501-3508
    • (1977) J. Biol. Chem. , vol.252 , pp. 3501-3508
    • Geary, L.E.1    Meister, A.2
  • 38
    • 0026335088 scopus 로고
    • Mechanistic studies on Azospirillum brasilense glutamate synthase
    • Vanoni M. A., Edmondson D. E., Rescigno M., Zanetti G. and Curti B. (1991) Mechanistic studies on Azospirillum brasilense glutamate synthase. Biochemistry 30: 11478-11484
    • (1991) Biochemistry , vol.30 , pp. 11478-11484
    • Vanoni, M.A.1    Edmondson, D.E.2    Rescigno, M.3    Zanetti, G.4    Curti, B.5
  • 39
    • 0029964615 scopus 로고    scopus 로고
    • Glutamate synthase: Properties of the recombinant β subunit
    • Vanoni M. A., Verzotti E., Zanetti G. and Curti B. (1996) Glutamate synthase: properties of the recombinant β subunit. Eur. J. Biochem. 236: 937-946
    • (1996) Eur. J. Biochem. , vol.236 , pp. 937-946
    • Vanoni, M.A.1    Verzotti, E.2    Zanetti, G.3    Curti, B.4
  • 40
    • 0021100241 scopus 로고
    • Characterisation of 3-iron ferredoxins by means of the linear electric field effect in EPR
    • Peisach J., Beinert H., Emptage M., Mims W. B., Fee J. A., Orme-Johnson W. H. et al. (1983) Characterisation of 3-iron ferredoxins by means of the linear electric field effect in EPR. J. Biol. Chem. 258: 13014-13016
    • (1983) J. Biol. Chem. , vol.258 , pp. 13014-13016
    • Peisach, J.1    Beinert, H.2    Emptage, M.3    Mims, W.B.4    Fee, J.A.5    Orme-Johnson, W.H.6
  • 41
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H., Holm R. H. and Muenek E. (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277: 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Muenek, E.3
  • 42
    • 0032043449 scopus 로고    scopus 로고
    • Iron-sulfur proteins: New roles for old clusters
    • Johnson M. K. (1998) Iron-sulfur proteins: new roles for old clusters. Curr. Opin. Chem. Biol. 2: 173-181
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 173-181
    • Johnson, M.K.1
  • 43
    • 0025874679 scopus 로고
    • Spectroscopic evidence for a [3Fe-4S] cluster in spinach glutamate synthase
    • Knaff D. B., Hirasawa M., Ameyibor E., Fu W. and Johnson M. (1991) Spectroscopic evidence for a [3Fe-4S] cluster in spinach glutamate synthase. J. Biol. Chem. 266: 15080-15084
    • (1991) J. Biol. Chem. , vol.266 , pp. 15080-15084
    • Knaff, D.B.1    Hirasawa, M.2    Ameyibor, E.3    Fu, W.4    Johnson, M.5
  • 44
    • 0016293208 scopus 로고
    • Glutamine-binding subunit of glutamate synthase and partial reactions catalysed by this glutamine amidotransferase
    • Trotta P. P., Platzer K. E. B., Haschemeyer R. H. and Meister A. (1974) Glutamine-binding subunit of glutamate synthase and partial reactions catalysed by this glutamine amidotransferase. Proc. Natl. Acad. Sci. USA 71: 4607-4611
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4607-4611
    • Trotta, P.P.1    Platzer, K.E.B.2    Haschemeyer, R.H.3    Meister, A.4
  • 45
    • 0017115904 scopus 로고
    • Glutamate synthase: Properties of the glutamine-dependent activity
    • Mantsala P. and Zalkin H. (1976) Glutamate synthase: properties of the glutamine-dependent activity. J. Biol. Chem. 251: 3294-3299
    • (1976) J. Biol. Chem. , vol.251 , pp. 3294-3299
    • Mantsala, P.1    Zalkin, H.2
  • 46
    • 0020479381 scopus 로고
    • Inhibition by homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae
    • Masters D. S. and Meister A. (1982) Inhibition by homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae. J. Biol. Chem. 257: 8711-8715
    • (1982) J. Biol. Chem. , vol.257 , pp. 8711-8715
    • Masters, D.S.1    Meister, A.2
  • 48
    • 0025768404 scopus 로고
    • Molecular cloning and characterization of complementary DNA encoding for ferredoxin-dependent glutamate synthase in maize leaf
    • Sakakibara H., Watanabe M., Hase T. and Sugiyama T. (1991) Molecular cloning and characterization of complementary DNA encoding for ferredoxin-dependent glutamate synthase in maize leaf. J. Biol. Chem. 266: 2028-2035
    • (1991) J. Biol. Chem. , vol.266 , pp. 2028-2035
    • Sakakibara, H.1    Watanabe, M.2    Hase, T.3    Sugiyama, T.4
  • 49
    • 0027412184 scopus 로고
    • Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing and analysis of functional domains
    • Pelanda R., Vanoni M. A., Perego M., Piubelli L., Galizzi A., Curti B. et al. (1993) Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing and analysis of functional domains. J. Biol. Chem. 268: 3099-3106
    • (1993) J. Biol. Chem. , vol.268 , pp. 3099-3106
    • Pelanda, R.1    Vanoni, M.A.2    Perego, M.3    Piubelli, L.4    Galizzi, A.5    Curti, B.6
  • 50
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan J. A., Dodson G., Duggleby H. J., Moody P. C. E., Smith J. L., Tomchick D. R. et al. (1995) A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378: 416-419
    • (1995) Nature , vol.378 , pp. 416-419
    • Brannigan, J.A.1    Dodson, G.2    Duggleby, H.J.3    Moody, P.C.E.4    Smith, J.L.5    Tomchick, D.R.6
  • 51
    • 0032539513 scopus 로고    scopus 로고
    • The recombinant α subunit of glutamate synthase: Spectroscopic and catalytic properties
    • Vanoni M. A., Fischer F., Ravasio S., Verzotti E., Edmondson D. E., Hagen W. R. et al. (1998) The recombinant α subunit of glutamate synthase: spectroscopic and catalytic properties. Biochemistry 37: 1828-1838
    • (1998) Biochemistry , vol.37 , pp. 1828-1838
    • Vanoni, M.A.1    Fischer, F.2    Ravasio, S.3    Verzotti, E.4    Edmondson, D.E.5    Hagen, W.R.6
  • 52
    • 0023551349 scopus 로고
    • Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12
    • Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L. M., Flores N. et al. (1987) Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12. Gene 60: 1-11
    • (1987) Gene , vol.60 , pp. 1-11
    • Oliver, G.1    Gosset, G.2    Sanchez-Pescador, R.3    Lozoya, E.4    Ku, L.M.5    Flores, N.6
  • 53
    • 0027550316 scopus 로고
    • Molecular characterization of NADH-dependent glutamate synthase from Alfalfa nodules
    • Gregerson R. G., Miller S. S., Twary S. N., Gantt J. S. and Vance C. P. (1993) Molecular characterization of NADH-dependent glutamate synthase from Alfalfa nodules. Plant Cell 5: 215-226
    • (1993) Plant Cell , vol.5 , pp. 215-226
    • Gregerson, R.G.1    Miller, S.S.2    Twary, S.N.3    Gantt, J.S.4    Vance, C.P.5
  • 55
    • 0013475890 scopus 로고    scopus 로고
    • Glutamate synthase from Azospirillum brasilense
    • Stevenson K., Massey V. and Williams C. H. (eds), Calgary University Press, Calgary
    • Vanoni M. A., Verzotti E., Fischer F., Coppola M., Ferretti S., Zanetti G. et al. (1997) Glutamate synthase from Azospirillum brasilense. In: Flavins and Flavoproteins 1996, pp. 879-888, Stevenson K., Massey V. and Williams C. H. (eds), Calgary University Press, Calgary
    • (1997) Flavins and Flavoproteins 1996 , pp. 879-888
    • Vanoni, M.A.1    Verzotti, E.2    Fischer, F.3    Coppola, M.4    Ferretti, S.5    Zanetti, G.6
  • 56
    • 0028287640 scopus 로고
    • The pH dependent behaviour of catalytic activities of Azospirillum brasilense glutamate synthase and iodoacetamide modification of the enzyme provide evidence for a catalytic Cys-His ion pair
    • Vanoni M. A., Accornero P., Carrera G. and Curti B. (1994) The pH dependent behaviour of catalytic activities of Azospirillum brasilense glutamate synthase and iodoacetamide modification of the enzyme provide evidence for a catalytic Cys-His ion pair. Arch. Biochem. Biophys. 309: 222-230
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 222-230
    • Vanoni, M.A.1    Accornero, P.2    Carrera, G.3    Curti, B.4
  • 57
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga R. K., Terpstra P. and Hol W. G. J. (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187: 101-107
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 58
    • 0026060723 scopus 로고
    • Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes
    • McKie J. H. and Douglas K. T. (1991) Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett. 279: 5-7
    • (1991) FEBS Lett. , vol.279 , pp. 5-7
    • McKie, J.H.1    Douglas, K.T.2
  • 59
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas olcovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints
    • Eggink G., Engel H., Vriend G., Terpstra P. and Witholt B. (1990) Rubredoxin reductase of Pseudomonas olcovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J. Mol. Biol. 212: 135-142
    • (1990) J. Mol. Biol. , vol.212 , pp. 135-142
    • Eggink, G.1    Engel, H.2    Vriend, G.3    Terpstra, P.4    Witholt, B.5
  • 60
    • 0029809180 scopus 로고    scopus 로고
    • Characterization of the aeg A locus of Escherichia coli: Control of gene expression in response to anaerobiosis and nitrate
    • Cavicchioli R., Kolesnikow T., Chiang R. C. and Gunsalus R. P. (1996) Characterization of the aeg A locus of Escherichia coli: control of gene expression in response to anaerobiosis and nitrate. J. Bacteriol. 178: 6968-6974
    • (1996) J. Bacteriol. , vol.178 , pp. 6968-6974
    • Cavicchioli, R.1    Kolesnikow, T.2    Chiang, R.C.3    Gunsalus, R.P.4
  • 61
    • 0032534879 scopus 로고    scopus 로고
    • Porcine recombinant dihydropyrimidine dehydrogenase: Comparison of the spectroscopic and catalytic properties of the wild-type and C671A mutant enzymes
    • Rosenbaum K., Jahnke K., Curti B., Hagen W. R., Schnackerz K. and Vanoni M. A. (1998) Porcine recombinant dihydropyrimidine dehydrogenase: comparison of the spectroscopic and catalytic properties of the wild-type and C671A mutant enzymes. Biochemistry 37: 17598-17609
    • (1998) Biochemistry , vol.37 , pp. 17598-17609
    • Rosenbaum, K.1    Jahnke, K.2    Curti, B.3    Hagen, W.R.4    Schnackerz, K.5    Vanoni, M.A.6
  • 63
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J., Haeberli P. and Smithies O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12: 387-395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 64
    • 0030919815 scopus 로고    scopus 로고
    • Gene cloning, sequencing and enzymatic properties of glutamate synthase from the hyperthermophilic archaeon Pyrococcus sp. KOD1
    • Jongsareejit B., Rahman R. N. Z. A., Fujiwara S. and Imanaka T. (1997) Gene cloning, sequencing and enzymatic properties of glutamate synthase from the hyperthermophilic archaeon Pyrococcus sp. KOD1. Mol. Gen. Genet. 254: 635-642
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 635-642
    • Jongsareejit, B.1    Rahman, R.N.Z.A.2    Fujiwara, S.3    Imanaka, T.4
  • 65
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk H. P., Clayton R. A., Tomb J. F., White O., Nelson K. E., Ketchum K. A. et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390: 364-370
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3    White, O.4    Nelson, K.E.5    Ketchum, K.A.6
  • 66
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult C. J., White O., Olsen G. J., Zhou L., Fleischmann R. D., Sutton G. G. et al. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273: 1058-1073
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1    White, O.2    Olsen, G.J.3    Zhou, L.4    Fleischmann, R.D.5    Sutton, G.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.