메뉴 건너뛰기




Volumn 38, Issue 1, 2000, Pages 95-114

New sequence motifs in flavoproteins: Evidence for common ancestry and tools to predict structure

Author keywords

Cofactor binding; Dinucleotide; FAD; NAD; NADP; Oxidase; Reductase; Rossman fold

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); AMINO ACID OXIDASE; DIMETHYLANILINE MONOOXYGENASE; DINUCLEOTIDE; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; FUMARATE REDUCTASE; GLUTAMATE SYNTHASE; GLUTATHIONE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PROTOPORPHYRINOGEN OXIDASE; STEROID REDUCTASE; TRANSCORTIN;

EID: 0033970608     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000101)38:1<95::AID-PROT10>3.0.CO;2-A     Document Type: Article
Times cited : (95)

References (99)
  • 1
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann MG, Moras D, Olsen KW. Chemical and biological evolution of nucleotide-binding protein. Nature 1974;250:194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 2
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • Rao ST, Rossmann MG. Comparison of super-secondary structures in proteins. J Mol Biol 1973;76:241-256.
    • (1973) J Mol Biol , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 3
    • 0021095474 scopus 로고
    • Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD-as well as NADPH-binding domains of glutathione reductase
    • Wierenga RK, Drenth J, Schulz GE. Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD-as well as NADPH-binding domains of glutathione reductase. J Mol Biol 1983;167:725-739.
    • (1983) J Mol Biol , vol.167 , pp. 725-739
    • Wierenga, R.K.1    Drenth, J.2    Schulz, G.E.3
  • 5
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz GE. Binding of nucleotides by proteins. Curr Opin Struct Biol 1992;2:61-67.
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 6
    • 0016283234 scopus 로고
    • Structural and functional similarities within the coenzyme binding domains of dehydrogenases
    • Ohlsson I, Nordstrom B, Branden CI. Structural and functional similarities within the coenzyme binding domains of dehydrogenases. J Mol Biol 1974;89:339-354.
    • (1974) J Mol Biol , vol.89 , pp. 339-354
    • Ohlsson, I.1    Nordstrom, B.2    Branden, C.I.3
  • 7
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga RK, Terpstra P, Hol WG. Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint. J Mol Biol 1986;187:101-107.
    • (1986) J Mol Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.3
  • 8
    • 0025295960 scopus 로고
    • Recognition of different nucleotide-binding sites in primary structures using a property-pattern approach
    • Bork P, Grunwald C. Recognition of different nucleotide-binding sites in primary structures using a property-pattern approach. Eur J Biochem 1990;191:347-358.
    • (1990) Eur J Biochem , vol.191 , pp. 347-358
    • Bork, P.1    Grunwald, C.2
  • 9
    • 0026685776 scopus 로고
    • Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold: Implications for nucleotide specificity
    • published erratum appears in J Mol Biol 1993 Aug 5;232:1012
    • Baker PJ, Britton KL, Rice DW, Rob A, Stillman TJ. Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold: implications for nucleotide specificity [published erratum appears in J Mol Biol 1993 Aug 5;232:1012]. J Mol Biol 1992;228:662-671.
    • (1992) J Mol Biol , vol.228 , pp. 662-671
    • Baker, P.J.1    Britton, K.L.2    Rice, D.W.3    Rob, A.4    Stillman, T.J.5
  • 10
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton NS, Berry A, Perham RN. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 1990;343:38-43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 11
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas oleovorans: Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints
    • Eggink G, Engel H, Vriend G, Terpstra P, Witholt B. Rubredoxin reductase of Pseudomonas oleovorans: structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J Mol Biol 1990;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
  • 13
    • 0029056202 scopus 로고
    • An enzyme-substrate complex involved in bacterial cell wall biosynthesis
    • Benson TE, Filman DJ, Walsh CT, Hogle JM. An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nat Struct Biol 1995;2:644-653.
    • (1995) Nat Struct Biol , vol.2 , pp. 644-653
    • Benson, T.E.1    Filman, D.J.2    Walsh, C.T.3    Hogle, J.M.4
  • 14
    • 0009482534 scopus 로고    scopus 로고
    • cDNA sequence of Mα, the catalytic subunit of the Chlamydomonas reinhardtii L-amino acid oxidase (Accession No. U78797): A new sequence motif shared by a wide variety of flavoproteins (PGR97-171)
    • Vallon O, Wollman F-A. cDNA sequence of Mα, the catalytic subunit of the Chlamydomonas reinhardtii L-amino acid oxidase (Accession No. U78797): a new sequence motif shared by a wide variety of flavoproteins (PGR97-171). Plant Physiol 1997;115: 1729.
    • (1997) Plant Physiol , vol.115 , pp. 1729
    • Vallon, O.1    Wollman, F.-A.2
  • 15
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997;25:3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 16
    • 0026100921 scopus 로고
    • A workbench for multiple alignment construction and analysis
    • Schuler GD, Altschul SF, Lipman DJ. A workbench for multiple alignment construction and analysis. Proteins 1991;9:180-190.
    • (1991) Proteins , vol.9 , pp. 180-190
    • Schuler, G.D.1    Altschul, S.F.2    Lipman, D.J.3
  • 17
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 19
    • 0028800055 scopus 로고
    • A visual data flow environment for macromolecular crystallographic computing
    • published erratum appears in J Mol Graph 1995 Dec;13:385
    • Wild DL, Tucker PA, Choe S. A visual data flow environment for macromolecular crystallographic computing [published erratum appears in J Mol Graph 1995 Dec;13:385]. J Mol Graph 1995;13: 291-298, 299-300.
    • (1995) J Mol Graph , vol.13 , pp. 291-298
    • Wild, D.L.1    Tucker, P.A.2    Choe, S.3
  • 20
    • 0028033432 scopus 로고
    • Purification and properties of a novel cytochrome: Flavocytochrome c from Shewanella putrefaciens
    • Morris CJ, Black AC, Pealing SL, et al. Purification and properties of a novel cytochrome: flavocytochrome c from Shewanella putrefaciens. Biochem J 1994;302:587-593.
    • (1994) Biochem J , vol.302 , pp. 587-593
    • Morris, C.J.1    Black, A.C.2    Pealing, S.L.3
  • 21
    • 0032053552 scopus 로고    scopus 로고
    • Thiol:Fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum -Identification of the catalytic sites for fumarate reduction and thiol oxidation
    • Heim S, Kunkel A, Thauer RK, Hedderich R. Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum -identification of the catalytic sites for fumarate reduction and thiol oxidation. Eur J Biochem 1998;253:292-299.
    • (1998) Eur J Biochem , vol.253 , pp. 292-299
    • Heim, S.1    Kunkel, A.2    Thauer, R.K.3    Hedderich, R.4
  • 22
    • 0026752211 scopus 로고
    • Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: A tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria
    • published erratum appears in Biochemistry 1993 Apr 13; 32:3829
    • Pealing SL, Black AC, Manson FD, Ward FB, Chapman SK, Reid GA. Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria [published erratum appears in Biochemistry 1993 Apr 13; 32:3829]. Biochemistry 1992;31:12132-12140.
    • (1992) Biochemistry , vol.31 , pp. 12132-12140
    • Pealing, S.L.1    Black, A.C.2    Manson, F.D.3    Ward, F.B.4    Chapman, S.K.5    Reid, G.A.6
  • 23
    • 0028298547 scopus 로고
    • The covalent attachment of FAD to the flavoprotein of Saccharomyces cerevisiae succinate dehydrogenase is not necessary for import and assembly into mitochondria
    • Robinson KM, Rothery RA, Weiner JH, Lemire BD. The covalent attachment of FAD to the flavoprotein of Saccharomyces cerevisiae succinate dehydrogenase is not necessary for import and assembly into mitochondria. Eur J Biochem 1994;222:983-990.
    • (1994) Eur J Biochem , vol.222 , pp. 983-990
    • Robinson, K.M.1    Rothery, R.A.2    Weiner, J.H.3    Lemire, B.D.4
  • 24
    • 0030037614 scopus 로고    scopus 로고
    • L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: Fumarate oxidoreductase activity
    • Tedeschi G, Negri A, Mortarino M, et al. L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity. Eur J Biochem 1996;239:427-433.
    • (1996) Eur J Biochem , vol.239 , pp. 427-433
    • Tedeschi, G.1    Negri, A.2    Mortarino, M.3
  • 25
    • 0030018052 scopus 로고    scopus 로고
    • L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition
    • Mortarino M, Negri A, Tedeschi, et al. L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Eur J Biochem 1996;239:418-426.
    • (1996) Eur J Biochem , vol.239 , pp. 418-426
    • Mortarino, M.1    Negri, A.2    Tedeschi3
  • 26
    • 0027288794 scopus 로고
    • Characterization of the baiH gene encoding a bile acid-inducible NADH:Flavin oxidoreductase from Eubacterium sp. strain VPI 12708
    • Franklund CV, Baron SF, Hylemon PB. Characterization of the baiH gene encoding a bile acid-inducible NADH:flavin oxidoreductase from Eubacterium sp. strain VPI 12708. J Bacteriol 1993;175: 3002-3012.
    • (1993) J Bacteriol , vol.175 , pp. 3002-3012
    • Franklund, C.V.1    Baron, S.F.2    Hylemon, P.B.3
  • 27
    • 0022982155 scopus 로고
    • Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-A resolution
    • Lim LW, Shamala N, Mathews FS, Steenkamp DJ, Hamlin R, Xuong NH. Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-A resolution. J Biol Chem 1986;261:15140-15146.
    • (1986) J Biol Chem , vol.261 , pp. 15140-15146
    • Lim, L.W.1    Shamala, N.2    Mathews, F.S.3    Steenkamp, D.J.4    Hamlin, R.5    Xuong, N.H.6
  • 28
    • 0026739339 scopus 로고
    • Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase
    • Barber MJ, Neame PJ, Lim LW, White S, Matthews FS. Correlation of x-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase. J Biol Chem 1992;267:6611-6619.
    • (1992) J Biol Chem , vol.267 , pp. 6611-6619
    • Barber, M.J.1    Neame, P.J.2    Lim, L.W.3    White, S.4    Matthews, F.S.5
  • 29
    • 0023831537 scopus 로고
    • Identification of ADP in the iron-sulfur flavoprotein trimethylamine dehydrogenase
    • Lim LW, Mathews FS. Steenkamp DJ. Identification of ADP in the iron-sulfur flavoprotein trimethylamine dehydrogenase. J Biol Chem 1988;263:3075-3078.
    • (1988) J Biol Chem , vol.263 , pp. 3075-3078
    • Lim, L.W.1    Mathews, F.S.2    Steenkamp, D.J.3
  • 31
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm L, Sander C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res 1998;26:318-321.
    • (1998) Nucleic Acids Res , vol.26 , pp. 318-321
    • Holm, L.1    Sander, C.2
  • 32
    • 0026795398 scopus 로고
    • Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1: Comparison with NADH peroxidase and the flavoprotein disulfide reductases
    • Ross RP, Claiborne A. Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1: comparison with NADH peroxidase and the flavoprotein disulfide reductases. J Mol Biol 1992;227:658-671.
    • (1992) J Mol Biol , vol.227 , pp. 658-671
    • Ross, R.P.1    Claiborne, A.2
  • 33
    • 0029810580 scopus 로고    scopus 로고
    • Covalent structure of the flavoprotein subunit of the flavocytochrome c: Sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum
    • Van Driessche G, Koh M, Chen ZW, et al. Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum. Protein Sci 1996;5:1753-1764.
    • (1996) Protein Sci , vol.5 , pp. 1753-1764
    • Van Driessche, G.1    Koh, M.2    Chen, Z.W.3
  • 34
    • 0028519153 scopus 로고
    • The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium
    • Chen ZW, Koh M, Van Driessche G, et al. The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium. Science 1994;266:430-432.
    • (1994) Science , vol.266 , pp. 430-432
    • Chen, Z.W.1    Koh, M.2    Van Driessche, G.3
  • 35
    • 0029944499 scopus 로고    scopus 로고
    • Structure and mutational analysis of Rab GDP-dissociation inhibitor
    • Schalk I, Zeng K, Wu SK, et al. Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 1996;381:42-48.
    • (1996) Nature , vol.381 , pp. 42-48
    • Schalk, I.1    Zeng, K.2    Wu, S.K.3
  • 36
    • 0029868602 scopus 로고    scopus 로고
    • Human choroideremia protein contains a FAD-binding domain
    • published erratum appears in Nat Genet 1996 Apr;12:458
    • Koonin EV. Human choroideremia protein contains a FAD-binding domain [published erratum appears in Nat Genet 1996 Apr;12:458]. Nat Genet 1996;12:237-239.
    • (1996) Nat Genet , vol.12 , pp. 237-239
    • Koonin, E.V.1
  • 37
    • 0030446448 scopus 로고    scopus 로고
    • Structural insights into the function of the Rab GDI superfamily
    • Wu SK, Zeng K, Wilson IA, Balch WE. Structural insights into the function of the Rab GDI superfamily. Trends Biochem Sci 1996;21: 472-476.
    • (1996) Trends Biochem Sci , vol.21 , pp. 472-476
    • Wu, S.K.1    Zeng, K.2    Wilson, I.A.3    Balch, W.E.4
  • 38
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution
    • Vrielink A, Lloyd LF, Blow DM. Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution. J Mol Biol 1991;219:533-554.
    • (1991) J Mol Biol , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 39
    • 0027397187 scopus 로고
    • Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 Å resolution
    • Hecht HJ, Kalisz HM, Hendle J, Schmid RD, Schomburg D. Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 Å resolution. J Mol Biol 1993;229:153-172.
    • (1993) J Mol Biol , vol.229 , pp. 153-172
    • Hecht, H.J.1    Kalisz, H.M.2    Hendle, J.3    Schmid, R.D.4    Schomburg, D.5
  • 40
    • 0026544690 scopus 로고
    • GMC oxidoreductases: A newly defined family of homologous proteins with diverse catalytic activities
    • Cavener DR. GMC oxidoreductases: a newly defined family of homologous proteins with diverse catalytic activities. J Mol Biol 1992;223:811-814.
    • (1992) J Mol Biol , vol.223 , pp. 811-814
    • Cavener, D.R.1
  • 41
    • 0027432601 scopus 로고
    • Crystal structure of cholesterol oxidase complexed with a steroid substrate: Implications for flavin adenine dinucleotide dependent alcohol oxidases
    • Li J, Vrielink A, Brick P, Blow DM. Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases. Biochemistry 1993;32:11507-11515.
    • (1993) Biochemistry , vol.32 , pp. 11507-11515
    • Li, J.1    Vrielink, A.2    Brick, P.3    Blow, D.M.4
  • 42
    • 0030034322 scopus 로고    scopus 로고
    • A glutathione reductase-like flavoenzyme of the malaria parasite Plasmodium falciparum: Structural considerations based on the DNA sequence
    • Becker K, Muller S, Keese MA, Walter RD, Schirmer RH. A glutathione reductase-like flavoenzyme of the malaria parasite Plasmodium falciparum: structural considerations based on the DNA sequence. Biochem Soc Trans 1996;24:67-72.
    • (1996) Biochem Soc Trans , vol.24 , pp. 67-72
    • Becker, K.1    Muller, S.2    Keese, M.A.3    Walter, R.D.4    Schirmer, R.H.5
  • 43
    • 0029001789 scopus 로고
    • Structure and mechanism of parahydroxybenzoate hydroxylase
    • Entsch B, van Berkel WJ. Structure and mechanism of parahydroxybenzoate hydroxylase. FASEB J 1995;9:476-483.
    • (1995) FASEB J , vol.9 , pp. 476-483
    • Entsch, B.1    Van Berkel, W.J.2
  • 44
    • 0032524753 scopus 로고    scopus 로고
    • The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
    • Enroth C, Neujahr H, Schneider G, Lindqvist Y. The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis. Structure. 1998;6:605-617.
    • (1998) Structure , vol.6 , pp. 605-617
    • Enroth, C.1    Neujahr, H.2    Schneider, G.3    Lindqvist, Y.4
  • 45
    • 0029780471 scopus 로고    scopus 로고
    • Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 Å resolution
    • Mizutani H, Miyahara I, Hirotsu K, et al. Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 Å resolution. J Biochem (Tokyo) 1996;120:14-17.
    • (1996) J Biochem (Tokyo) , vol.120 , pp. 14-17
    • Mizutani, H.1    Miyahara, I.2    Hirotsu, K.3
  • 46
    • 0028051740 scopus 로고
    • Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: The single-domain reductases/epimerases/dehydrogenases (the 'RED' family)
    • Labesse G, Vidal-Cros A, Chomilier J, Gaudry M, Mornon JP. Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: the single-domain reductases/epimerases/dehydrogenases (the 'RED' family). Biochem J 1994;304:95-99.
    • (1994) Biochem J , vol.304 , pp. 95-99
    • Labesse, G.1    Vidal-Cros, A.2    Chomilier, J.3    Gaudry, M.4    Mornon, J.P.5
  • 47
    • 0017881332 scopus 로고
    • The alpha-helix dipole and the properties of proteins
    • Hol WG, van Duijnen PT, Berendsen H. The alpha-helix dipole and the properties of proteins. Nature 1978;273:443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.1    Van Duijnen, P.T.2    Berendsen, H.3
  • 48
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moietites with α-helices in dinucleotide binding proteins
    • Wierenga RK, De Maeyer MCH, Hol WG. Interaction of pyrophosphate moietites with α-helices in dinucleotide binding proteins. Biochemistry 1985;24:1346-1357.
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.3
  • 49
    • 0026060723 scopus 로고
    • Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes
    • McKie JH, Douglas KT. Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes. FEBS Lett. 1991;279:5-8.
    • (1991) FEBS Lett. , vol.279 , pp. 5-8
    • McKie, J.H.1    Douglas, K.T.2
  • 50
    • 0024042954 scopus 로고
    • cDNA cloning of human liver monoamine oxidase A and B: Molecular basis of differences in enzymatic properties
    • Bach AW, Lan NC, Johnson DL, et al. cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci USA 1988;85:4934-4938.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4934-4938
    • Bach, A.W.1    Lan, N.C.2    Johnson, D.L.3
  • 51
    • 0025900043 scopus 로고
    • Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis
    • Schroder I, Gunsalus RP, Ackrell BA, Cochran B, Cecchini G. Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis. J Biol Chem 1991;266: 13572-13579.
    • (1991) J Biol Chem , vol.266 , pp. 13572-13579
    • Schroder, I.1    Gunsalus, R.P.2    Ackrell, B.A.3    Cochran, B.4    Cecchini, G.5
  • 52
    • 0025606274 scopus 로고
    • Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708
    • Mallonee DH, White WB, Hylemon PB. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J Bacteriol 1990;172:7011-7019.
    • (1990) J Bacteriol , vol.172 , pp. 7011-7019
    • Mallonee, D.H.1    White, W.B.2    Hylemon, P.B.3
  • 53
    • 0030885424 scopus 로고    scopus 로고
    • Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli
    • He XY, Yang SY, Schulz H. Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. Eur J Biochem 1997;248: 516-520.
    • (1997) Eur J Biochem , vol.248 , pp. 516-520
    • He, X.Y.1    Yang, S.Y.2    Schulz, H.3
  • 54
    • 0025064564 scopus 로고
    • Molecular cloning of the L-amino-acid oxidase gene from Neurospora crassa
    • Niedermann DM, Lerch K. Molecular cloning of the L-amino-acid oxidase gene from Neurospora crassa. J Biol Chem 1990;265: 17246-17251.
    • (1990) J Biol Chem , vol.265 , pp. 17246-17251
    • Niedermann, D.M.1    Lerch, K.2
  • 55
    • 0029609718 scopus 로고
    • Partial amino acid sequence of an L-amino acid oxidase from the cyanobacterium Synechococcus PCC6301, cloning and DNA sequence analysis of the aoxA gene
    • Bockholt R, Masepohl B, Kruft V, Wittmann-Liebold B, Pistorius EK. Partial amino acid sequence of an L-amino acid oxidase from the cyanobacterium Synechococcus PCC6301, cloning and DNA sequence analysis of the aoxA gene. Biochim Biophys Acta 1995; 1264:289-293.
    • (1995) Biochim Biophys Acta , vol.1264 , pp. 289-293
    • Bockholt, R.1    Masepohl, B.2    Kruft, V.3    Wittmann-Liebold, B.4    Pistorius, E.K.5
  • 56
    • 0032581385 scopus 로고    scopus 로고
    • Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein
    • Raibekas AA, Massey V. Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein. Biochem Biophys Res Commun 1998;248:476-478.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 476-478
    • Raibekas, A.A.1    Massey, V.2
  • 57
    • 0030903762 scopus 로고    scopus 로고
    • Fig1, an interleukin 4-induced mouse B cell gene isolated by cDNA representational difference analysis
    • Chu CC, Paul WE. Fig1, an interleukin 4-induced mouse B cell gene isolated by cDNA representational difference analysis. Proc Natl Acad Sci USA 1997;94:2507-2512.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2507-2512
    • Chu, C.C.1    Paul, W.E.2
  • 59
    • 0029561752 scopus 로고
    • Molecular cloning of the defense factor in the albumen gland of the sea hare Aplysia kurodai
    • Takamatsu N, Shiba T, Muramoto K, Kamiya H. Molecular cloning of the defense factor in the albumen gland of the sea hare Aplysia kurodai. FEBS Lett 1995;27:373-376.
    • (1995) FEBS Lett , vol.27 , pp. 373-376
    • Takamatsu, N.1    Shiba, T.2    Muramoto, K.3    Kamiya, H.4
  • 60
    • 0027479446 scopus 로고
    • Cloning and expression of the gene from Candida albicans that encodes a high-affinity corticosteroid-binding protein
    • Malloy PJ, Zhao X, Madani ND, Feldman D. Cloning and expression of the gene from Candida albicans that encodes a high-affinity corticosteroid-binding protein. Proc Natl Acad Sci USA 1993;90:1902-1906.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1902-1906
    • Malloy, P.J.1    Zhao, X.2    Madani, N.D.3    Feldman, D.4
  • 61
    • 0029658939 scopus 로고    scopus 로고
    • Characterization of the saccharomyces cerevisiae FMS1 gene related to Candida albicans corticosteroid-binding protein 1
    • Joets J, Pousset D, Marcireau C, Karst F. Characterization of the saccharomyces cerevisiae FMS1 gene related to Candida albicans corticosteroid-binding protein 1. Curr Genet 1996;30:115-120.
    • (1996) Curr Genet , vol.30 , pp. 115-120
    • Joets, J.1    Pousset, D.2    Marcireau, C.3    Karst, F.4
  • 62
    • 0027516803 scopus 로고
    • Putrescine oxidase of Micrococcus rubens: Primary structure and Escherichia coli
    • Ishizuka H, Horinouchi S, Beppu T. Putrescine oxidase of Micrococcus rubens: primary structure and Escherichia coli. J Gen Microbiol 1993;139:425-432.
    • (1993) J Gen Microbiol , vol.139 , pp. 425-432
    • Ishizuka, H.1    Horinouchi, S.2    Beppu, T.3
  • 63
    • 0028999344 scopus 로고
    • Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger
    • Schilling B, Lerch K. Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger. Mol Gen Genet 1995;247:430-438.
    • (1995) Mol Gen Genet , vol.247 , pp. 430-438
    • Schilling, B.1    Lerch, K.2
  • 64
    • 0026134277 scopus 로고
    • The TR-DNA region carrying the auxin synthesis genes of the Agrobacterium rhizogenes agropine-type plasmid pRiA4: Nucleotide sequence analysis and introduction into tobacco plants
    • Camilleri C, Jouanin L. The TR-DNA region carrying the auxin synthesis genes of the Agrobacterium rhizogenes agropine-type plasmid pRiA4: nucleotide sequence analysis and introduction into tobacco plants. Mol Plant-Microbe Interact 1991;4:155-162.
    • (1991) Mol Plant-Microbe Interact , vol.4 , pp. 155-162
    • Camilleri, C.1    Jouanin, L.2
  • 65
    • 0028984991 scopus 로고
    • Purification and characterization of the flavoprotein tryptophan 2-monooxygenase expressed at high levels in Escherichia coli
    • Emanuele JJ, Heasley CJ, Fitzpatrick PF. Purification and characterization of the flavoprotein tryptophan 2-monooxygenase expressed at high levels in Escherichia coli. Arch Biochem Biophys 1995;316:241-248.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 241-248
    • Emanuele, J.J.1    Heasley, C.J.2    Fitzpatrick, P.F.3
  • 66
    • 0026697885 scopus 로고
    • Characterization and molecular cloning of a flavoprotein catalyzing the synthesis of phytofluene and zeta-carotene in Capsicum chromoplasts
    • Hugueney P, Romer S, Kuntz M, Camara B. Characterization and molecular cloning of a flavoprotein catalyzing the synthesis of phytofluene and zeta-carotene in Capsicum chromoplasts. Eur J Biochem 1992;209:399-407.
    • (1992) Eur J Biochem , vol.209 , pp. 399-407
    • Hugueney, P.1    Romer, S.2    Kuntz, M.3    Camara, B.4
  • 67
    • 0030008047 scopus 로고    scopus 로고
    • Biochemical characterization of purified zeta-carotene desaturase from Anabaena PCC 7120 after expression in Escherichia coli
    • Albrecht M, Linden H, Sandmann G. Biochemical characterization of purified zeta-carotene desaturase from Anabaena PCC 7120 after expression in Escherichia coli. Eur J Biochem 1996;236: 115-120.
    • (1996) Eur J Biochem , vol.236 , pp. 115-120
    • Albrecht, M.1    Linden, H.2    Sandmann, G.3
  • 68
    • 0027991862 scopus 로고
    • Isolation, sequence, and characterization of the Cercospora nicotianae phytoene dehydrogenase gene
    • Ehrenshaft M, Daub ME. Isolation, sequence, and characterization of the Cercospora nicotianae phytoene dehydrogenase gene. Appl Environ Microbiol 1994;60:2766-2771.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2766-2771
    • Ehrenshaft, M.1    Daub, M.E.2
  • 69
    • 0027120331 scopus 로고
    • Nucleotide sequence of the methoxyneurosporene dehydrogenase gene from Rhodobacter sphaeroides: Comparison with other bacterial carotenoid dehydrogenases
    • Gari E, Toledo JC, Gibert I, Barbe J. Nucleotide sequence of the methoxyneurosporene dehydrogenase gene from Rhodobacter sphaeroides: comparison with other bacterial carotenoid dehydrogenases. FEMS Microbiol Lett 1992;72:103-108.
    • (1992) FEMS Microbiol Lett , vol.72 , pp. 103-108
    • Gari, E.1    Toledo, J.C.2    Gibert, I.3    Barbe, J.4
  • 70
    • 0027971410 scopus 로고
    • Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus
    • Wieland B, Feil C, Gloria-Maercker E. Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus. J Bacteriol 1994;176: 7719-7726.
    • (1994) J Bacteriol , vol.176 , pp. 7719-7726
    • Wieland, B.1    Feil, C.2    Gloria-Maercker, E.3
  • 71
    • 0030012328 scopus 로고    scopus 로고
    • Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides
    • Camadro JM, Labbe P. Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides. J Biol Chem 1996;271: 9120-9128.
    • (1996) J Biol Chem , vol.271 , pp. 9120-9128
    • Camadro, J.M.1    Labbe, P.2
  • 72
    • 0028174034 scopus 로고
    • Expression of a cloned protoporphyrinogen oxidase
    • Dailey TA, Meissner P, Dailey HA. Expression of a cloned protoporphyrinogen oxidase. J Biol Chem 1994;269:813-815.
    • (1994) J Biol Chem , vol.269 , pp. 813-815
    • Dailey, T.A.1    Meissner, P.2    Dailey, H.A.3
  • 73
    • 0027421397 scopus 로고
    • General resistance to sterol biosynthesis inhibitors in Saccharomyces cerevisiae
    • Ladeveze V, Marcireau C, Delourme D, Karst F. General resistance to sterol biosynthesis inhibitors in Saccharomyces cerevisiae. Lipids 1993;28:907-912.
    • (1993) Lipids , vol.28 , pp. 907-912
    • Ladeveze, V.1    Marcireau, C.2    Delourme, D.3    Karst, F.4
  • 74
    • 0028167946 scopus 로고
    • Nmt2 of fission yeast: A second thiamine-repressible gene co-ordinately regulated with nmtl
    • Manetti AG, Rosetto M, Maundrell KG. nmt2 of fission yeast: a second thiamine-repressible gene co-ordinately regulated with nmtl. Yeast 1994;10:1075-1082.
    • (1994) Yeast , vol.10 , pp. 1075-1082
    • Manetti, A.G.1    Rosetto, M.2    Maundrell, K.G.3
  • 75
    • 0026767435 scopus 로고
    • MOL1, a Saccharomyces cerevisiae gene that is highly expressed in early stationary phase during growth on molasses
    • Praekelt UM, Meacock PA. MOL1, a Saccharomyces cerevisiae gene that is highly expressed in early stationary phase during growth on molasses. Yeast 1992;8:699-710.
    • (1992) Yeast , vol.8 , pp. 699-710
    • Praekelt, U.M.1    Meacock, P.A.2
  • 78
    • 0027281825 scopus 로고
    • Genetic organization and sequence of the rfb gene cluster of Yersinia enterocolitica serotype o:3: Similarities to the dTDP-L-rhamnose biosynthesis pathway of Salmonella and to the bacterial polysaccharide transport systems
    • Zhang L, al-Hendy A, Toivanen P, Skurnik M. Genetic organization and sequence of the rfb gene cluster of Yersinia enterocolitica serotype O:3: similarities to the dTDP-L-rhamnose biosynthesis pathway of Salmonella and to the bacterial polysaccharide transport systems. Mol Microbiol 1993;9:309-321.
    • (1993) Mol Microbiol , vol.9 , pp. 309-321
    • Zhang, L.1    Al-Hendy, A.2    Toivanen, P.3    Skurnik, M.4
  • 79
    • 0028303288 scopus 로고
    • Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: Identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a
    • Yao Z, Valvano MA. Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a. J Bacteriol 1994;176:4133-4143.
    • (1994) J Bacteriol , vol.176 , pp. 4133-4143
    • Yao, Z.1    Valvano, M.A.2
  • 80
    • 0030608184 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding the soluble fumarate reductase from Saccharomyces cerevisiae
    • Enomoto K, Ohki R, Muratsubaki H. Cloning and sequencing of the gene encoding the soluble fumarate reductase from Saccharomyces cerevisiae. DNA Res 1996;3:263-267.
    • (1996) DNA Res , vol.3 , pp. 263-267
    • Enomoto, K.1    Ohki, R.2    Muratsubaki, H.3
  • 81
    • 0025748721 scopus 로고
    • Cloning, sequencing, and expression of the Pseudomonas testosteroni gene encoding 3-oxosteroid delta 1-dehydrogenase
    • Plesiat P, Grandguillot M, Harayama S, Vragar S, Michel-Briand Y. Cloning, sequencing, and expression of the Pseudomonas testosteroni gene encoding 3-oxosteroid delta 1-dehydrogenase. J Bacteriol 1991;173:7219-7227.
    • (1991) J Bacteriol , vol.173 , pp. 7219-7227
    • Plesiat, P.1    Grandguillot, M.2    Harayama, S.3    Vragar, S.4    Michel-Briand, Y.5
  • 82
    • 0029895848 scopus 로고    scopus 로고
    • Comamonas testosteroni 3-ketosteroid-delta4(5alpha)-dehydrogenase: Gene and protein characterization
    • Florin C, Kohler T, Grandguillot M, Plesiat P. Comamonas testosteroni 3-ketosteroid-delta4(5alpha)-dehydrogenase: gene and protein characterization. J Bacteriol 1996;178:3322-3330.
    • (1996) J Bacteriol , vol.178 , pp. 3322-3330
    • Florin, C.1    Kohler, T.2    Grandguillot, M.3    Plesiat, P.4
  • 83
    • 0015523879 scopus 로고
    • Glutamate synthase from Escherichia coli : An iron-sulfide flavoprotein
    • Miller RE, Stadtman ER. Glutamate synthase from Escherichia coli : an iron-sulfide flavoprotein. J Biol Chem 1972;247:7407-7419.
    • (1972) J Biol Chem , vol.247 , pp. 7407-7419
    • Miller, R.E.1    Stadtman, E.R.2
  • 84
    • 0027550316 scopus 로고
    • Molecular characterization of NADH-dependent glutamate synthase from alfalfa nodules
    • Gregerson RG, Miller SS, Twary SN, Gantt JS, Vance CP. Molecular characterization of NADH-dependent glutamate synthase from alfalfa nodules. Plant Cell 1993;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
  • 87
    • 0029809180 scopus 로고    scopus 로고
    • Characterization of the aegA locus of Escherichia coli: Control of gene expression in response to anaerobiosis and nitrate
    • Cavicchioli R, Kolesnikow T, Chiang RC, Gunsalus RP. Characterization of the aegA locus of Escherichia coli: control of gene expression in response to anaerobiosis and nitrate. J Bacteriol 1996;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
  • 88
    • 0030471750 scopus 로고    scopus 로고
    • cDNA cloning of bovine liver dihydropyrimidine dehydrogenase
    • Albin N, Johnson MR, Diasio RB. cDNA cloning of bovine liver dihydropyrimidine dehydrogenase. DNA Seq 1996;6:243-250.
    • (1996) DNA Seq , vol.6 , pp. 243-250
    • Albin, N.1    Johnson, M.R.2    Diasio, R.B.3
  • 89
    • 0028302414 scopus 로고
    • A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities
    • Lawton MP, Cashman JR, Cresteil T, et al. A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities. Arch Biochem Biophys 1994;308: 254-257.
    • (1994) Arch Biochem Biophys , vol.308 , pp. 254-257
    • Lawton, M.P.1    Cashman, J.R.2    Cresteil, T.3
  • 90
    • 0027315840 scopus 로고
    • Cloning, sequencing, distribution, and expression in Escherichia coli of flavin-containing monooxygenase 1C1: Evidence for a third gene subfamily in rabbits
    • Atta-Asafo-Adjei E, Lawton MP, Philpot RM. Cloning, sequencing, distribution, and expression in Escherichia coli of flavin-containing monooxygenase 1C1: evidence for a third gene subfamily in rabbits. J Biol Chem 1993;268:9681-9689.
    • (1993) J Biol Chem , vol.268 , pp. 9681-9689
    • Atta-Asafo-Adjei, E.1    Lawton, M.P.2    Philpot, R.M.3
  • 91
    • 0030589542 scopus 로고    scopus 로고
    • Molecular cloning and kinetic characterization of a flavin-containing monooxygenase from Saccharomyces cerevisiae
    • Suh JK, Poulsen LL, Ziegler DM, Robertus JD. Molecular cloning and kinetic characterization of a flavin-containing monooxygenase from Saccharomyces cerevisiae. Arch Biochem Biophys 1996; 336:268-274.
    • (1996) Arch Biochem Biophys , vol.336 , pp. 268-274
    • Suh, J.K.1    Poulsen, L.L.2    Ziegler, D.M.3    Robertus, J.D.4
  • 92
    • 0023958999 scopus 로고
    • Acinetobacter cyclohexanone monooxygenase: Gene cloning and sequence determination
    • Chen YC, Peoples OP, Walsh CT. Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence determination. J Bacteriol 1988;170:781-789.
    • (1988) J Bacteriol , vol.170 , pp. 781-789
    • Chen, Y.C.1    Peoples, O.P.2    Walsh, C.T.3
  • 93
    • 0029912229 scopus 로고    scopus 로고
    • Twenty-five coregulated transcripts define a sterigmatocystin gene cluster in Aspergillus nidulans
    • Brown DW, Yu JH, Kelkar HS, et al. Twenty-five coregulated transcripts define a sterigmatocystin gene cluster in Aspergillus nidulans. Proc Natl Acad Sci USA 1996;93:1418-1422.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1418-1422
    • Brown, D.W.1    Yu, J.H.2    Kelkar, H.S.3
  • 94
    • 0027250514 scopus 로고
    • Cloning, sequencing and expression of the gene encoding NADH oxidase from the extreme anaerobic thermophile Thermoanaeroblum brockli
    • Liu XL, Scopes RK. Cloning, sequencing and expression of the gene encoding NADH oxidase from the extreme anaerobic thermophile Thermoanaeroblum brockli. Biochim Biophys Acta 1993;1174: 187-190.
    • (1993) Biochim Biophys Acta , vol.1174 , pp. 187-190
    • Liu, X.L.1    Scopes, R.K.2
  • 95
    • 0026696303 scopus 로고
    • Trimethylamine dehydrogenase of bacterium W3A1: Molecular cloning, sequence determination and over-expression of the gene
    • Boyd G, Mathews FS, Packman LC, Scrutton NS. Trimethylamine dehydrogenase of bacterium W3A1: molecular cloning, sequence determination and over-expression of the gene. FEBS Lett 1992; 308:271-276.
    • (1992) FEBS Lett , vol.308 , pp. 271-276
    • Boyd, G.1    Mathews, F.S.2    Packman, L.C.3    Scrutton, N.S.4
  • 96
    • 0029166692 scopus 로고
    • The primary structure of Hyphomicrobium X dimethylamine dehydrogenase: Relationship to trimethylamine dehydrogenase and implications for substrate recognition
    • Yang CC, Packman LC, Scrutton NS. The primary structure of Hyphomicrobium X dimethylamine dehydrogenase: relationship to trimethylamine dehydrogenase and implications for substrate recognition. Eur J Biochem 1995;232:264-271.
    • (1995) Eur J Biochem , vol.232 , pp. 264-271
    • Yang, C.C.1    Packman, L.C.2    Scrutton, N.S.3
  • 97
    • 0028875230 scopus 로고
    • The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein
    • Huang L, Rohlfs RJ, Hille R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. J Biol Chem 1995;270:23958-23965.
    • (1995) J Biol Chem , vol.270 , pp. 23958-23965
    • Huang, L.1    Rohlfs, R.J.2    Hille, R.3
  • 98
    • 0027412184 scopus 로고
    • Glutamate synthase genes of the diazotroph Azospirillum brasilense: Cloning, sequencing, and analysis of functional domains
    • Pelanda R, Vanoni MA, Perego M, et al. Glutamate synthase genes of the diazotroph Azospirillum brasilense: cloning, sequencing, and analysis of functional domains. J Biol Chem 1993;268: 3099-3106.
    • (1993) J Biol Chem , vol.268 , pp. 3099-3106
    • Pelanda, R.1    Vanoni, M.A.2    Perego, M.3
  • 99
    • 0026508060 scopus 로고
    • Evidence that the methylesterase of bacterial chemotaxis may be a serine hydrolase
    • Krueger JK, Stock J, Schutt CE. Evidence that the methylesterase of bacterial chemotaxis may be a serine hydrolase. Biochim Biophys Acta 1992;1119:322-326.
    • (1992) Biochim Biophys Acta , vol.1119 , pp. 322-326
    • Krueger, J.K.1    Stock, J.2    Schutt, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.