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Volumn 221, Issue 1-2, 2001, Pages 117-126

Purification and characterization of β-methylaspartase from Fusobacterium varium

Author keywords

methylaspartase; Characterization; Fusobacterium; Purification; Stereochemistry

Indexed keywords

FUSOBACTERIUM; FUSOBACTERIUM VARIUM;

EID: 0035346461     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010938111292     Document Type: Article
Times cited : (5)

References (55)
  • 1
    • 0001957353 scopus 로고
    • Proton transfer, acid-base catalysis, and enzymatic hydrolysis
    • Eigen M: Proton transfer, acid-base catalysis, and enzymatic hydrolysis. Angew Chem Int Ed Engl 3: 1-19, 1964
    • (1964) Angew Chem Int Ed Engl , vol.3 , pp. 1-19
    • Eigen, M.1
  • 2
    • 0000738729 scopus 로고
    • Application of the Marcus relation to concerted proton transfers
    • Albery WJ: Application of the Marcus relation to concerted proton transfers. J Chem Soc Faraday Trans 1 78: 1579-1590, 1982
    • (1982) J Chem Soc Faraday Trans 1 , vol.78 , pp. 1579-1590
    • Albery, W.J.1
  • 3
    • 0001213231 scopus 로고
    • Ketonization of acetophenone enol in aqueous buffer solutions. Rate-equilibrium relations and mechanism of the 'uncatalyzed' reaction
    • Chiang Y, Kresge AJ, Santaballa JA, Wirz J: Ketonization of acetophenone enol in aqueous buffer solutions. Rate-equilibrium relations and mechanism of the 'uncatalyzed' reaction. J Am Chem Soc 110: 5506-5510, 1988
    • (1988) J Am Chem Soc , vol.110 , pp. 5506-5510
    • Chiang, Y.1    Kresge, A.J.2    Santaballa, J.A.3    Wirz, J.4
  • 4
    • 5244358350 scopus 로고
    • Generation and study of enols and other reactive species
    • Kresge AJ: Generation and study of enols and other reactive species. Pure Appl Chem 63: 213-221, 1991
    • (1991) Pure Appl Chem , vol.63 , pp. 213-221
    • Kresge, A.J.1
  • 5
    • 0030567338 scopus 로고    scopus 로고
    • a of ethyl acetate: Brønsted correlation for deprotonation of a simple oxygen ester in aqueous solution
    • a of ethyl acetate: Brønsted correlation for deprotonation of a simple oxygen ester in aqueous solution. J Am Chem Soc 118: 3129-3141, 1996
    • (1996) J Am Chem Soc , vol.118 , pp. 3129-3141
    • Amyes, T.L.1    Richard, J.P.2
  • 7
    • 0013561355 scopus 로고
    • Catalytic mechanism and active site structure of methylaspartate ammonia-lyase: Possible involvement of an electrophilic dehydroalanine reaction centre
    • S.M. Roberts (ed). RSC Special Publication 111, Royal Society of Chemistry, London
    • Botting NP, Akhtar M, Archer CH, Cohen MA, Thomas NR, Goda S, Minton NP, Gani D: Catalytic mechanism and active site structure of methylaspartate ammonia-lyase: Possible involvement of an electrophilic dehydroalanine reaction centre. In: S.M. Roberts (ed). Molecular Recognition: Chemical and Biochemical Problems II. RSC Special Publication 111, Royal Society of Chemistry, London, 1992, pp 95-109
    • (1992) Molecular Recognition: Chemical and Biochemical Problems II , pp. 95-109
    • Botting, N.P.1    Akhtar, M.2    Archer, C.H.3    Cohen, M.A.4    Thomas, N.R.5    Goda, S.6    Minton, N.P.7    Gani, D.8
  • 8
    • 0001508740 scopus 로고    scopus 로고
    • Mechanism of 3-methylaspartase probed using deuterium and solvent isotope effects and active-site directed reagents: Identification of an essential cysteine residue
    • Pollard JR, Richardson S, Akhtar M, Lasry P, Neal T, Botting NP, Gani D: Mechanism of 3-methylaspartase probed using deuterium and solvent isotope effects and active-site directed reagents: Identification of an essential cysteine residue. Bioorg Med Chem 7: 949-975, 1999
    • (1999) Bioorg Med Chem , vol.7 , pp. 949-975
    • Pollard, J.R.1    Richardson, S.2    Akhtar, M.3    Lasry, P.4    Neal, T.5    Botting, N.P.6    Gani, D.7
  • 9
    • 0001537887 scopus 로고    scopus 로고
    • 15N-isotope effects for three substrates: A flip from a concerted to a carbocationic amino-enzyme elimination mechanism upon changing the C-3 stereochemistry in the substrate from R to S
    • 15N-isotope effects for three substrates: A flip from a concerted to a carbocationic amino-enzyme elimination mechanism upon changing the C-3 stereochemistry in the substrate from R to S. Bioorg Med Chem 7: 977-990, 1999
    • (1999) Bioorg Med Chem , vol.7 , pp. 977-990
    • Gani, D.1    Archer, C.H.2    Botting, N.P.3    Pollard, J.R.4
  • 10
    • 0014670950 scopus 로고
    • Dehydroalanine in histidine ammonia-lyase
    • Wickner RB : Dehydroalanine in histidine ammonia-lyase. J Biol Chem 244: 6550-6552, 1969
    • (1969) J Biol Chem , vol.244 , pp. 6550-6552
    • Wickner, R.B.1
  • 11
    • 0021960593 scopus 로고
    • Presence and quantity of dehydroalanine in histidine ammonia-lyase from Pseudomonas putida
    • Consevage MW, Phillips AT: Presence and quantity of dehydroalanine in histidine ammonia-lyase from Pseudomonas putida. Biochemistry 24: 301-308, 1985
    • (1985) Biochemistry , vol.24 , pp. 301-308
    • Consevage, M.W.1    Phillips, A.T.2
  • 12
    • 0028246559 scopus 로고
    • Identification of serine 143 as the most likely precursor of dehydroalanine in the active site of histidine ammonia-lyase. A study of the overexpressed enzyme by site-directed mutagenesis
    • Langer M, Reck G, Reed J, Rétey J: Identification of serine 143 as the most likely precursor of dehydroalanine in the active site of histidine ammonia-lyase. A study of the overexpressed enzyme by site-directed mutagenesis. Biochemistry 33: 6462-6467, 1994
    • (1994) Biochemistry , vol.33 , pp. 6462-6467
    • Langer, M.1    Reck, G.2    Reed, J.3    Rétey, J.4
  • 13
    • 0028033826 scopus 로고
    • Histidine ammonia-lyase mutant S143C is post-translationally converted into fully active wild-type enzyme. Evidence for serine 143 to be the precursor of active site dehydroalanine
    • Langer M, Lieber A, Rétey J: Histidine ammonia-lyase mutant S143C is post-translationally converted into fully active wild-type enzyme. Evidence for serine 143 to be the precursor of active site dehydroalanine. Biochemistry 33: 14034-14038, 1994
    • (1994) Biochemistry , vol.33 , pp. 14034-14038
    • Langer, M.1    Lieber, A.2    Rétey, J.3
  • 14
    • 0028152601 scopus 로고
    • Site-directed mutagenesis of conserved serines in rat histidase. Identification of serine 254 as an essential active site residue
    • Taylor RG, McInnes RR: Site-directed mutagenesis of conserved serines in rat histidase. Identification of serine 254 as an essential active site residue. J Biol Chem 269: 27473-27477, 1994
    • (1994) J Biol Chem , vol.269 , pp. 27473-27477
    • Taylor, R.G.1    McInnes, R.R.2
  • 15
    • 0015217702 scopus 로고
    • Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of a catalytically essential dehydroalanine
    • Hodgins DS: Yeast phenylalanine ammonia-lyase. Purification, properties, and the identification of a catalytically essential dehydroalanine. J Biol Chem 246: 2977-2985, 1971
    • (1971) J Biol Chem , vol.246 , pp. 2977-2985
    • Hodgins, D.S.1
  • 16
    • 0027992090 scopus 로고
    • Serine 202 is the putative precursor of the active site dehydroalanine of phenylalanine ammonia-lyase. Site-directed mutagenesis studies on the enzyme from parsley (Petroselinum crispum L.)
    • Schuster B, Rétey J: Serine 202 is the putative precursor of the active site dehydroalanine of phenylalanine ammonia-lyase. Site-directed mutagenesis studies on the enzyme from parsley (Petroselinum crispum L.). FEBS Lett 349: 252-254, 1994
    • (1994) FEBS Lett , vol.349 , pp. 252-254
    • Schuster, B.1    Rétey, J.2
  • 17
    • 0029082859 scopus 로고
    • The mechanism of action of phenylalanine ammonia-lyase: The role of prosthetic dehydroalanine
    • Schuster B, Rétey J: The mechanism of action of phenylalanine ammonia-lyase: The role of prosthetic dehydroalanine. Proc Natl Acad Sci USA 92: 8433-8437, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8433-8437
    • Schuster, B.1    Rétey, J.2
  • 18
    • 0342602049 scopus 로고    scopus 로고
    • Identification of essential amino acids in phenylalanine ammonia-lyase by site-directed mutagenesis
    • Langer B, Röther D, Rétey J: Identification of essential amino acids in phenylalanine ammonia-lyase by site-directed mutagenesis. Biochemistry 36: 10867-10871, 1997
    • (1997) Biochemistry , vol.36 , pp. 10867-10871
    • Langer, B.1    Röther, D.2    Rétey, J.3
  • 19
    • 0041154057 scopus 로고    scopus 로고
    • Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
    • Schwede TF, Rétey J, Schulz GE: Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry 38: 5355-5361, 1999
    • (1999) Biochemistry , vol.38 , pp. 5355-5361
    • Schwede, T.F.1    Rétey, J.2    Schulz, G.E.3
  • 20
    • 17344395175 scopus 로고    scopus 로고
    • Spectroscopic evidence for a 4-methylidene imidazol-5-one in histidine and phenylalanine ammonia-lyases
    • Röther D, Merkel D, Rétey J: Spectroscopic evidence for a 4-methylidene imidazol-5-one in histidine and phenylalanine ammonia-lyases. Angew Chem Int Ed 39: 2462-2464, 2000
    • (2000) Angew Chem Int Ed , vol.39 , pp. 2462-2464
    • Röther, D.1    Merkel, D.2    Rétey, J.3
  • 22
    • 0013633550 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of poly[(2R,3S)-benzyl β-3-methylmalate]: β-Methylaspartase as a versatile enzyme in the preparation of the chiral precursor
    • Bear M-M, Cammas S, Langlois V, Guérin P: Chemoenzymatic synthesis of poly[(2R,3S)-benzyl β-3-methylmalate]: β-Methylaspartase as a versatile enzyme in the preparation of the chiral precursor. C R Acad Sci Paris (11B) 325: 165-172, 1997
    • (1997) C R Acad Sci Paris (11B) , vol.325 , pp. 165-172
    • Bear, M.-M.1    Cammas, S.2    Langlois, V.3    Guérin, P.4
  • 23
    • 37049086056 scopus 로고
    • Kinetics and mechanism of syn-elimination of ammonia from (2S,3R)-3-methylaspartic acid by methylaspartase
    • Archer CH, Gani D: Kinetics and mechanism of syn-elimination of ammonia from (2S,3R)-3-methylaspartic acid by methylaspartase. J C S Chem Commun: 140-142, 1993
    • (1993) J C S Chem Commun , pp. 140-142
    • Archer, C.H.1    Gani, D.2
  • 24
    • 0027310492 scopus 로고
    • 2H]-3-methylaspartic acid: Slow substrates for a syn-elimination reaction catalyzed by methylaspartase
    • 2H]-3-methylaspartic acid: Slow substrates for a syn-elimination reaction catalyzed by methylaspartase. Tetrahedron: Asymmetry 4: 1141-1152, 1993
    • (1993) Tetrahedron: Asymmetry , vol.4 , pp. 1141-1152
    • Archer, C.H.1    Thomas, N.R.2    Gani, D.3
  • 28
    • 0001064401 scopus 로고
    • Stereochemical course of the enzymatic amination of chloro- and bromo-fumaric acid by 3-methylaspartate ammonia-lyase
    • Akhtar M, Cohen MA, Gani D: Stereochemical course of the enzymatic amination of chloro- and bromo-fumaric acid by 3-methylaspartate ammonia-lyase. Tetrahedron Lett 28: 2413-2416, 1987
    • (1987) Tetrahedron Lett , vol.28 , pp. 2413-2416
    • Akhtar, M.1    Cohen, M.A.2    Gani, D.3
  • 29
    • 0023608355 scopus 로고
    • Enantiospecific synthesis of 3-substituted aspartic acids via enzymatic amination of substituted fumaric acids
    • Akhtar M, Botting NP, Cohen MA, Gani D: Enantiospecific synthesis of 3-substituted aspartic acids via enzymatic amination of substituted fumaric acids. Tetrahedron 43: 5899-5908, 1987
    • (1987) Tetrahedron , vol.43 , pp. 5899-5908
    • Akhtar, M.1    Botting, N.P.2    Cohen, M.A.3    Gani, D.4
  • 30
    • 85007940552 scopus 로고
    • Occurrence of 3-methylaspartate ammonia-lyase in facultative anaerobes and their application to synthesis of 3-substituted (S)-aspartic acids
    • Asano Y, Kato Y: Occurrence of 3-methylaspartate ammonia-lyase in facultative anaerobes and their application to synthesis of 3-substituted (S)-aspartic acids. Biosci Biotech Biochem 58: 223-224, 1994
    • (1994) Biosci Biotech Biochem , vol.58 , pp. 223-224
    • Asano, Y.1    Kato, Y.2
  • 31
    • 0015994398 scopus 로고
    • Two pathways of glutamate fermentation by anaerobic bacteria
    • Buckel W, Barker HA: Two pathways of glutamate fermentation by anaerobic bacteria. J Bacteriol 117: 1248-1260, 1974
    • (1974) J Bacteriol , vol.117 , pp. 1248-1260
    • Buckel, W.1    Barker, H.A.2
  • 32
    • 0030729079 scopus 로고    scopus 로고
    • 3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae
    • Kato Y, Asano Y: 3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae. Arch Microbiol 168: 457-463, 1997
    • (1997) Arch Microbiol , vol.168 , pp. 457-463
    • Kato, Y.1    Asano, Y.2
  • 33
    • 0026469359 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding β-methylaspartase and characterization of the recombinant protein
    • Goda, SK, Minton NP, Botting NP, Gani D: Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding β-methylaspartase and characterization of the recombinant protein. Biochemistry 31: 10747-10756, 1992
    • (1992) Biochemistry , vol.31 , pp. 10747-10756
    • Goda, S.K.1    Minton, N.P.2    Botting, N.P.3    Gani, D.4
  • 35
    • 85007810217 scopus 로고
    • Purification and properties of crystalline 3-methyl-aspartase from two facultative anaerobes, Citrobacter sp. strain YG-0504 and Morganella morganii strain YG-0601
    • Kato Y, Asano Y: Purification and properties of crystalline 3-methyl-aspartase from two facultative anaerobes, Citrobacter sp. strain YG-0504 and Morganella morganii strain YG-0601. Biosci Biotech Biochem 59: 93-99, 1995
    • (1995) Biosci Biotech Biochem , vol.59 , pp. 93-99
    • Kato, Y.1    Asano, Y.2
  • 36
    • 0028973507 scopus 로고
    • 3-Methylaspartate ammonia-lyase from a facultative anaerobe, strain YG-1002
    • Kato Y, Asano Y: 3-Methylaspartate ammonia-lyase from a facultative anaerobe, strain YG-1002. Appl Microbiol Biotechnol 43: 901-907, 1995
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 901-907
    • Kato, Y.1    Asano, Y.2
  • 37
    • 0031738218 scopus 로고    scopus 로고
    • Cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002
    • Kato Y, Asano Y: Cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002. Appl Microbiol Biotechnol 50: 468-474, 1998
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 468-474
    • Kato, Y.1    Asano, Y.2
  • 38
    • 0014248295 scopus 로고
    • Amino acid fermentation by Fusobacterium nucleatum
    • Loesche WJ, Gibbons RJ: Amino acid fermentation by Fusobacterium nucleatum. Arch Oral Biol 13: 191-201, 1968
    • (1968) Arch Oral Biol , vol.13 , pp. 191-201
    • Loesche, W.J.1    Gibbons, R.J.2
  • 39
    • 0042954768 scopus 로고    scopus 로고
    • Anaerobic gram-negative rods: Bacteroides, Prevotella, Porphyromonas, Fusobacterium, Bilophilia, Sutterella
    • S.L. Gorbach, J.G. Bartlett, N.R. Blacklow (eds). WB. Saunders Co., Philadelphia
    • Finegold SM: Anaerobic gram-negative rods: Bacteroides, Prevotella, Porphyromonas, Fusobacterium, Bilophilia, Sutterella. In: S.L. Gorbach, J.G. Bartlett, N.R. Blacklow (eds). Infectious Diseases. WB. Saunders Co., Philadelphia, 1998, pp 1904-1915
    • (1998) Infectious Diseases , pp. 1904-1915
    • Finegold, S.M.1
  • 40
    • 0027501515 scopus 로고
    • Fusobacteria: New taxonomy and related diseases
    • Bennett KW, Eley A: Fusobacteria: new taxonomy and related diseases. J Med Microbiol 39: 246-254, 1993
    • (1993) J Med Microbiol , vol.39 , pp. 246-254
    • Bennett, K.W.1    Eley, A.2
  • 41
    • 0025767776 scopus 로고
    • Pathways of glutamate catabolism among Fusobacterium species
    • Gharbia SE, Shah HN: Pathways of glutamate catabolism among Fusobacterium species. J Gen Microbiol 137: 1201-1206, 1991
    • (1991) J Gen Microbiol , vol.137 , pp. 1201-1206
    • Gharbia, S.E.1    Shah, H.N.2
  • 43
    • 0021321776 scopus 로고
    • Pleomorphism of fusobacteria isolated from the cockroachhindgut
    • Foglesong MA, Cruden DL, Markovetz AJ: Pleomorphism of fusobacteria isolated from the cockroachhindgut. J Bacteriol 158: 474-480, 1984
    • (1984) J Bacteriol , vol.158 , pp. 474-480
    • Foglesong, M.A.1    Cruden, D.L.2    Markovetz, A.J.3
  • 44
    • 0020263079 scopus 로고
    • Synthesis and absolute stereochemistry of serricornin [(4S,6S,7S)-4,6-dimethyl-7-hydroxy-3-nonanone]
    • Mori K, Nomi H, Chuman T, Kohno M, Kato K, Noguchi M: Synthesis and absolute stereochemistry of serricornin [(4S,6S,7S)-4,6-dimethyl-7-hydroxy-3-nonanone]. Tetrahedron 38: 3705-3711, 1982
    • (1982) Tetrahedron , vol.38 , pp. 3705-3711
    • Mori, K.1    Nomi, H.2    Chuman, T.3    Kohno, M.4    Kato, K.5    Noguchi, M.6
  • 45
    • 0022460782 scopus 로고
    • Resolution of D- and L-amino acids after precolumn derivatization with o-phthalaldehyde by mixed chelation with Cu(II)-L-proline
    • Lam S: Resolution of D- and L-amino acids after precolumn derivatization with o-phthalaldehyde by mixed chelation with Cu(II)-L-proline. J Chromatogr 355: 157-164, 1986
    • (1986) J Chromatogr , vol.355 , pp. 157-164
    • Lam, S.1
  • 46
    • 0028092772 scopus 로고
    • Biosynthesis of 5-hydroxy-4-oxo-L-norvaline in Streptomyces akiyoshiensis
    • White RL, Smith KC, De Marco AC: Biosynthesis of 5-hydroxy-4-oxo-L-norvaline in Streptomyces akiyoshiensis. Can J Chem 72: 1645-1655, 1994
    • (1994) Can J Chem , vol.72 , pp. 1645-1655
    • White, R.L.1    Smith, K.C.2    DeMarco, A.C.3
  • 47
    • 0024291672 scopus 로고
    • Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: Observation of differential relative reaction rates for substrate-product pairs
    • Botting NP, Akhtar M, Cohen MA, Gani D: Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: Observation of differential relative reaction rates for substrate-product pairs. Biochemistry 27: 2953-2955, 1988
    • (1988) Biochemistry , vol.27 , pp. 2953-2955
    • Botting, N.P.1    Akhtar, M.2    Cohen, M.A.3    Gani, D.4
  • 48
    • 0032885303 scopus 로고    scopus 로고
    • Utilization of D-amino acids by Fusobacterium nucleatum and Fusobacterium varium
    • Ramezani M, MacIntosh SE, White RL: Utilization of D-amino acids by Fusobacterium nucleatum and Fusobacterium varium. Amino Acids 17: 185-193, 1999
    • (1999) Amino Acids , vol.17 , pp. 185-193
    • Ramezani, M.1    MacIntosh, S.E.2    White, R.L.3
  • 49
    • 0002192038 scopus 로고
    • Protein and peptide purification
    • J.B.C. Findlay, M.J. Geisow (eds). Oxford University Press, New York
    • Wilson KJ, Yuan PM: Protein and peptide purification. In: J.B.C. Findlay, M.J. Geisow (eds). Protein Sequencing: A Practical Approach. Oxford University Press, New York, 1989, p. 13.
    • (1989) Protein Sequencing: A Practical Approach , pp. 13
    • Wilson, K.J.1    Yuan, P.M.2
  • 50
    • 0014786816 scopus 로고
    • Configuration of the β-methylaspartic acid residue in amphomycin
    • Bodanszky M, Marconi GG: Configuration of the β-methylaspartic acid residue in amphomycin. J Antibiot 23: 238-241, 1970
    • (1970) J Antibiot , vol.23 , pp. 238-241
    • Bodanszky, M.1    Marconi, G.G.2
  • 51
    • 77956939611 scopus 로고
    • The enzymatic elimination of ammonia
    • P.D. Boyer (ed). Academic Press, New York
    • Hanson KR, Havir EA: The enzymatic elimination of ammonia. In: P.D. Boyer (ed). The Enzymes. Vol. VII. Academic Press, New York, 1972, pp 75-166
    • (1972) The Enzymes , vol.7 , pp. 75-166
    • Hanson, K.R.1    Havir, E.A.2
  • 52
    • 0023060471 scopus 로고
    • L-Aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology
    • Takagi JS, Tokushige M, Shimura Y, Kanehisa M: L-Aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology. Biochem Biophys Res Commun 138: 568-572, 1986
    • (1986) Biochem Biophys Res Commun , vol.138 , pp. 568-572
    • Takagi, J.S.1    Tokushige, M.2    Shimura, Y.3    Kanehisa, M.4
  • 53
    • 0022474612 scopus 로고
    • Structural and functional relationships between fumarase and aspartase
    • Woods SA, Miles JS, Roberts RE, Guest JR: Structural and functional relationships between fumarase and aspartase. Biochem J 237: 547-557, 1986
    • (1986) Biochem J , vol.237 , pp. 547-557
    • Woods, S.A.1    Miles, J.S.2    Roberts, R.E.3    Guest, J.R.4
  • 55
    • 0026794264 scopus 로고
    • 3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: A new reaction in the evolution of a mechanistic motif
    • Williams SE, Woolridge EM, Ransom SC, Landro JA, Babbitt PC, Kozarich JW: 3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: A new reaction in the evolution of a mechanistic motif. Biochemistry 31: 9768-9776, 1992
    • (1992) Biochemistry , vol.31 , pp. 9768-9776
    • Williams, S.E.1    Woolridge, E.M.2    Ransom, S.C.3    Landro, J.A.4    Babbitt, P.C.5    Kozarich, J.W.6


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