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Volumn 121, Issue 1, 1997, Pages 161-171

Paracoccus denitrificans aromatic amino acid aminotransferase: A model enzyme for the study of dual substrate recognition mechanism

Author keywords

Aromatic amino acid aminotransferase; Aspartate aminotransferase; Paracoccus denitrificans; Pyridoxal 5' phosphate; Substrate specificity

Indexed keywords

ALIPHATIC COMPOUND; AMINOTRANSFERASE; AROMATIC AMINO ACID; ASPARTATE AMINOTRANSFERASE; BACTERIAL ENZYME; PHENYLALANINE; TYROSINE;

EID: 0031014286     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021561     Document Type: Article
Times cited : (30)

References (37)
  • 2
    • 0022372131 scopus 로고
    • Aromatic amino acid aminotransferase of Escherichia coli: Nucleotide sequence of the tyrB gene
    • Kuramitsu, S., Inoue, K., Ogawa, T., Ogawa, H., and Kagamiyama, H. (1985) Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. Biochem. Biophys. Res. Commun. 133, 134-139
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 134-139
    • Kuramitsu, S.1    Inoue, K.2    Ogawa, T.3    Ogawa, H.4    Kagamiyama, H.5
  • 3
    • 0022550466 scopus 로고
    • The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes
    • Fotheringham, I.G., Dacey, S.A., Taylor, P.P., Smith, T.J., Hunter, M.G., Finlay, M.E., Primrose, S.B., Parker, D.M., and Edwards, R.M. (1986) The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Biochem. J. 234, 593-604
    • (1986) Biochem. J. , vol.234 , pp. 593-604
    • Fotheringham, I.G.1    Dacey, S.A.2    Taylor, P.P.3    Smith, T.J.4    Hunter, M.G.5    Finlay, M.E.6    Primrose, S.B.7    Parker, D.M.8    Edwards, R.M.9
  • 4
    • 0002646776 scopus 로고
    • Pig cytosolic aspartate aminotransferase: The structures of the internal aldimine, external aldimine, and ketimine and of the β-subform
    • (Christen, P. and Metzler, D.E., eds.) John Wiley and Sons, New York
    • Arnone, A., Rogers, P.H., Hyde, C.C., Briley, P.D., Metzler, C.M., and Metzler, D.E. (1985) Pig cytosolic aspartate aminotransferase: The structures of the internal aldimine, external aldimine, and ketimine and of the β-subform in Transaminasea (Christen, P. and Metzler, D.E., eds.) pp. 138-154, John Wiley and Sons, New York
    • (1985) Transaminasea , pp. 138-154
    • Arnone, A.1    Rogers, P.H.2    Hyde, C.C.3    Briley, P.D.4    Metzler, C.M.5    Metzler, D.E.6
  • 5
    • 0038064633 scopus 로고
    • Spatial structure of mitochondrial aspartate aminotransferase
    • (Christen, P. and Metzler, D.E., eds.) John Wiley & Sons, New York
    • Jansonius, J.N., Eichele, G., Ford, G.C., Picot, D., Thaller, C., and Vincent, M. (1985) Spatial structure of mitochondrial aspartate aminotransferase in Transaminasea (Christen, P. and Metzler, D.E., eds.) pp. 109-137, John Wiley & Sons, New York
    • (1985) Transaminasea , pp. 109-137
    • Jansonius, J.N.1    Eichele, G.2    Ford, G.C.3    Picot, D.4    Thaller, C.5    Vincent, M.6
  • 6
    • 0028167665 scopus 로고
    • X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form
    • Okamoto, A., Higuchi, T., Hirotsu, K., Kuramitsu, S., and Kagamiyama, H. (1994) X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form. J. Biochem. 116, 95-107
    • (1994) J. Biochem. , vol.116 , pp. 95-107
    • Okamoto, A.1    Higuchi, T.2    Hirotsu, K.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 7
    • 0027420413 scopus 로고
    • Escherichia coli aromatic amino acid aminotransferase: Characterization and comparison with aspartate aminotransferase
    • Hayashi, H., Inoue, K., Nagata, T., Kuramitsu, S., and Kagamiyama, H. (1993) Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase. Biochemistry 32, 12229-12239
    • (1993) Biochemistry , vol.32 , pp. 12229-12239
    • Hayashi, H.1    Inoue, K.2    Nagata, T.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 8
    • 0017884206 scopus 로고
    • The purification and properties of the aspartate aminotransferase and aromaticamino-acid aminotransferase from Escherichia coli
    • Powell, J.T. and Morrison, J.F. (1978) The purification and properties of the aspartate aminotransferase and aromaticamino-acid aminotransferase from Escherichia coli. Eur. J. Biochem. 87, 391-400
    • (1978) Eur. J. Biochem. , vol.87 , pp. 391-400
    • Powell, J.T.1    Morrison, J.F.2
  • 9
    • 0028140310 scopus 로고
    • Significant improvement to the catalytic properties of aspartate aminotransferase: Role of Hydrophobic and charged residues in the substrate binding pocket
    • Köhler, E., Seville, M., Jäger, J., Fotheringham, I., Hunter, M., Edwards, M., Jansonius, J.N., and Kirschner, K. (1994) Significant improvement to the catalytic properties of aspartate aminotransferase: Role of Hydrophobic and charged residues in the substrate binding pocket. Biochemistry 33, 90-97
    • (1994) Biochemistry , vol.33 , pp. 90-97
    • Köhler, E.1    Seville, M.2    Jäger, J.3    Fotheringham, I.4    Hunter, M.5    Edwards, M.6    Jansonius, J.N.7    Kirschner, K.8
  • 10
    • 0030008569 scopus 로고    scopus 로고
    • Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: Systematic hydroxy-group addition/deletion studies to probe the enzyme-substrate interactions
    • Hayashi, H., Inoue, K., Mizuguchi, H., and Kagamiyama, H. (1996) Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: Systematic hydroxy-group addition/deletion studies to probe the enzyme-substrate interactions. Biochemistry 35, 6754-6761
    • (1996) Biochemistry , vol.35 , pp. 6754-6761
    • Hayashi, H.1    Inoue, K.2    Mizuguchi, H.3    Kagamiyama, H.4
  • 11
    • 0029111444 scopus 로고
    • The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases
    • Onuffer, J.J., Ton, B.T., Klement, I., and Kirsch, J.F. (1995) The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases. Protein Sci. 4, 1743-1749
    • (1995) Protein Sci. , vol.4 , pp. 1743-1749
    • Onuffer, J.J.1    Ton, B.T.2    Klement, I.3    Kirsch, J.F.4
  • 12
    • 0030579935 scopus 로고    scopus 로고
    • Cloning and characterization of the tyrB gene, from Salmonella typhimurium
    • Nakai, Y., Hayashi, H., and Kagamiyama, H. (1996) Cloning and characterization of the tyrB gene, from Salmonella typhimurium. Biochim. Biophys. Acta 1308, 189-192
    • (1996) Biochim. Biophys. Acta , vol.1308 , pp. 189-192
    • Nakai, Y.1    Hayashi, H.2    Kagamiyama, H.3
  • 13
    • 0026013118 scopus 로고
    • Molecular cloning of the L-phenylalanine transaminase gene from Paracoccus denitrificans in Escherichia coli K-12
    • Takagi, T., Taniguchi, T., Yamamoto, Y., and Shibatani, T. (1991) Molecular cloning of the L-phenylalanine transaminase gene from Paracoccus denitrificans in Escherichia coli K-12. Biotechnol. Appl. Biochem. 13, 112-119
    • (1991) Biotechnol. Appl. Biochem. , vol.13 , pp. 112-119
    • Takagi, T.1    Taniguchi, T.2    Yamamoto, Y.3    Shibatani, T.4
  • 14
    • 3643069904 scopus 로고
    • α-Amino-ω-hydroxy acids
    • Barton, D.H.R. and Ollis, W.D., eds. Sutherland, I.O., ed. Pergamon Press, Oxford, UK
    • Jones, J.H. (1979) α-Amino-ω-hydroxy acids in Comprehensive Organic Chemistry (Barton, D.H.R. and Ollis, W.D., eds.) Vol. 2 (Sutherland, I.O., ed.) pp. 2589-2643, Pergamon Press, Oxford, UK
    • (1979) Comprehensive Organic Chemistry , vol.2 , pp. 2589-2643
    • Jones, J.H.1
  • 15
    • 0018437071 scopus 로고
    • Preparation of the diastereoisomers of β-hydroxy-L-aspartate with pig heart aspartate aminotransferase
    • Jenkins, W.T. (1979) Preparation of the diastereoisomers of β-hydroxy-L-aspartate with pig heart aspartate aminotransferase. Anal. Biochem. 93, 134-138
    • (1979) Anal. Biochem. , vol.93 , pp. 134-138
    • Jenkins, W.T.1
  • 16
    • 0001699572 scopus 로고
    • The synthesis of amino acids from ethyl acetamidomalonate and ethyl acetamidocyanoacetate. III. the use of primary halides
    • Albertson, N.F. (1946) The synthesis of amino acids from ethyl acetamidomalonate and ethyl acetamidocyanoacetate. III. The use of primary halides. J. Am. Chem. Soc. 69, 450-453
    • (1946) J. Am. Chem. Soc. , vol.69 , pp. 450-453
    • Albertson, N.F.1
  • 17
    • 0025366034 scopus 로고
    • Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity
    • Kuramitsu, S., Hiromi, K., Hayashi, H., Morino, Y., and Kagamiyama, H. (1990) Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. Biochemistry 29, 5469-5476
    • (1990) Biochemistry , vol.29 , pp. 5469-5476
    • Kuramitsu, S.1    Hiromi, K.2    Hayashi, H.3    Morino, Y.4    Kagamiyama, H.5
  • 20
    • 0025922823 scopus 로고
    • The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase
    • Yano, T., Kuramitsu, S., Tanase, S., Morino, Y., Hiromi, K., and Kagamiyama, H. (1991) The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase. J. Biol. Chem. 266, 6079-6085
    • (1991) J. Biol. Chem. , vol.266 , pp. 6079-6085
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Morino, Y.4    Hiromi, K.5    Kagamiyama, H.6
  • 21
    • 0021107165 scopus 로고
    • PH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase
    • Kiick, D.M. and Cook, F.F. (1983) pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase. Biochemistry 22, 375-382
    • (1983) Biochemistry , vol.22 , pp. 375-382
    • Kiick, D.M.1    Cook, F.F.2
  • 22
    • 0029919942 scopus 로고    scopus 로고
    • Evolutionary recruitment of biochemically specialized subdivisions of family I within the protein superfamily of aminotransferases
    • Jensen, R.A. and Gu, W. (1996) Evolutionary recruitment of biochemically specialized subdivisions of family I within the protein superfamily of aminotransferases. J. Bacteriol. 178, 2161-2171
    • (1996) J. Bacteriol. , vol.178 , pp. 2161-2171
    • Jensen, R.A.1    Gu, W.2
  • 23
    • 0001515809 scopus 로고
    • The enzymatic oxidation of pyridoxine and pyridoxamine phosphates
    • Wada, H. and Snell, E.E. (1961) The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J. Biol. Chem. 236, 2089-2095
    • (1961) J. Biol. Chem. , vol.236 , pp. 2089-2095
    • Wada, H.1    Snell, E.E.2
  • 24
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta, P.K., Hale, T.I., and Christen, P. (1993) Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem. 214, 549-561
    • (1993) Eur. J. Biochem. , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 25
    • 0021998790 scopus 로고
    • Aspartate aminotransferase of Escherichia coli: Nucleotide sequence of the aspC gene
    • Kuramitsu, S., Okuno, S., Ogawa, T., Ogawa, H., and Kagamiyama, H. (1985) Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene. J. Biochem. 97, 1259-1262
    • (1985) J. Biochem. , vol.97 , pp. 1259-1262
    • Kuramitsu, S.1    Okuno, S.2    Ogawa, T.3    Ogawa, H.4    Kagamiyama, H.5
  • 27
    • 0014940647 scopus 로고
    • Physical-chemical studies on the pyridoxal phosphate binding site in sodium borohydride -reduced and native phosphorylase
    • Johnson, G.F., Tu, J.-I., Shonka Bartlett, M.L., and Graves, D.J. (1970) Physical-chemical studies on the pyridoxal phosphate binding site in sodium borohydride -reduced and native phosphorylase. J. Biol. Chem. 245, 5560-5568
    • (1970) J. Biol. Chem. , vol.245 , pp. 5560-5568
    • Johnson, G.F.1    Tu, J.-I.2    Shonka Bartlett, M.L.3    Graves, D.J.4
  • 28
    • 0025834941 scopus 로고
    • Equilibria and absorption spectra of tryptophanase
    • Metzler, C.M., Viswanath, R., and Metzler, D.E. (1991) Equilibria and absorption spectra of tryptophanase. J. Biol. Chem. 266, 9374-9381
    • (1991) J. Biol. Chem. , vol.266 , pp. 9374-9381
    • Metzler, C.M.1    Viswanath, R.2    Metzler, D.E.3
  • 29
    • 0000427037 scopus 로고
    • A kinetic and equilibrium analysis of glutamic oxaloacetate transaminase mechanism
    • Velick, S.F. and Vavra, J. (1962) A kinetic and equilibrium analysis of glutamic oxaloacetate transaminase mechanism. J. Biol. Chem. 237, 2109-2122
    • (1962) J. Biol. Chem. , vol.237 , pp. 2109-2122
    • Velick, S.F.1    Vavra, J.2
  • 30
    • 0014098783 scopus 로고
    • A temperature jump study of aspartate aminotransferase, A reinvestigation
    • Fasella, P. and Hammes, G.G. (1967) A temperature jump study of aspartate aminotransferase, A reinvestigation. Biochemistry 6, 1798-1804
    • (1967) Biochemistry , vol.6 , pp. 1798-1804
    • Fasella, P.1    Hammes, G.G.2
  • 31
    • 0014011701 scopus 로고
    • Glutamic-aspartic transaminase. X. Mechanism and order of formation of the enzymesubstrate carboxylate bonds
    • Jenkins, W.T. and D'Ari, L. (1966) Glutamic-aspartic transaminase. X. Mechanism and order of formation of the enzymesubstrate carboxylate bonds. J. Biol. Chem. 241, 5667-5674
    • (1966) J. Biol. Chem. , vol.241 , pp. 5667-5674
    • Jenkins, W.T.1    D'Ari, L.2
  • 32
    • 0028054696 scopus 로고
    • Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: Modulation by binding of Uganda and implications for its role in catalysis
    • Iwasaki, M., Hayashi, H., and Kagamiyama, H. (1994) Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of Uganda and implications for its role in catalysis, J. Biochem. 115, 156-161
    • (1994) J. Biochem. , vol.115 , pp. 156-161
    • Iwasaki, M.1    Hayashi, H.2    Kagamiyama, H.3
  • 33
    • 0029080677 scopus 로고
    • Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: Involvement of Tyr70 in stabilization of the catalytic intermediates
    • Hayashi, H. and Kagamiyama, H. (1995) Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: Involvement of Tyr70 in stabilization of the catalytic intermediates. Biochemistry 34, 9413-9423
    • (1995) Biochemistry , vol.34 , pp. 9413-9423
    • Hayashi, H.1    Kagamiyama, H.2
  • 34
    • 0029079958 scopus 로고
    • Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis
    • Onuffer, J.J. and Kirsch, J.F. (1995) Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis. Protein Sci. 4, 1750-1757
    • (1995) Protein Sci. , vol.4 , pp. 1750-1757
    • Onuffer, J.J.1    Kirsch, J.F.2
  • 35
    • 0029124159 scopus 로고
    • Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase
    • Malashkevich, V.N., Onuffer, J.J., Kirsch, J.F., and Jansonius, J.N. (1995) Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nature Struct. Biol. 2, 548-553
    • (1995) Nature Struct. Biol. , vol.2 , pp. 548-553
    • Malashkevich, V.N.1    Onuffer, J.J.2    Kirsch, J.F.3    Jansonius, J.N.4
  • 36
    • 0028249912 scopus 로고
    • CLUSTAL V: Multiple alignment of DNA and protein sequences
    • Higgins, D.G. (1994) CLUSTAL V: multiple alignment of DNA and protein sequences. Methods Mol. Biol. 25, 307-318
    • (1994) Methods Mol. Biol. , vol.25 , pp. 307-318
    • Higgins, D.G.1


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