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Volumn 125, Issue 6, 1999, Pages 987-990

Role of tyrosine 265 of alanine racemase from Bacillus stearothermophilus

Author keywords

Alanine racemase; Chemical rescue; chloroalanine

Indexed keywords

3 CHLOROALANINE; ALANINE RACEMASE; TYROSINE;

EID: 0032775642     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022406     Document Type: Article
Times cited : (23)

References (22)
  • 1
    • 84954325196 scopus 로고
    • Alanine racemase: Structure and function
    • (Fukui, T. and Soda, K., eds.), Kodansha, Tokyo
    • Yoshimura, T. and Soda, K. (1994) Alanine racemase: structure and function in Molecular Aspects of Enzyme Catalysis (Fukui, T. and Soda, K., eds.) pp. 147-163, Kodansha, Tokyo
    • (1994) Molecular Aspects of Enzyme Catalysis , pp. 147-163
    • Yoshimura, T.1    Soda, K.2
  • 2
    • 0033548158 scopus 로고    scopus 로고
    • Role of lysine39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5′-phosphate: Chemical rescue studies of Lys39→Ala mutant
    • Watanabe, A., Kurokawa, Y., Yoshimura, T., Kurihara, T., Soda, K., and Esaki, N. (1999) Role of lysine39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5′-phosphate: chemical rescue studies of Lys39→Ala mutant. J. Biol. Chem. 274, 4189-4194
    • (1999) J. Biol. Chem. , vol.274 , pp. 4189-4194
    • Watanabe, A.1    Kurokawa, Y.2    Yoshimura, T.3    Kurihara, T.4    Soda, K.5    Esaki, N.6
  • 3
    • 0031032448 scopus 로고    scopus 로고
    • Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution
    • Shaw, J.P., Petsko, A., and Ringe, D. (1997) Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution. Biochemistry 36, 1329-1342
    • (1997) Biochemistry , vol.36 , pp. 1329-1342
    • Shaw, J.P.1    Petsko, A.2    Ringe, D.3
  • 4
    • 0032555181 scopus 로고    scopus 로고
    • Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine
    • Stamper, C.G.F., Morollo, A.A., and Ringe, D. (1998) Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine. Biochemistry 37, 10438-10445
    • (1998) Biochemistry , vol.37 , pp. 10438-10445
    • Stamper, C.G.F.1    Morollo, A.A.2    Ringe, D.3
  • 5
    • 0033574155 scopus 로고    scopus 로고
    • Structure of a Michaelis complex analogue: Propionate binds in the substrate carboxylate site of alanine racemase
    • Morolo, A.A., Petsko, G.A., and Ringe, D. (1999) Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase. Biochemistry 38, 3293-3301
    • (1999) Biochemistry , vol.38 , pp. 3293-3301
    • Morolo, A.A.1    Petsko, G.A.2    Ringe, D.3
  • 6
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 7
    • 0017854719 scopus 로고
    • Suicide substrates for the alanine racemase of Escherichia coli B
    • Wang, E. and Walsh, C.T. (1978) Suicide substrates for the alanine racemase of Escherichia coli B. Biochemistry 17, 1313-1321
    • (1978) Biochemistry , vol.17 , pp. 1313-1321
    • Wang, E.1    Walsh, C.T.2
  • 8
    • 0021769535 scopus 로고
    • Inactivation of the dadB salmonella typhimurium alanine racemase by D and L isomers of β-substituted alanines: Kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism
    • Badet, B., Roise, D., and Walsh, C.T. (1984) Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of β-substituted alanines: kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism. Biochemistry 23, 5188-5194
    • (1984) Biochemistry , vol.23 , pp. 5188-5194
    • Badet, B.1    Roise, D.2    Walsh, C.T.3
  • 9
    • 0022536214 scopus 로고
    • Biosynthetic alanine racemase of Salmonella typhimurium: Purification and characterization of the enzyme encoded by the air gene
    • Esaki, N. and Walsh, C.T. (1986) Biosynthetic alanine racemase of Salmonella typhimurium: purification and characterization of the enzyme encoded by the air gene. Biochemistry 25, 3261-3267
    • (1986) Biochemistry , vol.25 , pp. 3261-3267
    • Esaki, N.1    Walsh, C.T.2
  • 10
    • 0020494540 scopus 로고
    • Chemistry of the inactivation of cytosolic aspartate aminotransferase by serine O-sulfate
    • Ueno, H., Likos, J.J., and Metzler, D.E. (1982) Chemistry of the inactivation of cytosolic aspartate aminotransferase by serine O-sulfate. Biochemistry 21, 4387-4393
    • (1982) Biochemistry , vol.21 , pp. 4387-4393
    • Ueno, H.1    Likos, J.J.2    Metzler, D.E.3
  • 11
    • 0027462120 scopus 로고
    • Lysine 87 in the β subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transamination, catalysis, product release
    • Lu, Z., Nagata, S., McPhie, P., and Miles, E.W. (1993) Lysine 87 in the β subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transamination, catalysis, product release. J. Biol. Chem. 268, 8727-8734
    • (1993) J. Biol. Chem. , vol.268 , pp. 8727-8734
    • Lu, Z.1    Nagata, S.2    McPhie, P.3    Miles, E.W.4
  • 12
    • 0025829773 scopus 로고
    • Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine
    • Nishimura, K., Tanizawa, K., Yoshimura, T., Esaki, N., Futaki, S., Manning, J.M., and Soda, K. (1991) Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine. Biochemistry 30, 4072-4076
    • (1991) Biochemistry , vol.30 , pp. 4072-4076
    • Nishimura, K.1    Tanizawa, K.2    Yoshimura, T.3    Esaki, N.4    Futaki, S.5    Manning, J.M.6    Soda, K.7
  • 13
    • 0026439099 scopus 로고
    • Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5′-phosphate
    • Yoshimura, T., Bhatia, M.B., Manning, J.M., Ringe, D., and Soda, K. (1992) Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5′-phosphate. Biochemistry 31, 11748-11754
    • (1992) Biochemistry , vol.31 , pp. 11748-11754
    • Yoshimura, T.1    Bhatia, M.B.2    Manning, J.M.3    Ringe, D.4    Soda, K.5
  • 14
    • 0030983015 scopus 로고    scopus 로고
    • An anomalous side reaction of the Lys303 mutant aromatic L-amino acid decarboxylase unravels the role of the residue in catalysis
    • Nishino, J., Hayashi, H., Ishii, S., and Kagamiyama, H. (1997) An anomalous side reaction of the Lys303 mutant aromatic L-amino acid decarboxylase unravels the role of the residue in catalysis. J. Biochem. 121, 604-611
    • (1997) J. Biochem. , vol.121 , pp. 604-611
    • Nishino, J.1    Hayashi, H.2    Ishii, S.3    Kagamiyama, H.4
  • 15
    • 0016286734 scopus 로고
    • Formate-induced labeling of the active site of aspartate aminotransferase by β-chloro-L-alanine
    • Morino, Y., Osman, A.M., and Okamoto, M. (1974) Formate-induced labeling of the active site of aspartate aminotransferase by β-chloro-L-alanine. J. Biol. Chem. 249, 6684-6692
    • (1974) J. Biol. Chem. , vol.249 , pp. 6684-6692
    • Morino, Y.1    Osman, A.M.2    Okamoto, M.3
  • 16
    • 0018192418 scopus 로고
    • Inactivation of pig heart alanine aminotransferase by β-chloroalanine
    • Golichowski, A. and Jenkins, W.T. (1978) Inactivation of pig heart alanine aminotransferase by β-chloroalanine. Arch. Biochem. Biophys. 189, 109-114
    • (1978) Arch. Biochem. Biophys. , vol.189 , pp. 109-114
    • Golichowski, A.1    Jenkins, W.T.2
  • 17
    • 0019855423 scopus 로고
    • Mechanistic studies on the pyridoxal phosphate enzyme 1-aminocyclopropane-1-carboxylate deaminaae from Pseudomonas sp.
    • Walsh, C., Pascal, R.A., Jr., Johnston, M., Raines, R., Dikshit, D., Krantz, A., and Honma, M. (1981) Mechanistic studies on the pyridoxal phosphate enzyme 1-aminocyclopropane-1-carboxylate deaminaae from Pseudomonas sp. Biochemistry 20, 7509-7519
    • (1981) Biochemistry , vol.20 , pp. 7509-7519
    • Walsh, C.1    Pascal R.A., Jr.2    Johnston, M.3    Raines, R.4    Dikshit, D.5    Krantz, A.6    Honma, M.7
  • 18
    • 0021216801 scopus 로고
    • Mechanism-based inactivation of bacterial kynureninase by β-substituted amino acid
    • Kishore, G.M. (1984) Mechanism-based inactivation of bacterial kynureninase by β-substituted amino acid. J. Biol. Chem. 259, 10669-10674
    • (1984) J. Biol. Chem. , vol.259 , pp. 10669-10674
    • Kishore, G.M.1
  • 19
    • 0021769545 scopus 로고
    • Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D and L isomers of β-substituted alanines: Kinetics, stoichiometry, active site peptide, and mechanistic studies
    • Roise, D., Soda, K., Yagi, T., and Walsh, C.T. (1984) Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D and L isomers of β-substituted alanines: kinetics, stoichiometry, active site peptide, and mechanistic studies. Biochemistry 23, 5195-5201
    • (1984) Biochemistry , vol.23 , pp. 5195-5201
    • Roise, D.1    Soda, K.2    Yagi, T.3    Walsh, C.T.4
  • 20
    • 0027183564 scopus 로고
    • Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants
    • Tai, C.H., Nalaboulu, S.R., Jacobson, T.M., Minter, D.E., and Cook, P.F. (1993) Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants. Biochemistry 32, 6433-6442
    • (1993) Biochemistry , vol.32 , pp. 6433-6442
    • Tai, C.H.1    Nalaboulu, S.R.2    Jacobson, T.M.3    Minter, D.E.4    Cook, P.F.5
  • 21
    • 0019832030 scopus 로고
    • Different modes of action of inhibitors of bacterial D-amino acid transaminase: A target enzyme for the design of new antibacterial agents
    • Soper, T.S. and Manning, J.M. (1981) Different modes of action of inhibitors of bacterial D-amino acid transaminase: a target enzyme for the design of new antibacterial agents. J. Biol. Chem. 256, 4263-4268
    • (1981) J. Biol. Chem. , vol.256 , pp. 4263-4268
    • Soper, T.S.1    Manning, J.M.2
  • 22
    • 0024478059 scopus 로고
    • Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
    • Toney, M.D. and Kirsch, J.F. (1989) Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science 243, 1485-1488
    • (1989) Science , vol.243 , pp. 1485-1488
    • Toney, M.D.1    Kirsch, J.F.2


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