메뉴 건너뛰기




Volumn 44, Issue 14, 2005, Pages 5541-5550

Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; DIFFUSION; ENZYMES; PH; PLANTS (BOTANY); SUBSTRATES;

EID: 16844378688     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047479i     Document Type: Article
Times cited : (23)

References (23)
  • 1
    • 0014669977 scopus 로고
    • The Purification and Characterization of O-Acetylserine Sulfhydrylase-A from Salmonella typhimirium
    • Becker, M. A., Kredich, N. M., and Tomkins, G. M. (1969) The Purification and Characterization of O-Acetylserine Sulfhydrylase-A from Salmonella typhimirium. J. Biol. Chem. 244, 2418-2427.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2418-2427
    • Becker, M.A.1    Kredich, N.M.2    Tomkins, G.M.3
  • 2
    • 0017281552 scopus 로고
    • A Reaction Mechanism from Steady-State Kinetic Studies for O-Acetylserine Sulfhydrylase from Salmonella typhimurium LT-2
    • Cook, P. F., and Wedding, R. T. (1976) A Reaction Mechanism from Steady-State Kinetic Studies for O-Acetylserine Sulfhydrylase from Salmonella typhimurium LT-2. J. Biol. Chem. 251, 2023-2029.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2023-2029
    • Cook, P.F.1    Wedding, R.T.2
  • 3
    • 0026511957 scopus 로고
    • 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine
    • 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine. Biochemistry 31, 2299-2303.
    • (1992) Biochemistry , vol.31 , pp. 2299-2303
    • Cook, P.F.1    Hara, S.2    Nalabolu, S.3    Schnackerz, K.D.4
  • 4
    • 0029995666 scopus 로고    scopus 로고
    • Substitution of Pyridoxal 5′-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides a Test of the Mechanism Proposed for Formation of the α-Aminoacrylate Intermediate
    • Cook, P. F., Tai, C.-H., Hwang, C.-C., Woehl, E. U., Dunn, M. F., and Schanckerz, K. D. (1996) Substitution of Pyridoxal 5′-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides a Test of the Mechanism Proposed for Formation of the α-Aminoacrylate Intermediate. J. Biol. Chem. 271, 25842-25849.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25842-25849
    • Cook, P.F.1    Tai, C.-H.2    Hwang, C.-C.3    Woehl, E.U.4    Dunn, M.F.5    Schanckerz, K.D.6
  • 5
    • 0029089919 scopus 로고
    • Identification and Spectral Characterization of the External Aldimine of the O-Acetylserine Sulfhydrylase Reaction
    • Schnackerz, K. D., Tai, C.-H., Simmons, J. W., III, Jacobson, T. M., Rao, G. S. J., and Cook, P. F. (1995) Identification and Spectral Characterization of the External Aldimine of the O-Acetylserine Sulfhydrylase Reaction. Biochemistry 34, 12152-12160.
    • (1995) Biochemistry , vol.34 , pp. 12152-12160
    • Schnackerz, K.D.1    Tai, C.-H.2    Simmons III, J.W.3    Jacobson, T.M.4    Rao, G.S.J.5    Cook, P.F.6
  • 6
    • 0035954390 scopus 로고    scopus 로고
    • Characterization of the Allosteric Anion-Binding Site of O-Acetylsrine Sulfhydrylase
    • Tai, C.-H., Burkhard, P., Gani, D., Jenn, T., Johnson, C., and Cook, P. F. (2001) Characterization of the Allosteric Anion-Binding Site of O-Acetylsrine Sulfhydrylase. Biochemistry 40, 7446-7452.
    • (2001) Biochemistry , vol.40 , pp. 7446-7452
    • Tai, C.-H.1    Burkhard, P.2    Gani, D.3    Jenn, T.4    Johnson, C.5    Cook, P.F.6
  • 8
    • 16844375923 scopus 로고
    • Role of Lysine 42 in the β-Elimination Reaction Catalyzed by O-Acetylserine Sulfhydrylase a from Salmonella typhimurium
    • Rege, V. D., Kredich, N. M., Tai, C.-H., Karsten, W. E., and Cook, P. F. (1995) Role of Lysine 42 in the β-Elimination Reaction Catalyzed by O-Acetylserine Sulfhydrylase A from Salmonella typhimurium. FASEB J. 9, A1297.
    • (1995) FASEB J. , vol.9
    • Rege, V.D.1    Kredich, N.M.2    Tai, C.-H.3    Karsten, W.E.4    Cook, P.F.5
  • 9
    • 0034746703 scopus 로고    scopus 로고
    • Pyridoxal 5′-Phosphate-Dependent α,β-Elimination Reactions: Mechanism of O-Acetylserine Sulfhydrylase
    • Tai, C.-H., and Cook, P. F. (2001) Pyridoxal 5′-Phosphate-Dependent α,β-Elimination Reactions: Mechanism of O-Acetylserine Sulfhydrylase. Acc. Chem. Res. 34, 49-59.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 49-59
    • Tai, C.-H.1    Cook, P.F.2
  • 10
    • 0029865896 scopus 로고    scopus 로고
    • Formation of the α-Aminoacrylate Intermediate Limits the Overall Reaction Catalyzed by O-Acetylserine Sulfhydrylase
    • Woehl, E. U., Tai, C.-H., Dunn, M. F., and Cook, P. F. (1996) Formation of the α-Aminoacrylate Intermediate Limits the Overall Reaction Catalyzed by O-Acetylserine Sulfhydrylase. Biochemistry 35, 4776-4783.
    • (1996) Biochemistry , vol.35 , pp. 4776-4783
    • Woehl, E.U.1    Tai, C.-H.2    Dunn, M.F.3    Cook, P.F.4
  • 11
    • 0029093707 scopus 로고
    • Acid-Base Chemical Mechanism of O-Acetylserine Sulfhydrylases-A and -B from pH Studies
    • Tai, C.-H., Nalabolu, S. R., Simmons, J. W., III, Jacobson, T. M., and Cook, P. F. (1995) Acid-Base Chemical Mechanism of O-Acetylserine Sulfhydrylases-A and -B from pH Studies. Biochemistry 34, 12311-12322.
    • (1995) Biochemistry , vol.34 , pp. 12311-12322
    • Tai, C.-H.1    Nalabolu, S.R.2    Simmons III, J.W.3    Jacobson, T.M.4    Cook, P.F.5
  • 12
    • 0036405469 scopus 로고    scopus 로고
    • Detection of Intermediates in the Reactions Catalyzed by PLP-Dependent Enzymes
    • Karsten, W. E., Tai, C.-H., and Cook, P. F. (2002) Detection of Intermediates in the Reactions Catalyzed by PLP-Dependent Enzymes. Methods Enzymol. 354, 223-237.
    • (2002) Methods Enzymol. , vol.354 , pp. 223-237
    • Karsten, W.E.1    Tai, C.-H.2    Cook, P.F.3
  • 13
    • 0027183564 scopus 로고
    • Kinetic Mechanisms of the a and B Isozymes of O-Acetylserine Sulfhydrylases from Salmonella typhimurium LT-2 Using the Natual and Alternative Reactants
    • Tai, C.-H., Nalabolu, S. R., Jacobson, T. M., Minter, D. E., and Cook, P. F. (1993) Kinetic Mechanisms of the A and B Isozymes of O-Acetylserine Sulfhydrylases from Salmonella typhimurium LT-2 Using the Natual and Alternative Reactants. Biochemistry 32, 6433-6442.
    • (1993) Biochemistry , vol.32 , pp. 6433-6442
    • Tai, C.-H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Minter, D.E.4    Cook, P.F.5
  • 14
    • 0030012777 scopus 로고    scopus 로고
    • Kinetic Isotope Effects as a Probe of the β-Elimination Reaction Catalyzed by O-Acetylserine Sulfhydrylase
    • Hwang, C.-C., Woehl, E. U., Dunn, M. F., and Cook, P. F. (1996) Kinetic Isotope Effects as a Probe of the β-Elimination Reaction Catalyzed by O-Acetylserine Sulfhydrylase. Biochemistry 35, 6358-6365.
    • (1996) Biochemistry , vol.35 , pp. 6358-6365
    • Hwang, C.-C.1    Woehl, E.U.2    Dunn, M.F.3    Cook, P.F.4
  • 15
    • 0034692879 scopus 로고    scopus 로고
    • Identification of an Allosteric Anion-Binding Site on O-Acetylserine Sulfhydrylase: Structure of the Enzyme with Chloride Bound
    • Burkhard, P., Tai, C.-H., Jansonius, J. N., and Cook, P. F. (2000) Identification of an Allosteric Anion-Binding Site on O-Acetylserine Sulfhydrylase: Structure of the Enzyme with Chloride Bound. J. Mol. Biol. 303, 279-286.
    • (2000) J. Mol. Biol. , vol.303 , pp. 279-286
    • Burkhard, P.1    Tai, C.-H.2    Jansonius, J.N.3    Cook, P.F.4
  • 16
    • 0025486959 scopus 로고
    • A Rapid Purification Procedure and Computer-Assisted Sulfide Ion Selective Electrode Assay from O-Acetylserine Sulfhydrylase from Salmonella typhimurium
    • Hara, S., Payne, M. A., Schnackarz, K. D., and Cook, P. F. (1990) A Rapid Purification Procedure and Computer-Assisted Sulfide Ion Selective Electrode Assay from O-Acetylserine Sulfhydrylase from Salmonella typhimurium. Protein Expression Purif. 1, 70-76.
    • (1990) Protein Expression Purif. , vol.1 , pp. 70-76
    • Hara, S.1    Payne, M.A.2    Schnackarz, K.D.3    Cook, P.F.4
  • 17
    • 0027183564 scopus 로고
    • Kinetic mechanisms of a and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants
    • Tai, C.-H., Nalabolu, S. R., Jacobson, T. M., Minier, D. E., and Cook, P. F. (1993) Kinetic mechanisms of 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    Nalabolu, S.R.2    Jacobson, T.M.3    Minier, D.E.4    Cook, P.F.5
  • 18
    • 0018735516 scopus 로고
    • Statistical Analysis of Enzyme Kinetic Data
    • Cleland, W. W. (1979) Statistical Analysis of Enzyme Kinetic Data. Methods Enzymol. 63, 103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 21
    • 0017339091 scopus 로고
    • Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies
    • Cleland, W. W. (1977) Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies. Adv. Enzymol. 45, 273-387.
    • (1977) Adv. Enzymol. , vol.45 , pp. 273-387
    • Cleland, W.W.1
  • 22
    • 0033609810 scopus 로고    scopus 로고
    • Ligand Binding Induces a Large Conformational Change in O-Acetylserine Sulfhydrylase from Salmonella typhimurium
    • Burkhard, P., Tai, C.-H., Ristroph, C., Cook, P. F., and Jansonius, J. N. (1999) Ligand Binding Induces a Large Conformational Change in O-Acetylserine Sulfhydrylase from Salmonella typhimurium. J. Mol. Biol. 291, 941-953.
    • (1999) J. Mol. Biol. , vol.291 , pp. 941-953
    • Burkhard, P.1    Tai, C.-H.2    Ristroph, C.3    Cook, P.F.4    Jansonius, J.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.