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Volumn 119, Issue 7, 1997, Pages 1507-1515

The linkage of catalysis and regulation in enzyme action. Fluoropyruvate as a probe of regulation in pyruvate decarboxylases

Author keywords

[No Author keywords available]

Indexed keywords

PYRUVATE DECARBOXYLASE;

EID: 0030943414     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja963259j     Document Type: Article
Times cited : (11)

References (41)
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    • (1992) The Enzymes, 3rd Ed. , vol.20 , pp. 271-318
    • Kluger, R.1
  • 2
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    • (b) Kluger, R. Chem. Rev. 1987, 87, 863-876.
    • (1987) Chem. Rev. , vol.87 , pp. 863-876
    • Kluger, R.1
  • 4
    • 0004166052 scopus 로고    scopus 로고
    • Sinnott, M. L., Ed.; Academic Press; London; section H, in press
    • (d) Schowen, R. L. In Comprehensive Biological Catalysis; Sinnott, M. L., Ed.; Academic Press; London; Vol. III, section H, in press.
    • Comprehensive Biological Catalysis , vol.3
    • Schowen, R.L.1
  • 17
    • 0020000969 scopus 로고
    • Sable, H. Z., Gubler, C. J., Eds.; New York Academy of Sciences: New York
    • (d) Ullrich, J. In Thiamin: Twenty Years of Progress; Sable, H. Z., Gubler, C. J., Eds.; New York Academy of Sciences: New York, 1982; pp 287-305.
    • (1982) Thiamin: Twenty Years of Progress , pp. 287-305
    • Ullrich, J.1
  • 25
    • 8244252754 scopus 로고
    • M.S. Thesis, Department of Biological Science, University of Nebraska, Lincoln
    • (a) Smith, G. S. M.S. Thesis, Department of Biological Science, University of Nebraska, Lincoln, 1992.
    • (1992)
    • Smith, G.S.1
  • 29
    • 0020346954 scopus 로고
    • Schowen, K. B.; Schowen, R. L. Methods Enzymol. 1982, 87c, 551-606. Quinn, D. M.; Sutton, L. D. In Enzyme Mechanism from Isotope Effects; Cook, P. F., Ed.; CRC Press: Boca Raton, FL, 1991.
    • (1982) Methods Enzymol. , vol.87 C , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 30
    • 0004082237 scopus 로고
    • Cook, P. F., Ed.; CRC Press: Boca Raton, FL
    • Schowen, K. B.; Schowen, R. L. Methods Enzymol. 1982, 87c, 551-606. Quinn, D. M.; Sutton, L. D. In Enzyme Mechanism from Isotope Effects; Cook, P. F., Ed.; CRC Press: Boca Raton, FL, 1991.
    • (1991) Enzyme Mechanism from Isotope Effects
    • Quinn, D.M.1    Sutton, L.D.2
  • 31
    • 0015912725 scopus 로고
    • + = 0.85. The data also agree with a biphasic fit against σ with a change in rate-limiting step from a step with ρ = 2.8 to a step with ρ = 0, the former step being 26% rate limiting for the unsubstituted phenylglyoxalate. It is not certain what the rate-limiting step for k is with these substrates but the biphasic fit to the substituent effect is consistent with decarboxylation being largely rate limiting (ρ = 2.8) for electron-donating substitutents and product release (ρ = 0) becoming rate limiting for electron-withdrawing substituents.
    • (1973) Eur. J. Biochem. , vol.32 , pp. 83-87
    • Lehmann, H.1    Fischer, G.2    Hübner, G.3    Hohnert, K.D.4    Schellenberger, A.5
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    • (1970) Methods Enzymol. , vol.18 A , pp. 109-115
    • Ullrich, J.1


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