Catalytic Acid−Base Groups in Yeast Pyruvate Decarboxylase. 3. A Steady-State Kinetic Model Consistent with the Behavior of both Wild-Type and Variant Enzymes at All Relevant pH Values-Reference-Cited by-同舟云学术

Catalytic Acid−Base Groups in Yeast Pyruvate Decarboxylase. 3. A Steady-State Kinetic Model Consistent with the Behavior of both Wild-Type and Variant Enzymes at All Relevant pH Values

Published:2001-05-31 Issue:25 Volume:40 Page:7382-7403
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sergienko Eduard A.¹,Jordan Frank¹

Affiliation:

1. Department of Chemistry and Program in Cellular and Molecular Biodynamics, Rutgers, The State University of New Jersey, Newark, New Jersey 07102

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi002857e

Reference44 articles.

1. Bisswanger, H., and Schellenberger, A., Eds. (1996)Biochemistry and Physiology of Thiamin Diphosphate Enzymes, pp 1−599, A.u.C. Intemann, Wissenschaftlicher Verlag, Prien, Germany.

2. Regulation of thiamin diphosphate-dependent 2-oxo acid decarboxylases by substrate and thiamin diphosphate.Mg(II) – evidence for tertiary and quaternary interactions

3. Allosteric properties of yeast pyruvate decarboxylase

4. The Mechanism of Substrate Activation of Pyruvate Decarboxylase: A First Approach

5. Catalytic power of pyruvate decarboxylase. Rate-limiting events and microscopic rate constants from primary carbon and secondary hydrogen isotope effects

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