Yeast Pyruvate Decarboxylase Tetramers Can Dissociate into Dimers along Two Interfaces. Hybrids of Low-Activity D28A (or D28N) and E477Q Variants, with Substitution of Adjacent Active Center Acidic Groups from Different Subunits, Display Restored Activity
Author:
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/bi0121712
Reference18 articles.
1. Crystal Structure of the Thiamin Diphosphate-dependent Enzyme Pyruvate Decarboxylase from the YeastSaccharomyces cerevisiaeat 2.3 Å Resolution
2. The Mechanism of Substrate Activation of Pyruvate Decarboxylase: A First Approach
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2. Bifunctionality of the Thiamin Diphosphate Cofactor: Assignment of Tautomeric/Ionization States of the 4′-Aminopyrimidine Ring When Various Intermediates Occupy the Active Sites during the Catalysis of Yeast Pyruvate Decarboxylase;Journal of the American Chemical Society;2012-02-17
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4. The Two Active Sites in Human Branched-chain α-Keto Acid Dehydrogenase Operate Independently without an Obligatory Alternating-site Mechanism;Journal of Biological Chemistry;2007-04
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