Directed Evolution of Yeast Pyruvate Decarboxylase 1 for Attenuated Regulation and Increased Stability
Author:
Affiliation:
1. Research School of Chemistry, Australian National University, Canberra 0200, Australia
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi701858u
Reference31 articles.
1. Catalytic power of pyruvate decarboxylase. Rate-limiting events and microscopic rate constants from primary carbon and secondary hydrogen isotope effects
2. The Mechanism of Substrate Activation of Pyruvate Decarboxylase: A First Approach
3. Allosteric properties of yeast pyruvate decarboxylase
4. 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
5. Crystal Structure of the Thiamin Diphosphate-dependent Enzyme Pyruvate Decarboxylase from the YeastSaccharomyces cerevisiaeat 2.3 Å Resolution
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