Remarkable Stabilization of Zwitterionic Intermediates May Account for a Billion-fold Rate Acceleration by Thiamin Diphosphate-Dependent Decarboxylases-Reference-Cited by-同舟云学术

Remarkable Stabilization of Zwitterionic Intermediates May Account for a Billion-fold Rate Acceleration by Thiamin Diphosphate-Dependent Decarboxylases

Published:1999-04-29 Issue:20 Volume:38 Page:6369-6373
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Jordan Frank¹,Li Haijuan¹,Brown Angela¹

Affiliation:

1. Departments of Chemistry and Biological Sciences and Program in Cellular and Molecular Biodynamics, Rutgers, the State University, Newark, New Jersey 07102

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi990373g

Reference33 articles.

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

2. Crystal Structure of the Thiamin Diphosphate-dependent Enzyme Pyruvate Decarboxylase from the YeastSaccharomyces cerevisiaeat 2.3 Å Resolution

3. Observation of a 2-.alpha.-enamine from a 2-(methoxyphenylmethyl)-3,4-dimethylthiazolium salt in water: implications for catalysis by thiamin diphosphate-dependent .alpha.-keto acid decarboxylases

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