Mechanism of Benzaldehyde Lyase Studied via Thiamin Diphosphate-Bound Intermediates and Kinetic Isotope Effects
Author:
Affiliation:
1. Department of Chemistry, Rutgers University, Newark, New Jersey 07102, and Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan 48109
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi702302u
Reference37 articles.
1. Benzaldehyde lyase, a novel thiamine PPi-requiring enzyme, from Pseudomonas fluorescens biovar I
2. A new perspective on thiamine catalysis
3. Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens
4. Interplay of organic and biological chemistry in understanding coenzyme mechanisms: example of thiamin diphosphate-dependent decarboxylations of 2-oxo acids
5. Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions
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