Mechanistic Characterization of Escherichia coli l-Aspartate Oxidase from Kinetic Isotope Effects
Author:
Affiliation:
1. Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, United States
Funder
National Institute of Allergy and Infectious Diseases
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00307
Reference38 articles.
1. Crystallization of L-aspartate oxidase, the first enzyme in the bacterial de novo biosynthesis of NAD
2. Structure ofL-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family
3. On the catalytic role of the active site residue E121 of E. coli l-aspartate oxidase
4. l-Aspartate Oxidase from Escherichia coli. II. Interaction with C4 Dicarboxylic Acids and Identification of a Novel l-Aspartate:Fumarate Oxidoreductase Activity
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