Pleiotropic Impact of a Single Lysine Mutation on Biosynthesis of and Catalysis by N-Methyltryptophan Oxidase
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi200349m
Reference43 articles.
1. pH and Kinetic Isotope Effects on Sarcosine Oxidation by N-Methyltryptophan Oxidase
2. N-Methyltryptophan Oxidase from Escherichia coli: Reaction Kinetics with N-Methyl Amino Acid and Carbinolamine Substrates
3. Characterization of the FAD-Containing N-Methyltryptophan Oxidase from Escherichia coli
4. Structure of the Flavocoenzyme of Two Homologous Amine Oxidases: Monomeric Sarcosine Oxidase and N-Methyltryptophan Oxidase
5. The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity
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