Understanding Which Residues of the Active Site and Loop Structure of a Tyrosine Aminomutase Define Its Mutase and Lyase Activities
Author:
Affiliation:
1. Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States
2. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States
Funder
AgBioResearch, Michigan State University
Office for Inclusion and Intercultural Initiatives, Michigan State University
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00269
Reference34 articles.
1. A new member of the 4-methylideneimidazole-5-one-containing aminomutase family from the enediyne kedarcidin biosynthetic pathway
2. Detection of a Phenylalanine Aminomutase in Cell-Free Extracts of Taxus brevifolia and Preliminary Characterization of Its Reaction
3. A Novel 4-Methylideneimidazole-5-one-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis
4. Cloning, Heterologous Expression, and Characterization of a Phenylalanine Aminomutase Involved in Taxol Biosynthesis
5. Gatekeeping versus Promiscuity in the Early Stages of the Andrimid Biosynthetic Assembly Line
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