Interaction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis
Author:
Affiliation:
1. Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida 32827, United States
2. Department of Genetics and Microbiology, University of Murcia, Murcia 30100, Spain
Funder
National Institute of General Medical Sciences
Burnett School of Biomedical Sciences, University of Central Florida
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00274
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1. Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor;Nature Communications;2021-02-10
2. Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase;Journal of Biological Chemistry;2020-05
3. Protein-Derived Cofactors;Comprehensive Natural Products III;2020
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5. Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolacea;Archives of Biochemistry and Biophysics;2019-10
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