Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase
Author:
Funder
HHS | NIH | National Institute of General Medical Sciences
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
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2. A novel type of lysine oxidase: l-lysine-epsilon-oxidase;Gómez;Biochim. Biophys. Acta,2006
3. X-ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in l-lysine ɛ-oxidase from Marinomonas mediterranea;Okazaki;J. Biochem,2013
4. Characterization of recombinant biosynthetic precursors of the cysteine tryptophylquinone cofactors of l-lysine-ɛ-oxidase and glycine oxidase from Marinomonas mediterranea;Chacón-Verdú;Biochim. Biophys. Acta,2015
5. LodB is required for the recombinant synthesis of the quinoprotein l-lysine-ɛ-oxidase from Marinomonas mediterranea;Chacón-Verdú;Appl. Microbiol. Biotechnol,2014
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
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
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