Journal
ORGANIC LETTERS
Volume 16, Issue 8, Pages 2122-2125Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ol5005438
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Funding
- NSF [CHE-1309148]
- NIH [GM093903]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1309148] Funding Source: National Science Foundation
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OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regio-selectivity. Due to the potential application of this reaction for industrial ergothioneine production, in this study, we systematically characterized OvoA by a combination of three different assays. Our studies revealed that OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. Remarkably, these OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine.
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