Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis

[Image: see text] 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...

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Autores principales: Song, Heng, Her, Ampon Sae, Raso, Fiona, Zhen, Zhibin, Huo, Yuda, Liu, Pinghua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3998768/
https://www.ncbi.nlm.nih.gov/pubmed/24684381
http://dx.doi.org/10.1021/ol5005438
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author Song, Heng
Her, Ampon Sae
Raso, Fiona
Zhen, Zhibin
Huo, Yuda
Liu, Pinghua
author_facet Song, Heng
Her, Ampon Sae
Raso, Fiona
Zhen, Zhibin
Huo, Yuda
Liu, Pinghua
author_sort Song, Heng
collection PubMed
description [Image: see text] 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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spelling pubmed-39987682015-03-31 Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis Song, Heng Her, Ampon Sae Raso, Fiona Zhen, Zhibin Huo, Yuda Liu, Pinghua Org Lett [Image: see text] 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. American Chemical Society 2014-03-31 2014-04-18 /pmc/articles/PMC3998768/ /pubmed/24684381 http://dx.doi.org/10.1021/ol5005438 Text en Copyright © 2014 American Chemical Society
spellingShingle Song, Heng
Her, Ampon Sae
Raso, Fiona
Zhen, Zhibin
Huo, Yuda
Liu, Pinghua
Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
title Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
title_full Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
title_fullStr Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
title_full_unstemmed Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
title_short Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
title_sort cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (ovoa) in ovothiol biosynthesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3998768/
https://www.ncbi.nlm.nih.gov/pubmed/24684381
http://dx.doi.org/10.1021/ol5005438
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