| Literature DB >> 30141637 |
Nathchar Naowarojna1, Pei Huang1,2, Yujuan Cai3, Heng Song1, Lian Wu3, Ronghai Cheng1, Yan Li3, Shu Wang1, Huijue Lyu1, Lixin Zhang1, Jiahai Zhou3,4, Pinghua Liu1.
Abstract
Ovothiols are thiolhistidine derivatives. The first step of ovothiol biosynthesis is OvoA-catalyzed oxidative coupling between histidine and cysteine. In this report, the remaining steps of ovothiol A biosynthesis were reconstituted in vitro. ETA_14770 (OvoB) was reported as a PLP-dependent sulfoxide lyase, responsible for mercaptohistidine production. OvoA was found to be a bifunctional enzyme, which mediates both oxidative C-S bond formation and methylation of mercaptohistidine to afford ovothiol A. Besides reconstituting the whole biosynthetic pathway, two unique features proposed in the literature were also examined: a potential cysteine-recycling mechanism of the C-S lyase (OvoB) and the selectivity of the π- N methyltransferase.Entities:
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Year: 2018 PMID： 30141637 DOI： 10.1021/acs.orglett.8b02332
Source DB: PubMed Journal: Org Lett ISSN： 1523-7052 Impact factor: 6.005