期刊
ORGANIC LETTERS
卷 20, 期 17, 页码 5427-5430出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.8b02332
关键词
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资金
- National Science Foundation [CHE-1309148]
- Strategic Priority Research Program (B) of the CAS [XDB20000000]
- National Science Foundation of China [31430002, 31320103911]
- Shanghai Science and Technology Committee [17DZ1205402]
- Warren McLoed Fellowship from the Boston University Marine Program
- China Scholarship Council
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 pi-N methyltransferase.
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