Structural highlights
Function
B2VJB8_ERWT9
Publication Abstract from PubMed
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.
In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C-S Lyase and Methyltransferase Reactions.,Naowarojna N, Huang P, Cai Y, Song H, Wu L, Cheng R, Li Y, Wang S, Lyu H, Zhang L, Zhou J, Liu P Org Lett. 2018 Sep 7;20(17):5427-5430. doi: 10.1021/acs.orglett.8b02332. Epub, 2018 Aug 24. PMID:30141637[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Naowarojna N, Huang P, Cai Y, Song H, Wu L, Cheng R, Li Y, Wang S, Lyu H, Zhang L, Zhou J, Liu P. In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C-S Lyase and Methyltransferase Reactions. Org Lett. 2018 Sep 7;20(17):5427-5430. doi: 10.1021/acs.orglett.8b02332. Epub, 2018 Aug 24. PMID:30141637 doi:http://dx.doi.org/10.1021/acs.orglett.8b02332
