|
type |
Journal Article |
authors |
Naowarojna N, Huang P, Cai Y, Song H, Wu L, Cheng R, Li Y, Wang S, Lyu H, Zhang L, Zhou J, Liu P. |
title |
In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C-S Lyase and Methyltransferase Reactions. |
journal |
Org Lett. |
Activity |
ovob |
Family |
ovob |
PLP Fold Type |
1 |
sel |
selected |
ui |
30141637 |
year |
(2018) |
volume |
20 |
number |
17 |
pages |
5427-5430 |
| |
keywords |
10.1021/acs.orglett.8b02332 |
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. |
last changed |
2019/01/22 12:27 |
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