Department of Chemistry, Boston University , 590 Commonwealth Avenue, Boston, Massachussetts 02215, United States.
Org Lett. 2014 Apr 18;16(8):2122-5. doi: 10.1021/ol5005438. Epub 2014 Mar 31.
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.
OvoA 在卵硫醇生物合成中是一种单核非血红素铁酶，催化组氨酸和半胱氨酸之间的氧化偶联。它还可以催化赫曲汀和半胱氨酸之间的氧化偶联，但具有不同的区域选择性。由于该反应在工业生产麦硫因方面具有潜在的应用价值，因此在本研究中，我们通过三种不同的测定方法相结合，对 OvoA 进行了系统的表征。我们的研究表明，OvoA 还可以催化半胱氨酸氧化为半胱氨酸亚磺酸或胱氨酸。值得注意的是，其一个底物组氨酸的微小修饰可以系统地调节这些由 OvoA 催化的反应。
