EC Number |
Natural Substrates |
---|
1.14.99.52 | hercynine + gamma-L-glutamyl-L-cysteine + O2 |
- |
1.14.99.52 | hercynine + L-cysteine + O2 |
- |
1.14.99.52 | hercynine + L-cysteine + O2 |
reaction of EC 1.14.99.51 |
1.14.99.52 | L-histidine + L-cysteine + O2 |
- |
1.14.99.52 | more |
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50 |
1.14.99.52 | more |
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase |
1.14.99.52 | more |
OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between L-histidine and L-cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity (cf. Ec 1.14.99.51). OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine, OvoA has cysteine dioxygenase activity (cf. EC 1.13.11.20). A 3-His catalytic triad is a prerequisite for the cysteine dioxygenase activity |
1.14.99.52 | more |
short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production |
1.14.99.52 | more |
the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency |