Application | Comment | Organism |
---|---|---|
synthesis | the ergothioneine biosynthetic pathway (EgtA-EgtE catalysis) provides an opportunity for ergothioneine production through metabolic engineering, but the kinetic properties and the presence of side-reaction render OvoA not suitable for use in ergothioneine production through metabolic engineering | Erwinia tasmaniensis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | non-heme iron, required for catalysis | Erwinia tasmaniensis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
hercynine + L-cysteine + O2 | Erwinia tasmaniensis | reaction of EC 1.14.99.51 | S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
L-histidine + L-cysteine + O2 | Erwinia tasmaniensis | - |
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Erwinia tasmaniensis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hercynine + L-cysteine + O2 | reaction of EC 1.14.99.51 | Erwinia tasmaniensis | S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
L-histidine + L-cysteine + O2 | - |
Erwinia tasmaniensis | S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
additional information | when OvoA's native substrate histidine is replaced by hercynine, OvoA can catalyze a one-step transformation reaction of hercynylcysteine S-oxide synthase, EC 1.14.99.51, resulting in kobs changes by 2fold for hercynine, while Km for cysteine increases from 0.3 mM to 3.19 mM. OvoA preferentially uses histidine and cysteine. OvoA also catalyzes the oxidation of cysteine to cysteine sulfinic acid, EC 1.13.11.20. Enzyme activity determination using : a 1H NMR assay of chemical shift of the imidazole hydrogen atoms | Erwinia tasmaniensis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
OvoA | - |
Erwinia tasmaniensis |
General Information | Comment | Organism |
---|---|---|
evolution | OvoA and EgtB, EC 1.14.99.50, are related in sequence, while they are biochemically distinct | Erwinia tasmaniensis |
metabolism | enzyme OvoA is responsible for the oxidative C-S bond formation in ovothiol biosynthesis. OvoA in ovothiol biosynthesis has a relaxed substrate specificity | Erwinia tasmaniensis |