| Accepted Name |
|---|
| 2-oxoethane-1-sulfonamide synthase
|
| Reaction catalysed |
|---|
| L-cysteine + 2 O2 = 2-oxoethane-1-sulfonamide + CO2 + H2O |
| Comment(s) |
|---|
- The enzyme, characterized from the bacterium Streptomyces sp.
NCIMB40513, is a cupin dioxygenase that participates in the
biosynthesis of the monoterpene alkaloids altemicidin, SB-203207 and
SB-203208.
- The enzyme catalyzes a complex transformation: it first catalyzes a
monooxygenation of the sulfur atom, which results in decarboxylation
and formation of (Z)-(2-aminovinyl)sulfanolate.
- This is followed by a dioxygenation of the sulfur atom, forming (Z)-
2-aminoethene-1-sulfonate.
- The resulting compound is unstable and undergoes an intramolecular
rearrangement in which the amino group moves onto the oxidized sulfur
atom, displacing an oxygen atom in the form of a water molecule and
forming an SN bond.
- Another water molecule (not shown in the overall reaction) donates an
oxygen atom that replaces the nitrogen at the other end of the
molecule.
|
| Cross-references |
|---|
| BRENDA | 1.13.11.95 |
| EC2PDB | 1.13.11.95 |
| ExplorEnz | 1.13.11.95 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.13.11.95 |
| IUBMB Enzyme Nomenclature | 1.13.11.95 |
| MEDLINE | Find literature relating to 1.13.11.95 |
| MetaCyc | 1.13.11.95 |
| Rhea expert-curated reactions | 1.13.11.95 |
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