ID   1.13.11.95
DE   2-oxoethane-1-sulfonamide synthase.
CA   L-cysteine + 2 O2 = 2-oxoethane-1-sulfonamide + CO2 + H2O.
CC   -!- The enzyme, characterized from the bacterium Streptomyces sp.
CC       NCIMB40513, is a cupin dioxygenase that participates in the
CC       biosynthesis of the monoterpene alkaloids altemicidin, SB-203207 and
CC       SB-203208.
CC   -!- The enzyme catalyzes a complex transformation: it first catalyzes a
CC       monooxygenation of the sulfur atom, which results in decarboxylation
CC       and formation of (Z)-(2-aminovinyl)sulfanolate.
CC   -!- This is followed by a dioxygenation of the sulfur atom, forming (Z)-
CC       2-aminoethene-1-sulfonate.
CC   -!- The resulting compound is unstable and undergoes an intramolecular
CC       rearrangement in which the amino group moves onto the oxidized sulfur
CC       atom, displacing an oxygen atom in the form of a water molecule and
CC       forming an SN bond.
CC   -!- Another water molecule (not shown in the overall reaction) donates an
CC       oxygen atom that replaces the nitrogen at the other end of the
CC       molecule.
DR   P0DY49, SBZM_STRSQ ;
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