Oxidoreductases;
Acting on a sulfur group of donors;
With oxygen as acceptor
BRITE hierarchy

[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)

a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O [RN:R11878]

R11878
Reaction

[sulfatase]-L-cysteine [CPD:C21740];
O2 [CPD:C00007];
a thiol

Requires a copper cofactor and Ca2+. The enzyme, which is found in both prokaryotes and eukaryotes, catalyses a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. Glutathione alo acts in vitro, but it is not known whether it is used in vivo.

EC 1.8.3.7 created 2014