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Information on EC - formylglycine-generating enzyme

for references in articles please use BRENDA:EC1.8.3.7
EC Tree
     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.3 With oxygen as acceptor
       formylglycine-generating enzyme
IUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
a [sulfatase]-L-cysteine
a [sulfatase]-3-oxo-L-alanine
AtsB, C-alpha-formylglycine-generating enzyme 1, Calpha-formylglycine-generating enzyme, Calpha-formylglycine-generating enzyme 1, FGE, FGly-generating enzyme, formylglycine generating enzyme, sulfatase-modifying factor 1, SUMF1, more
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
show the reaction diagram
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