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EC 1.8.3.7 Details
EC number
1.8.3.7
Accepted name
formylglycine-generating enzyme
Reaction
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
Other name(s)
sulfatase-modifying factor 1, Cα-formylglycine-generating enzyme 1, SUMF1 (gene name)
Systematic name
[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)
Comment
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.
History
created 2014
EC Tree
1.1.1.68 created 1965, deleted 1978 [transferred to EC 1.1.99.15, deleted 1980]
1.1.1.70 created 1965, deleted 1978
1.1.1.74 created 1972, deleted 1976
1.1.1.89 created 1972, deleted 1976
1.1.1.109 created 1972, deleted 1976
1.1.1.139 created 1972, deleted 1978
1.1.1.155 created 1976, deleted 2004
1.1.1.171 created 1978, deleted 1984
1.1.1.180 created 1983, deleted 1984
1.1.1.182 created 1983, deleted 1990
1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004
1.1.1.242 created 1992, deleted 2001
1.1.1.249 provisional version created 1999, deleted 1999 (reinstated 2001 as EC 2.5.1.46)
1.1.1.253 created 1999, deleted 2003