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ENZYME entry: EC 1.8.3.7

Accepted Name
Formylglycine-generating enzyme.
Alternative Name(s)
C-alpha-formylglycine-generating enzyme 1.
Sulfatase-modifying factor 1.
Reaction catalysed
A [sulfatase]-L-cysteine + O(2) + 2 a thiol <=> a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H(2)O
Cofactor(s)
Ca(2+); Cu cation.
Comment(s)
  • The enzyme, which is found in both prokaryotes and eukaryotes, catalyzes 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.
Cross-references
BRENDA1.8.3.7
EC2PDB1.8.3.7
ExplorEnz1.8.3.7
PRIAM enzyme-specific profiles1.8.3.7
KEGG Ligand Database for Enzyme Nomenclature1.8.3.7
IUBMB Enzyme Nomenclature1.8.3.7
IntEnz1.8.3.7
MEDLINEFind literature relating to 1.8.3.7
MetaCyc1.8.3.7
UniProtKB/Swiss-Prot
I6Y8I5, FGE_MYCTU;  Q9F3C7, FGE_STRCO;  D1A7C3, FGE_THECD;  
Q0P5L5, SUMF1_BOVIN;  Q8NBK3, SUMF1_HUMAN;  Q8R0F3, SUMF1_MOUSE;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.3.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-