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 |
BRENDA | 1.8.3.7 |
EC2PDB | 1.8.3.7 |
ExplorEnz | 1.8.3.7 |
PRIAM enzyme-specific profiles | 1.8.3.7 |
KEGG Ligand Database for Enzyme Nomenclature | 1.8.3.7 |
IUBMB Enzyme Nomenclature | 1.8.3.7 |
IntEnz | 1.8.3.7 |
MEDLINE | Find literature relating to 1.8.3.7 |
MetaCyc | 1.8.3.7 |
Rhea expert-curated reactions | 1.8.3.7 |
UniProtKB/Swiss-Prot |
|
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