SUMF1 mediates the oxidation of cysteine to formylglycine, producing active arylsulfatases
ARS + NAD+ → active ARS + NADH + H2S + H+
- Reactome
- R-HSA-1614362
- Compartment
- endoplasmic reticulum lumen
- Rhea
- None recorded
Inputs
- ARSR-HSA-1614312, endoplasmic reticulum lumen
- NAD+CHEBI:57540, C21H26N7O14P2, endoplasmic reticulum lumen
Outputs
- active ARSR-HSA-1614309, endoplasmic reticulum lumen
- NADHCHEBI:57945, C21H27N7O14P2, endoplasmic reticulum lumen
- H2SCHEBI:29919, HS, endoplasmic reticulum lumen
- H+CHEBI:15378, H, endoplasmic reticulum lumen
Catalysed by
- oxidoreductase activity of SUMF1 [endoplasmic reticulum lumen]EC 1; UniProt Q8NBK3
Literature
- Molecular characterization of the human Calpha-formylglycine-generating enzyme J Biol Chem, 2005
- The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases Cell, 2003
- The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes Gene, 2003
- Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme Cell, 2003
- The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri Eur J Biochem, 1996
- A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease Bioessays, 1998