MOCOS
Function
Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime.
Involvement in disease
Xanthinuria 2
XAN2
A disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. In addition, XAN2 patients cannot metabolize allopurinol into oxypurinol due to dual deficiency of xanthine dehydrogenase and aldehyde oxidase.
None
The disease is caused by variants affecting the gene represented in this entry.
Sequence Similarities
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.
Alternative names
Molybdenum cofactor sulfurase, MCS, MOS, MoCo sulfurase, hMCS, Molybdenum cofactor sulfurtransferase, MOCOS