MOCOS 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. Defects in MOCOS are the cause of xanthinuria type 2 (XU2). Xanthinuria is 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, patient suffering of XU2 cannot metabolize allopurinol into oxypurinol due to dual deficiency of xanthine dehydrogenase and aldehyde oxidase. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily. Note: This description may include information from UniProtKB.
Protein type: EC; Lyase
Chromosomal Location of Human Ortholog: 18q12.2
Cellular Component:  cytosol
Molecular Function:  lyase activity; Mo-molybdopterin cofactor sulfurase activity; molybdenum cofactor sulfurtransferase activity; molybdenum ion binding; protein binding; pyridoxal phosphate binding
Biological Process:  Mo-molybdopterin cofactor biosynthetic process; molybdopterin cofactor biosynthetic process; molybdopterin cofactor metabolic process
Disease: Xanthinuria, Type Ii
Reference #:  Q96EN8 (UniProtKB)
Alt. Names/Synonyms: FLJ20733; HMCS; MCS; MoCo sulfurase; MOCOS; Molybdenum cofactor sulfurase; MOS
Gene Symbols: MOCOS
Molecular weight: 98,120 Da
Basal Isoelectric point: 6.23  Predict pI for various phosphorylation states
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Protein Structure Not Found.

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