MOCOS

"Molybdenum cofactor sulfurase" redirects here. For the similar enzyme in plants also sometimes called Molybdenum cofactor sulfurase, see Molybdenum cofactor sulfurtransferase.

Molybdenum cofactor sulfurase is an enzyme that in humans is encoded by the MOCOS gene.

MOCOS
Identifiers
Aliases	MOCOS, hMCS, MCS, MOS, molybdenum cofactor sulfurase
External IDs	OMIM: 613274 MGI: 1915841 HomoloGene: 9931 GeneCards: MOCOS
Gene location (Human) Chr. Chromosome 18 (human) Band 18q12.2 Start 36,187,497 bp End 36,272,157 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 A2 Start 24,786,748 bp End 24,834,632 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte right lobe of liver palpebral conjunctiva right adrenal gland jejunal mucosa left adrenal gland duodenum bronchial epithelial cell stromal cell of endometrium skin of abdomen Top expressed in left lobe of liver esophagus jejunum respiratory epithelium olfactory epithelium duodenum ileum lip submandibular gland proximal tubule More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity molybdenum ion binding pyridoxal phosphate binding protein binding catalytic activity Mo-molybdopterin cofactor sulfurase activity molybdenum cofactor sulfurtransferase activity lyase activity Cellular component cytosol cellular component Biological process Mo-molybdopterin cofactor biosynthetic process molybdopterin cofactor biosynthetic process molybdopterin cofactor metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55034 68591 Ensembl ENSG00000075643 ENSMUSG00000039616 UniProt Q96EN8 Q14CH1 RefSeq (mRNA) NM_017947 NM_026779 RefSeq (protein) NP_060417 NP_081055 Location (UCSC) Chr 18: 36.19 – 36.27 Mb Chr 18: 24.79 – 24.83 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase (XDH) and aldehyde oxidase (AOX1), which is required for their enzymatic activities.

Further reading

• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Yamamoto T, Moriwaki Y, Takahashi S, Tsutsumi Z, Tuneyoshi K, Matsui K, et al. (November 2003). "Identification of a new point mutation in the human molybdenum cofactor sulferase gene that is responsible for xanthinuria type II". Metabolism. 52 (11): 1501–4. doi:10.1016/s0026-0495(03)00272-5. PMID 14624414.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
• Peretz H, Naamati MS, Levartovsky D, Lagziel A, Shani E, Horn I, et al. (May 2007). "Identification and characterization of the first mutation (Arg776Cys) in the C-terminal domain of the Human Molybdenum Cofactor Sulfurase (HMCS) associated with type II classical xanthinuria". Molecular Genetics and Metabolism. 91 (1): 23–9. doi:10.1016/j.ymgme.2007.02.005. PMID 17368066.