MOCOS

MOCOS
Identifiers
Aliases	MOCOS, hMCS, MCS, MOS, molybdenum cofactor sulfurase
External IDs	OMIM: 613274; MGI: 1915841; HomoloGene: 9931; GeneCards: MOCOS; OMA:MOCOS - orthologs
Gene location (Human)
Chr.	Chromosome 18 (human)
End	36,272,157 bp
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)
End	24,834,632 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; right lobe of liver; ; palpebral conjunctiva; ; right adrenal gland; ; right adrenal cortex; ; jejunal mucosa; ; left adrenal gland; ; left adrenal cortex; ; buccal mucosa cell; ; duodenum;
	Top expressed in
	granulocyte; ; left lobe of liver; ; esophagus; ; primary oocyte; ; jejunum; ; gastrula; ; respiratory epithelium; ; olfactory system; ; olfactory epithelium; ; duodenum;
	More reference expression data
	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
	55034
	68591
	ENSG00000075643
	ENSMUSG00000039616
	Q96EN8
	Q14CH1
	NM_017947
	NM_026779
	NP_060417
	NP_081055
	Wikidata
View/Edit Human	View/Edit Mouse

Molybdenum cofactor sulfurase is an enzyme that in humans is encoded by the MOCOS gene.^[5]^[6]

MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase (XDH) and aldehyde oxidase (AOX1), which is required for their enzymatic activities.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000075643 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000039616 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T (April 2001). "Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II". Biochemical and Biophysical Research Communications. 282 (5): 1194–200. doi:10.1006/bbrc.2001.4719. PMID 11302742.
^ "Entrez Gene: MOCOS molybdenum cofactor sulfurase".

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.

This article on a gene on human chromosome 18 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000075643 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000039616 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11302742-5] Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T (April 2001). "Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II". Biochemical and Biophysical Research Communications. 282 (5): 1194–200. doi:10.1006/bbrc.2001.4719. PMID 11302742.

[entrez-6] "Entrez Gene: MOCOS molybdenum cofactor sulfurase".

[1]

[2]

[3]

[4]

[5]

[6]

v t e Transferases: sulfur-containing group (EC 2.8)
2.8.1: Sulfurtransferases	Thiosulfate sulfurtransferase Rhodanese 3-mercaptopyruvate sulfurtransferase thiosulfate—thiol sulfurtransferase tRNA sulfurtransferase thiosulfate—dithiol sulfurtransferase biotin synthase cysteine desulfurase lipoyl synthase molybdenum cofactor sulfurtransferase thiazole synthase molybdopterin synthase sulfurtransferase molybdopterin synthase tRNA-uridine 2-sulfurtransferase () tRNA-5-taurinomethyluridine 2-sulfurtransferase () tRNA-5-methyluridine⁵⁴ 2-sulfurtransferase () L-aspartate semialdehyde sulfurtransferase ()
2.8.2: Sulfotransferases	aryl sulfotransferase amine sulfotransferase estrone sulfotransferase chondroitin 4-sulfotransferase choline sulfotransferase UDP-N-acetylgalactosamine-4-sulfate sulfotransferase heparan sulfate-glucosamine N-sulfotransferase tyrosine-ester sulfotransferase Renilla-luciferin sulfotransferase galactosylceramide sulfotransferase psychosine sulfotransferase bile salt sulfotransferase steroid sulfotransferase thiol sulfotransferase chondroitin 6-sulfotransferase cortisol sulfotransferase triglucosylalkylacylglycerol sulfotransferase protein-tyrosine sulfotransferase keratan sulfotransferase aryl-sulfate sulfotransferase (heparan sulfate)-glucosamine 3-sulfotransferase 1 desulfoglucosinolate sulfotransferase flavonol 3-sulfotransferase quercetin-3-sulfate 3′-sulfotransferase quercetin-3-sulfate 4′-sulfotransferase quercetin-3,3′-bissulfate 7-sulfotransferase (heparan sulfate)-glucosamine 3-sulfotransferase 2 (heparan sulfate)-glucosamine 3-sulfotransferase 3 petromyzonol sulfotransferase scymnol sulfotransferase N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase glycochenodeoxycholate sulfotransferase dermatan 4-sulfotransferase desulfo-A47934 sulfotransferase () trehalose 2-sulfotransferase () aliphatic desulfoglucosinolate sulfotransferase () hydroxyjasmonate sulfotransferase () ω-hydroxy-β-dihydromenaquinone-9 sulfotransferase (*) Alcohol sulfotransferase Tyrosylprotein sulfotransferase
2.8.3: CoA-transferases	Propionate CoA-transferase oxalate CoA-transferase malonate CoA-transferase 3-oxoacid CoA-transferase 3-oxoadipate CoA-transferase succinyl-CoA—Dcitramalate CoA-transferase acetate CoA-transferase butyrate—acetoacetate CoA-transferase citrate CoA-transferase citramalate CoA-transferase glutaconate CoA-transferase succinate—hydroxymethylglutarate CoA-transferase 5-hydroxypentanoate CoA-transferase succinyl-CoA:(R)-benzylsuccinate CoA-transferase formyl-CoA transferase cinnamoyl-CoA:phenyllactate CoA-transferase succinyl-CoA:acetate CoA-transferase () CoA:oxalate CoA-transferase () succinyl-CoA—D-citramalate CoA-transferase () L-carnitine CoA-transferase () succinyl-CoA—L-malate CoA-transferase () caffeate CoA-transferase () (R)-2-hydroxy-4-methylpentanoate CoA-transferase () bile acid CoA-transferase () succinyl-CoA:mesaconate CoA transferase (*)
2.8.4: Alkylthio	2.8.4: Coenzyme-B sulfoethylthiotransferase arsenate-mycothiol transferase tRNA-2-methylthio-N⁶-dimethylallyladenosine synthase () [ribosomal protein S12] (aspartate⁸⁹-C³)-methylthiotransferase () tRNA (N⁶-L-threonylcarbamoyladenosine³⁷-C²)-methylthiotransferase (*)
2.8.5:	2.8.5: S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent) () L-cysteine S-thiosulfotransferase ()

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

References

Further reading