Biology:MOCOS

From HandWiki
Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Molybdenum cofactor sulfurase is an enzyme that in humans is encoded by the MOCOS gene.[1][2]

MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase (XDH) and aldehyde oxidase (AOX1), which is required for their enzymatic activities.[1]

References

  1. 1.0 1.1 "Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II". Biochemical and Biophysical Research Communications 282 (5): 1194–200. April 2001. doi:10.1006/bbrc.2001.4719. PMID 11302742. 
  2. "Entrez Gene: MOCOS molybdenum cofactor sulfurase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55034. 

Further reading

  • "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
  • "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. November 2003. doi:10.1016/s0026-0495(03)00272-5. PMID 14624414. 
  • "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology 24 (10): 1285–92. October 2006. doi:10.1038/nbt1240. PMID 16964243. 
  • "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. May 2007. doi:10.1016/j.ymgme.2007.02.005. PMID 17368066.