MOCS3

From Wikipedia, the free encyclopedia


Molybdenum cofactor synthesis 3
Identifiers
Symbol(s) MOCS3; MGC9252; dJ914P20.3
External IDs OMIM: 609277 MGI: 1916622 HomoloGene: 6108
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 27304 69372
Ensembl ENSG00000124217 ENSMUSG00000074576
Uniprot O95396 n/a
Refseq NM_014484 (mRNA)
NP_055299 (protein)		 XM_130596 (mRNA)
XP_130596 (protein)
Location Chr 20: 49.01 - 49.01 Mb Chr 2: 167.92 - 167.92 Mb
Pubmed search [1] [2]

Molybdenum cofactor synthesis 3, also known as MOCS3, is a human gene.[1]

Molybdenum cofactor (MoCo) is necessary for the function of all molybdoenzymes. One of the enzymes required for the biosynthesis of MoCo is molybdopterin synthase (MPT synthase). The protein encoded by this gene adenylates and activates MPT synthase. This gene contains no introns. A pseudogene of this gene is present on chromosome 14.[1]

[edit] References

  1. ^ a b Entrez Gene: MOCS3 molybdenum cofactor synthesis 3.

[edit] Further reading

  • Reiss J, Johnson JL (2003). "Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH.". Hum. Mutat. 21 (6): 569-76. doi:10.1002/humu.10223. PMID 12754701. 
  • Johnson JL, Coyne KE, Rajagopalan KV, et al. (2002). "Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency.". Am. J. Med. Genet. 104 (2): 169-73. PMID 11746050. 
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865-71. doi:10.1038/414865a. PMID 11780052. 
  • Cortese MS, Caplan AB, Crawford RL (2003). "Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid).". BMC Evol. Biol. 2: 8. PMID 11972321. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S (2004). "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans.". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5946-51. doi:10.1073/pnas.0308191101. PMID 15073332. 
  • Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315-23. doi:10.1101/gr.2122004. PMID 15231747. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Matthies A, Nimtz M, Leimkühler S (2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.". Biochemistry 44 (21): 7912-20. doi:10.1021/bi0503448. PMID 15910006. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514. 
  • Krepinsky K, Leimkühler S (2007). "Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs.". FEBS J. 274 (11): 2778-87. doi:10.1111/j.1742-4658.2007.05811.x. PMID 17459099. 
 This article on a gene on chromosome 20 is a stub. You can help Wikipedia by expanding it.