MOCS3 explained

Adenylyltransferase and sulfurtransferase MOCS3 is an enzyme that in humans is encoded by the MOCS3 gene.^{[1] [2]}

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, encoded by MOCS2/Mocs2 in mammals). 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.

Further reading

• Reiss J, Johnson JL . Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH . Hum. Mutat. . 21 . 6 . 569–76 . 2003 . 12754701 . 10.1002/humu.10223 . 41013043 . free .
• Johnson JL . Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency . Am. J. Med. Genet. . 104 . 2 . 169–73 . 2002 . 11746050 . 10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8 . vanc. Coyne KE . Rajagopalan KV . 3 . Van Hove . Johan L.K. . MacKay . Mark . Pitt . James . Boneh . Avihu .
• Deloukas P . The DNA sequence and comparative analysis of human chromosome 20 . Nature . 414 . 6866 . 865–71 . 2002 . 11780052 . 10.1038/414865a . vanc. Matthews LH . Ashurst J . 3 . Burton . J. . Gilbert . J. G. R. . Jones . M. . Stavrides . G. . Almeida . J. P. . Babbage . A. K. . 2001Natur.414..865D . free .
• Cortese MS, Caplan AB, Crawford RL . 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 . 2003 . 11972321 . 10.1186/1471-2148-2-8 . 115864 . free .
• Strausberg RL . 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 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . vanc. Feingold EA . Grouse LH . 3 . Derge . JG . Klausner . RD . Collins . FS . Wagner . L . Shenmen . CM . Schuler . GD . 2002PNAS...9916899M . free .
• Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S . 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 . 2004 . 15073332 . 10.1073/pnas.0308191101 . 395903 . 2004PNAS..101.5946M . free .
• Lehner B, Sanderson CM . A protein interaction framework for human mRNA degradation . Genome Res. . 14 . 7 . 1315–23 . 2004 . 15231747 . 10.1101/gr.2122004 . 442147 .
• Gerhard DS . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . vanc. Wagner L . Feingold EA . 3 . Shenmen . CM . Grouse . LH . Schuler . G . Klein . SL . Old . S . Rasooly . R .
• Rual JF . Towards a proteome-scale map of the human protein-protein interaction network . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . vanc. Venkatesan K . Hao T . 3 . Hirozane-Kishikawa . Tomoko . Dricot . Amélie . Li . Ning . Berriz . Gabriel F. . Gibbons . Francis D. . Dreze . Matija . 2005Natur.437.1173R . 4427026 .
• Krepinsky K, Leimkühler S . 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 . 2007 . 17459099 . 10.1111/j.1742-4658.2007.05811.x . 82541137 . free .

Notes and References

1. Matthies A, Nimtz M, Leimkuhler S . 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 . May 2005 . 15910006 . 10.1021/bi0503448 .
2. Web site: Entrez Gene: MOCS3 molybdenum cofactor synthesis 3.