MOCS3

MOCS3

Molybdenum cofactor synthesis 3, also known as MOCS3, is a human gene.cite web | title = Entrez Gene: MOCS3 molybdenum cofactor synthesis 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27304| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: MOCS3 molybdenum cofactor synthesis 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27304| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Reiss J, Johnson JL |title=Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH. |journal=Hum. Mutat. |volume=21 |issue= 6 |pages= 569–76 |year= 2003 |pmid= 12754701 |doi= 10.1002/humu.10223
*cite journal | author=Johnson JL, Coyne KE, Rajagopalan KV, "et al." |title=Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency. |journal=Am. J. Med. Genet. |volume=104 |issue= 2 |pages= 169–73 |year= 2002 |pmid= 11746050 |doi=
*cite journal | author=Deloukas P, Matthews LH, Ashurst J, "et al." |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a
*cite journal | author=Cortese MS, Caplan AB, Crawford RL |title=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). |journal=BMC Evol. Biol. |volume=2 |issue= |pages= 8 |year= 2003 |pmid= 11972321 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S |title=Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 16 |pages= 5946–51 |year= 2004 |pmid= 15073332 |doi= 10.1073/pnas.0308191101
*cite journal | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Matthies A, Nimtz M, Leimkühler S |title=Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry. |journal=Biochemistry |volume=44 |issue= 21 |pages= 7912–20 |year= 2005 |pmid= 15910006 |doi= 10.1021/bi0503448
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Krepinsky K, Leimkühler S |title=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. |journal=FEBS J. |volume=274 |issue= 11 |pages= 2778–87 |year= 2007 |pmid= 17459099 |doi= 10.1111/j.1742-4658.2007.05811.x

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