MOCS3
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
Adenylyltransferase and sulfurtransferase MOCS3 is an enzyme that in humans is encoded by the MOCS3 gene.{{cite journal |vauthors=Matthies A, Nimtz M, Leimkuhler 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 |date=May 2005 | pmid = 15910006 | doi = 10.1021/bi0503448 }}{{cite web | title = Entrez Gene: MOCS3 molybdenum cofactor synthesis 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27304}}
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.
References
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Further reading
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- {{cite journal |vauthors=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 |s2cid=41013043 |doi-access=free }}
- {{cite journal | author=Johnson JL |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=10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8 |name-list-style=vanc| author2=Coyne KE | author3=Rajagopalan KV | display-authors=3 | last4=Van Hove | first4=Johan L.K. | last5=MacKay | first5=Mark | last6=Pitt | first6=James | last7=Boneh | first7=Avihu }}
- {{cite journal | author=Deloukas P |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 |name-list-style=vanc| author2=Matthews LH | author3=Ashurst J | display-authors=3 | last4=Burton | first4=J. | last5=Gilbert | first5=J. G. R. | last6=Jones | first6=M. | last7=Stavrides | first7=G. | last8=Almeida | first8=J. P. | last9=Babbage | first9=A. K. |bibcode=2001Natur.414..865D | doi-access=free }}
- {{cite journal |vauthors=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|pages= 8 |year= 2003 |pmid= 11972321 |doi=10.1186/1471-2148-2-8 | pmc=115864 |doi-access=free }}
- {{cite journal | author=Strausberg RL |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 | pmc=139241 |name-list-style=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD |bibcode=2002PNAS...9916899M |doi-access=free }}
- {{cite journal |vauthors=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 | pmc=395903 |bibcode=2004PNAS..101.5946M |doi-access=free }}
- {{cite journal |vauthors=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 | pmc=442147 }}
- {{cite journal | author=Gerhard DS |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 | pmc=528928 |name-list-style=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
- {{cite journal | author=Rual JF |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 |name-list-style=vanc| author2=Venkatesan K | author3=Hao T | display-authors=3 | last4=Hirozane-Kishikawa | first4=Tomoko | last5=Dricot | first5=Amélie | last6=Li | first6=Ning | last7=Berriz | first7=Gabriel F. | last8=Gibbons | first8=Francis D. | last9=Dreze | first9=Matija |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
- {{cite journal |vauthors=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 |s2cid=82541137 |doi-access=free }}
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{{Metabolism of vitamins, coenzymes, and cofactors}}
{{gene-20-stub}}