MPST

Mercaptopyruvate sulfurtransferase, also known as MPST, is a human gene.cite web | title = Entrez Gene: MPST mercaptopyruvate sulfurtransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4357| accessdate = ]

PBB_Summary
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summary_text = This gene encodes a protein which can function as a monomer or as a disulfide-linked homodimer and which catalyzes the transfer of a sulfur ion from 3-mercaptopyruvate to cyanide or other thiol compounds. It may be involved in cyanide degradation and in thiosulfate biosynthesis. The encoded cytoplasmic protein is a member of the rhodanese family but is not rhodanese itself, which is a mitochondrial protein. Alternatively spliced transcript variants encoding the same protein have been identified.cite web | title = Entrez Gene: MPST mercaptopyruvate sulfurtransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4357| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Billaut-Laden I, Rat E, Allorge D, "et al." |title=Evidence for a functional genetic polymorphism of the human mercaptopyruvate sulfurtransferase (MPST), a cyanide detoxification enzyme. |journal=Toxicol. Lett. |volume=165 |issue= 2 |pages= 101–11 |year= 2006 |pmid= 16545926 |doi= 10.1016/j.toxlet.2006.02.002
*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=Collins JE, Wright CL, Edwards CA, "et al." |title=A genome annotation-driven approach to cloning the human ORFeome. |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*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=Dunham I, Shimizu N, Roe BA, "et al." |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031
*cite journal | author=Aita N, Ishii K, Akamatsu Y, "et al." |title=Cloning and expression of human liver rhodanese cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 1 |pages= 56–60 |year= 1997 |pmid= 9070219 |doi= 10.1006/bbrc.1996.6046
*cite journal | author=Pallini R, Guazzi GC, Cannella C, Cacace MG |title=Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes. |journal=Biochem. Biophys. Res. Commun. |volume=180 |issue= 2 |pages= 887–93 |year= 1991 |pmid= 1953758 |doi=

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