MPST

From Wikipedia, the free encyclopedia

Mercaptopyruvate sulfurtransferase

Identifiers

MPST; MST; MGC24539; TST2

External IDs

OMIM: 602496 MGI: 2179733 HomoloGene: 87798

Gene ontology
Molecular Function:	• thiosulfate sulfurtransferase activity • transferase activity • 3-mercaptopyruvate sulfurtransferase activity
Cellular Component:	• mitochondrial matrix
Biological Process:	• sulfate transport • cyanate catabolic process • response to toxin

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001013436 (mRNA)
NP_001013454 (protein)

NM_138670 (mRNA)
NP_619611 (protein)

Location

Chr 22: 35.75 - 35.76 Mb

Chr 15: 78.23 - 78.24 Mb

Pubmed search

[1]

[2]

Mercaptopyruvate sulfurtransferase, also known as MPST, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: MPST mercaptopyruvate sulfurtransferase.

[edit] Further reading

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