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MMAA

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{other uses}}

{{Infobox_gene}}

Methylmalonic aciduria type A protein, mitochondrial also known as MMAA is a protein that in humans is encoded by the MMAA gene.{{cite journal |vauthors=Dobson CM, Wai T, Leclerc D, Wilson A, Wu X, Doré C, Hudson T, Rosenblatt DS, Gravel RA | title = Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 24 | pages = 15554–9 |date=November 2002 | pmid = 12438653 | pmc = 137755 | doi = 10.1073/pnas.242614799 | bibcode = 2002PNAS...9915554D | doi-access = free }}

Function

The protein encoded by this gene is involved in the translocation of cobalamin into the mitochondrion, where it is used in the final steps of adenosylcobalamin synthesis. Adenosylcobalamin is a coenzyme required for the activity of methylmalonyl-CoA mutase.{{cite web | title = Entrez Gene: MMAA methylmalonic aciduria (cobalamin deficiency) cblA type | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=166785 }}

Clinical significance

Mutations in the MMAA gene are associated with methylmalonic acidemia.{{cite journal |vauthors=Lerner-Ellis JP, Dobson CM, Wai T, Watkins D, Tirone JC, Leclerc D, Doré C, Lepage P, Gravel RA, Rosenblatt DS | title = Mutations in the MMAA gene in patients with the cblA disorder of vitamin B12 metabolism | journal = Hum. Mutat. | volume = 24 | issue = 6 | pages = 509–16 |date=December 2004 | pmid = 15523652 | doi = 10.1002/humu.20104 | s2cid = 34883155 | doi-access = free }}

References

{{Reflist}}

External links

  • [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=mma GeneReviews/NCBI/NIH/UW entry on Methylmalonic Acidemia]

Further reading

{{refbegin | 2}}

  • {{cite journal |vauthors=Padovani D, Labunska T, Banerjee R |title=Energetics of interaction between the G-protein chaperone, MeaB, and B12-dependent methylmalonyl-CoA mutase. |journal=J. Biol. Chem. |volume=281 |issue= 26 |pages= 17838–44 |year= 2006 |pmid= 16641088 |doi= 10.1074/jbc.M600047200 |doi-access= free }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 }}
  • {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |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 |doi-access= free }}
  • {{cite journal |vauthors=Yang X, Sakamoto O, Matsubara Y, etal |title=Mutation analysis of the MMAA and MMAB genes in Japanese patients with vitamin B(12)-responsive methylmalonic acidemia: identification of a prevalent MMAA mutation. |journal=Mol. Genet. Metab. |volume=82 |issue= 4 |pages= 329–33 |year= 2004 |pmid= 15308131 |doi= 10.1016/j.ymgme.2004.05.002 }}
  • {{cite journal |vauthors=Merinero B, Pérez B, Pérez-Cerdá C, etal |title=Methylmalonic acidaemia: examination of genotype and biochemical data in 32 patients belonging to mut, cblA or cblB complementation group. |journal=J. Inherit. Metab. Dis. |volume=31 |issue= 1 |pages= 55–66 |year= 2008 |pmid= 17957493 |doi= 10.1007/s10545-007-0667-y |hdl=10553/49375 |s2cid=26112025 |hdl-access=free }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Hörster F, Baumgartner MR, Viardot C, etal |title=Long-term outcome in methylmalonic acidurias is influenced by the underlying defect (mut0, mut-, cblA, cblB). |journal=Pediatr. Res. |volume=62 |issue= 2 |pages= 225–30 |year= 2007 |pmid= 17597648 |doi= 10.1203/PDR.0b013e3180a0325f |doi-access= free }}
  • {{cite journal |vauthors=Honjo RS, Casella EB, Vieira MA, etal |title=Spondylocostal dysostosis associated with methylmalonic aciduria. |journal=Genet Test Mol Biomarkers |volume=13 |issue= 2 |pages= 181–3 |year= 2009 |pmid= 19371216 |doi= 10.1089/gtmb.2008.0069 }}

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{{NLM content}}

{{Metabolism of vitamins, coenzymes, and cofactors}}

{{gene-4-stub}}