metabolism of cobalamin associated B
Last updated 1 Jun 2021
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The MMAB gene provides instructions for making an enzyme that is involved in the formation of a compound called adenosylcobalamin (AdoCbl). AdoCbl, which is derived from vitamin B12 (also known as cobalamin), is necessary for the normal function of another enzyme known as methylmalonyl CoA mutase. This enzyme helps break down certain proteins, fats (lipids), and cholesterol.
Normal function
The MMAB gene provides instructions for making an enzyme that is involved in the formation of a compound called adenosylcobalamin (AdoCbl). AdoCbl, which is derived from vitamin B12 (also known as cobalamin), is necessary for the normal function of another enzyme known as methylmalonyl CoA mutase. This enzyme helps break down certain proteins, fats (lipids), and cholesterol.
The MMAB enzyme is active in mitochondria, which are specialized structures inside cells that serve as energy-producing centers. Once vitamin B12 has been transported into mitochondria, the MMAB enzyme converts a form of the vitamin called cob(I)alamin to AdoCbl. Studies suggest that this enzyme may also deliver AdoCbl to methylmalonyl CoA mutase.
Conditions referring to this gene or chromosome
Other names
ATP:Cob(I)alamin Adenosyltransferase
ATR
cblB
CFAP23
cob(I)alamin adenosyltransferase
methylmalonic aciduria (cobalamin deficiency) cblB type
methylmalonic aciduria (cobalamin deficiency) type B
MMAB_HUMAN
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Further reading and references
- metabolism of cobalamin associated B; MedlinePlus, National Library of Medicine.
- Chandler RJ, Venditti CP. Genetic and genomic systems to study methylmalonic acidemia. Mol Genet Metab. 2005 Sep-Oct;86(1-2):34-43. doi: 10.1016/j.ymgme.2005.07.020. Epub 2005 Sep 22.
- Dobson CM, Wai T, Leclerc D, Kadir H, Narang M, Lerner-Ellis JP, Hudson TJ, Rosenblatt DS, Gravel RA. Identification of the gene responsible for the cblB complementation group of vitamin B12-dependent methylmalonic aciduria. Hum Mol Genet. 2002 Dec 15;11(26):3361-9. doi: 10.1093/hmg/11.26.3361.
- Horster F, Baumgartner MR, Viardot C, Suormala T, Burgard P, Fowler B, Hoffmann GF, Garbade SF, Kolker S, Baumgartner ER. Long-term outcome in methylmalonic acidurias is influenced by the underlying defect (mut0, mut-, cblA, cblB). Pediatr Res. 2007 Aug;62(2):225-30. doi: 10.1203/PDR.0b013e3180a0325f.
- Leal NA, Olteanu H, Banerjee R, Bobik TA. Human ATP:Cob(I)alamin adenosyltransferase and its interaction with methionine synthase reductase. J Biol Chem. 2004 Nov 12;279(46):47536-42. doi: 10.1074/jbc.M405449200. Epub 2004 Aug 30.
- Leal NA, Park SD, Kima PE, Bobik TA. Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant. J Biol Chem. 2003 Mar 14;278(11):9227-34. doi: 10.1074/jbc.M212739200. Epub 2003 Jan 3.
- Lerner-Ellis JP, Gradinger AB, Watkins D, Tirone JC, Villeneuve A, Dobson CM, Montpetit A, Lepage P, Gravel RA, Rosenblatt DS. Mutation and biochemical analysis of patients belonging to the cblB complementation class of vitamin B12-dependent methylmalonic aciduria. Mol Genet Metab. 2006 Mar;87(3):219-25. doi: 10.1016/j.ymgme.2005.11.011. Epub 2006 Jan 10.
- Manoli I, Sloan JL, Venditti CP. Isolated Methylmalonic Acidemia. 2005 Aug 16 [updated 2022 Sep 8]. In: Adam MP, Bick S, Mirzaa GM, Wallace SE, Amemiya A, editors. GeneReviews(R) [Internet]. Seattle (WA): University of Washington, Seattle; 1993-2026. Available from http://www.ncbi.nlm.nih.gov/books/NBK1231/
- Zhang J, Dobson CM, Wu X, Lerner-Ellis J, Rosenblatt DS, Gravel RA. Impact of cblB mutations on the function of ATP:cob(I)alamin adenosyltransferase in disorders of vitamin B12 metabolism. Mol Genet Metab. 2006 Apr;87(4):315-22. doi: 10.1016/j.ymgme.2005.12.003. Epub 2006 Jan 24.
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