Methylmalonyl-CoA mutase (MUT aka MCM) (Jansen et al. 1989) utilises adenosylcobalamin (AdoCbl) as a cofactor and catalyses interchange of a carbonyl-CoA group and a hydrogen atom in conversion of methymalonyl-CoA to form succinyl-CoA, a precursor for the citric acid cycle. MUT has a homodimeric structure and is located in the mitochondrial matrix. Defects in MUT cause methylmalonic aciduria type mut (MMAM; MIM:251000), an often fatal disorder of organic acid metabolism (Worgan et al. 2006). Methylmalonic aciduria type A protein (MMAA) (Dobson et al. 2002) is thought to act as a chaperone to MUT and is suggested to play a dual role with regards to MUT protection and reactivation. Defects in MMAA cause methylmalonic aciduria type cblA (MMAA aka methylmalonic aciduria type A or vitamin B12-responsive methylmalonicaciduria of cblA complementation type; MIM:251100). Affected individuals accumulate methylmalonic acid in the blood and urine and are prone to potentially life threatening acidotic crises in infancy or early childhood (Dobson et al. 2002, Lerner-Ellis et al. 2004).
Worgan, LC, Niles, K, Tirone, JC, Hofmann, A, Verner, A, Sammak, A, Kucic, T, Lepage, P, Rosenblatt, DS
Dobson, CM, Wai, T, Leclerc, D, Wilson, A, Wu, X, Doré, C, Hudson, T, Rosenblatt, DS, Gravel, RA
Lerner-Ellis, JP, Dobson, CM, Wai, T, Watkins, D, Tirone, JC, Leclerc, D, Doré, C, Lepage, P, Gravel, RA, Rosenblatt, DS
Jansen, R, Kalousek, F, Fenton, WA, Rosenberg, LE, Ledley, FD
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