Methylmalonic aciduria type A protein, mitochondrial

Definition:

GTPase, binds and hydrolyzes GTP. Involved in intracellular vitamin B12 metabolism, mediates the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis. Functions as a G-protein chaperone that assists AdoCbl cofactor delivery from MMAB to the methylmalonyl-CoA mutase (MMUT). Plays a dual role as both a protectase and a reactivase for MMUT. Protects MMUT from progressive inactivation by oxidation by decreasing the rate of the formation of the oxidized inactive cofactor hydroxocobalamin (OH2Cbl). Additionally acts a reactivase by promoting the replacement of OH2Cbl by the active cofactor AdoCbl, restoring the activity of MMUT in the presence and hydrolysis of GTP.

References:

[1]. Tóshiko Takahashi-Íñiguez, et al. Protection and reactivation of human methylmalonyl-CoA mutase by MMAA protein. Biochem Biophys Res Commun. 2011 Jan 7;404(1):443-7. [Content Brief]

[2]. Tanja Plessl, et al. Protein destabilization and loss of protein-protein interaction are fundamental mechanisms in cblA-type methylmalonic aciduria. Hum Mutat. 2017 Aug;38(8):988-1001. [Content Brief]

[3]. D Sean Froese, et al. Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. J Biol Chem. 2010 Dec 3;285(49):38204-13. [Content Brief]

[4]. Toshiko Takahashi-Iñiguez, et al. Human MMAA induces the release of inactive cofactor and restores methylmalonyl-CoA mutase activity through their complex formation. Biochimie. 2017 Nov;142:191-196. [Content Brief]

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