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Literature summary for 5.4.99.2 extracted from

  • Froese, D.S.; Kochan, G.; Muniz, J.R.; Wu, X.; Gileadi, C.; Ugochukwu, E.; Krysztofinska, E.; Gravel, R.A.; Oppermann, U.; Yue, W.W.
    Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation (2010), J. Biol. Chem., 285, 38204-38213.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)R3-Rosetta cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in the apo, holo, and substrate-bound ternary forms, sitting drop vapor diffusion method, using 1.6 M Na/K-phosphate, 0.1 M HEPES pH 7.5 (apo form), or 30% (w/v) PEG3350, 0.1 M Bis-Tris pH 5.5, 0.3 M (NH4)2SO4 (holo form), or 20% (w/v) PEG3350, 0.1 M Bis-Tris pH 5.5, 0.1 M (NH4)2SO4 (ternary form) Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P22033
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-methylmalonyl-CoA
-
Homo sapiens succinyl-CoA
-
?
additional information human MMAA and MUT interact in vitro and in vivo. This interaction is nucleotide-selective for MMAA and apoenzyme-dependent for MUT and is associated with stimulation of MMAA GTPase activity by MUT Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Homo sapiens

Synonyms

Synonyms Comment Organism
MCM
-
Homo sapiens
MuT
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin
-
Homo sapiens
Cobalamin essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin Homo sapiens