EC Number |
General Information |
Reference |
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5.4.99.2 | evolution |
the two genes PH1306 and PH0275, which encode the subunits of methylmalonyl-CoA mutase in Pyrococcus horikoshii have deduced amino acid sequences that share high homology with the N- and C-terminal regions of human MCM (UniProt ID P22033), respectively. The AdoCbl-binding domain contains a signature DXHXXG motif that is conserved in PH0275. Furthermore, Tyr110, Arg228, and His265 of human MCM are involved in catalysis, and the corresponded amino acid residues are conserved in gene PH1306 |
-, 747314 |
5.4.99.2 | malfunction |
metabolic disorder methylmalonic aciduria can be caused by nonsense mutations within the methylmalonyl-CoA mutase gene, resulting in the production of a truncated protein with little or no catalytic activity |
726874 |
5.4.99.2 | malfunction |
methylmalonic acidemia (MMA) is an inherited metabolic disease that is caused by either low MCM activity or deficiency of adenosylcobalamin owing to altered vitamin B12 metabolism |
746727 |
5.4.99.2 | metabolism |
inhibitor cyanocobalamin dodecylamine, a ribose 5'-carbamate derivative of cofactor cyanocobalamin, is absorbed and accumulated to significant levels by Caenorhabditis elegans and is not further metabolized. The dodecylamine derivative does not affect the levels of mRNAs encoding enzymes or proteins involved in intercellular cobalamin metabolism, including methylmalonyl-CoA mutase (mmcm-1), methylmalonic acidemia cobalamin A complementation group (mmaa-1), methylmalonic aciduria cblC type (cblc-1), and methionine synthase reductase (mtrr-1). In contrast, the level of the mRNAs encoding cob(I)alamin adenosyltransferase (mmab-1) is increased significantly and identical to that of cobalamin-deficient Caenorhabditis elegans. The cyanocobalamindodecylamine inhibitor of cobalamin-dependent enzymes induces severe cobalamin deficiency in Caenorhabditis elegans. Cobalamin deficiency decreases the egg-laying rates and prolongs the life cycle of the worms, phenotype overview |
-, 747783 |
5.4.99.2 | more |
optimization and validation of a reversed-phase high performance liquid chromatography method to evalidate MCM activity in bovine liver, conditions to optimize reproducibility of the method and to determine stability of the enzyme and its product during storage and processing of samples, overview |
727246 |
5.4.99.2 | physiological function |
human mitochondrial methylmalonyl-CoA mutase (hMCM) is an isomerase that converts methylmalonyl-CoA to succinyl-CoA, a crucial step for the incorporation of some compounds derived from the diet into the central metabolism. hMCM employs highly reactive radicals from its cofactor (adenosylcobalamin, AdoCbl) to perform its reaction. hMCM loses activity during catalysis, but the interaction with human MMAA (hMMAA), a GTPase protein, avoids this loss or restores hMCM activity. Formation and accumulation of OH2Cbl, the oxidized form of cofactor AdoCbl formed during catalysis, is the cause of hMCM inactivation. The complex formation of hMCM/hMMAA decreases the rate of oxidized cofactor formation, protecting the hMCM enzyme. hMMAA is able to remove the damaged cofactor through GTP hydrolysis.a modification in the kinetic parameters of hMCM in presence of hMMAA is observed |
747209 |
5.4.99.2 | physiological function |
methylmalonyl coenzyme A (CoA) is a catabolite of valine, isoleucine, methionine, threonine, odd-chain fatty acids, and cholesterol, and is converted to succinyl-CoA by enzymatic reaction of methylmalonyl-CoA mutase (MCM) with its coenzyme vitamin B12 |
746727 |
5.4.99.2 | physiological function |
methylmalonyl-CoA mutase (MUT) expression influences the risk of acquiring Mycobacterium bovis infection and developing bovine tuberculosis. Genetically-defined higher host MUT expression levels result in lower serum cholesterol concentration and tissue deposits that increase the protective immune response to Mycobacterium bovis, thus resulting in resistance to bovine tuberculosis and better response to Mycobacterium bovis bacilli Calmette-Guerin vaccination |
716097 |
5.4.99.2 | physiological function |
methylmalonyl-CoA mutase catalyzes the reversible interconversion of (2R)-methylmalonyl-CoA and succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle. The enzyme requires 5'-deoxyadenosylcobalamin (5'-deoxyadenosyl vitamin B12 or AdoCbl) as a cofactor and is widely distributed in a variety of organisms from bacteria to humans |
-, 747314 |
5.4.99.2 | physiological function |
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway |
-, 726729 |