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5.4.99.2: methylmalonyl-CoA mutase

This is an abbreviated version!
For detailed information about methylmalonyl-CoA mutase, go to the full flat file.

Word Map on EC 5.4.99.2

Reaction

(R)-methylmalonyl-CoA
=
succinyl-CoA

Synonyms

(R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase, (S)-Methylmalonyl-CoA mutase, cobalamin-dependent methylmalonyl-CoA mutase, hMCM, L-methylmalonyl-co-enzyme-A mutase, L-methylmalonyl-CoA mutase, MCB-beta, MCM, MCM-alpha, MCM-beta, mcmB, Methylmalonyl CoA mutase, Methylmalonyl coenzyme A carbonylmutase, Methylmalonyl coenzyme A mutase, methylmalonyl-CoA mutase, Methylmalonyl-CoA-carbonyl mutase, mitochondrial methylmalonyl-CoA mutase, mmcm-1, Msed_0638, Msed_2055, MuT, Mutase, methylmalonyl coenzyme A, Sbm, sleeping beauty mutase

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.2 methylmalonyl-CoA mutase

Activating Compound

Activating Compound on EC 5.4.99.2 - methylmalonyl-CoA mutase

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Cobeta-5'-Deoxyadenosine-5'-yl)-(p-cresolyl)cobamide
-
can serve as coenzyme, Km: 0.000064
adenosylcobalamin
-
required
hMMAA
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. No activity is recovered in the presence of hMMAAwith GMPPNP, confirming the need of GTP hydrolysis for this cofactor removal. In vivo localization of hMMAA and its colocalization with hMCM in human fibroblasts mitochondria. hMMAAis localized in both the cytoplasm and mitochondria but in less abundance and distribution than enzyme hMCM
-
hydroxocobalamin
-
supplementation of hydroxocobalamin results in a marked increase in the holo-MCM activity in a dose-dependent manner, although the holo-MCM activity does not exceed 30% of the total-MCM activity even if hydroxocobalamin is supplemented at 10 mM
methylmalonic acidemia protein
-
after 60 min of reaction, when MCM is inactive, the addition of methylmalonic acidemia protein increases the enzymatic activity through GTP hydrolysis, indicating reactivation of MCM by exchange of the damaged cofactor. Methylmalonic acidemia protein acts as a chaperone of human MCM
-