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
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5.4.99.2
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methylmalonic
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acidemia
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acidurias
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adenosylcobalamin
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propionate
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succinyl-coa
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inborn
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b12-dependent
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propionyl-coa
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adocbl
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homocysteine
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methylcobalamin
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apoenzyme
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shermanii
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adenosylcobalamin-dependent
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5\'-deoxyadenosylcobalamin
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propionibacterium
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hyperammonemia
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homolysis
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adenosylation
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homocystinuria
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mutases
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propionylcarnitine
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adenosyltransferase
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mmaa
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transcobalamins
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methylmalonyl-coenzyme
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propionyl
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adocbl-dependent
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odd-chain
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megaloblastic
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cobalt-carbon
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cyanocobalamin
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mmachc
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cobiialamin
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b12-binding
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hydroxycobalamin
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medicine
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mecbl
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cobalamin-binding
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cinnamonensis
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5\'-deoxyadenosyl
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isobutyryl-coa
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analysis
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extorquens
- 5.4.99.2
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methylmalonic
- acidemia
- acidurias
- adenosylcobalamin
- propionate
- succinyl-coa
-
inborn
-
b12-dependent
- propionyl-coa
-
adocbl
- homocysteine
- methylcobalamin
-
apoenzyme
- shermanii
-
adenosylcobalamin-dependent
-
5\'-deoxyadenosylcobalamin
- propionibacterium
-
hyperammonemia
-
homolysis
-
adenosylation
- homocystinuria
- mutases
- propionylcarnitine
-
adenosyltransferase
- mmaa
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transcobalamins
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methylmalonyl-coenzyme
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propionyl
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adocbl-dependent
-
odd-chain
-
megaloblastic
-
cobalt-carbon
- cyanocobalamin
- mmachc
-
cobiialamin
-
b12-binding
- hydroxycobalamin
- medicine
-
mecbl
-
cobalamin-binding
- cinnamonensis
-
5\'-deoxyadenosyl
- isobutyryl-coa
- analysis
- extorquens
Reaction
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
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Cofactor
Cofactor on EC 5.4.99.2 - methylmalonyl-CoA mutase
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Coalpha(alpha-Benzimidazolyl)-Cobeta-adenosyl-cobamide
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can serve as coenzyme
Coalpha-(alpha-Purinyl)-Cobeta-adenosylcobamide
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can serve as coenzyme
Coalpha-Hydroxo-Cobeta-adenosylcobinamide
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can serve as coenzyme
Coalpha[alpha-(Aden-7-yl)]-Cobeta-adenosyl-cobamide
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can serve as coenzyme
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P-loop GTPase MeaB increases affinity of the mutase for cofactor twofold, in presence of MeaB and GDP, affinity decreases fivifold
5'-deoxyadenosylcobalamin
the apoenzyme is converted to a holoenzyme by incubation for 4 h at 4°C with 0.01 mM 5'-deoxyadenosylcobalamin, the purified enzyme contains one mole of prosthetic 5'-deoxyadenosylcobalamin per mole of subunit
5'-deoxyadenosylcobalamin
O74009; O58013
the 5'-deoxyadenosyl vitamin B12 orAdoCbl, methylmalonyl-CoA mutase (MCM) requires 5'-deoxyadenosylcobalamin as a cofactor
adenosylcobalamin
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adenosylcobalamin
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dependent on adenosylcobalamin as prosthetic group, under cobalamin-deficient conditions, (R)-2-methylmalonyl-CoA and its precursor, propionyl-CoA, increase as a result of a decrease in the catalytic activity of MCM due to deficiency of adenosylcobalamin
adenosylcobalamin
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dependent on adenosylcobalamin which is delivered by adenosyltransferase
adenosylcobalamin
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MCM activity with adenosylcobalamin increases linearly during the first 3-4 min
adenosylcobalamin
binding analysis with recombinant wild-type and mutant enzymes, overview
adenosylcobalamin
AdoCbl, the enzyme converts methylmalonyl-CoA to succinyl-CoA employing highly reactive radicals from its cofactor adenosylcobalamin to perform its reaction. Formation and accumulation of OH2Cbl, the oxidized form of the AdoCbl cofactor formed during catalysis, is the cause of hMCM inactivation. GTPase hMMAA is able to remove the damaged cofactor through GTP hydrolysis
Cobalamin
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dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
Cobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
cobamide
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dependent on
cobamide
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adenosylcobalamin protects the apoenzyme from inactivation by NEM or iodoacetamide. Km: 0.000021 mM
cobamide
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enzyme-bound and free 5'-deoxyadenonosylcobalamin molecules are frequently exchanged during incubation, deuterium is transferred from the 5' position of 5'-deoxyadenonosylcobalamin to the solvent, deuterium scrambling between the two diastereotopic 5'-positions occurrs