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
-
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
-
transcobalamins
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methylmalonyl-coenzyme
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propionyl
-
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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Inhibitors
Inhibitors on EC 5.4.99.2 - methylmalonyl-CoA mutase
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2-(N,N-diethylamino)-diazenolate-2-oxide
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1 mM, about 50% inhibition of enzyme activity. Similar inhibitory effects of 2-(N,N-diethylamino)-diazenolate-2-oxide in the presence of 25 mM glutathione and dithiothreitol
allylmalonyl-CoA
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competitive with wild-type, O2-independent suicide inactivation with mutant Y243A via an internal electron transfer from cob(II)alamin to the inhibitor radical
cyanocobalamin dodecylamine
CN-Cbl dodecylamine, a ribose 5'-carbamate derivative of 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 derivative acts as a potent inhibitor of cobalamin-dependent enzymes and induces severe cobalamin deficiency in Caenorhabditis elegans. The CN-Cbl dodecylamine derivative competitively inhibits the apoenzyme. CN-Cbl dodecylamine has increased affinity for the apoenzyme relative to that of cofactor adenosylcobalamin (AdoCbl). CN-Cbl does not reduce the apo-MCM activity in the presence of AdoCbl
ethylmalonyl-CoA
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competitive with wild-type, O2-dependent suicide inactivation with mutant Y243A
Hg2+
MCM activity is inhibited completely by the addition of 3 mM Hg2+
isobutyryl-CoA
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R207Q and Y89F/R207Q mutants show conversion of adenosylcobalamin to hydroxycobalamin, indicating inactivation of the enzyme
n-butyryl-CoA
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R207Q and Y89F/R207Q mutants show conversion of adenosylcobalamin to hydroxycobalamin, indicating inactivation of the enzyme. No changes in wild-type and Y89F-mutant
Na+, K+, Ca2+, Fe2+, Mg2+, and Co2+ (all at 3 mM) and 3 mM EDTA do not cause inhibition of the MCM activity
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