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
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inborn
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b12-dependent
- propionyl-coa
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adocbl
- homocysteine
- methylcobalamin
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apoenzyme
- shermanii
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adenosylcobalamin-dependent
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5\'-deoxyadenosylcobalamin
- propionibacterium
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hyperammonemia
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homolysis
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adenosylation
- homocystinuria
- mutases
- propionylcarnitine
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adenosyltransferase
- 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
- cyanocobalamin
- mmachc
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cobiialamin
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b12-binding
- hydroxycobalamin
- medicine
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mecbl
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cobalamin-binding
- cinnamonensis
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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
Advanced search results
Engineering
Engineering on EC 5.4.99.2 - methylmalonyl-CoA mutase
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E392A
site-directed mutagenesis, kcat is reduced 12fold compared to the wild-type enzyme. The mutant shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
E392D
site-directed mutagenesis, kcat is reduced 330fold compared to the wild-type enzyme. The mutant shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
E392Q
site-directed mutagenesis, kcat is reduced 16fold compared to the wild-type enzyme. The mutant shows no detectable adenosylcobalamin homolysis upon binding of the physiological substrate
G623R
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six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein
G717V
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six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein
G94V
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six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein
H678R
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six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein
L692P
naturally occuring mutation, from patient with methylmalonic acidemia (MMA)
R108H
naturally occuring mutation, from patient with methylmalonic acidemia (MMA)
R228Q
naturally occuring mutation, from patient with methylmalonic acidemia (MMA)
R369H
Y231N
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six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein
H224Q
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lower turnover than wild-type enzyme
H244A
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lower turnover than wild-type enzyme
H610A
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weakened affinity to the cofactor and much lower turnover than wild-type enzyme
H610N
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weakened affinity to the cofactor and much lower turnover than wild-type enzyme
R207Q
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active site residue, mutation lowering kcat 10000-fold and increasing KM for methylmalonyl-CoA over 30fold
R207Q/Y86F
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double mutant designed to mimic active site of isobutyryl-CoA mutase
Y243A
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40000fold decrease in catalytic efficiency, twofold decrease of cob(II)alamin concentration under steady state turnover conditions, no loss of stereochemical preference for substrate
Y89F
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active site residue, mutation lowering kcat and increasing KM for methylmalonyl-CoA
additional information
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six missense mutations, producing the amino acid changes G94V, Y231N, R369H, G623R, H678R and G717V are detected in L-methylmalonyl-CoA mutase cDNA of patients suffering from the mut-form of methylmalonic acidemia resulting from defective adenosylcobalamin binding. The mutations increase the Km for adenosylcobalamin by 40fold to 900fold, while the values for maximal velocity varies from 0.2% to nearly 100% of that of the wild-type protein
R369H
naturally occuring mutation, from patient with methylmalonic acidemia (MMA)
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enzyme depletion by RNA interference results in accumulation of methylmalonic acid. Enzyme deletion mutants display reduced propionate incorporation into macromolecules and produce increased amounts of methylmalonic acid in the culture medium. Lentiviral delivery of gene into fibroblasts derived from a patient with mut0 class methylmalonic acidemia can partially restore propionate flux
additional information
neither a species barrier to mitochondrial processing nor an apparent immune response to MUT limits the murine model as an experimental platform to test the efficacy of human gene therapy vectors for methylmalonic acidemia
additional information
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neither a species barrier to mitochondrial processing nor an apparent immune response to MUT limits the murine model as an experimental platform to test the efficacy of human gene therapy vectors for methylmalonic acidemia
additional information
O74009; O58013
generation of N-terminal deletion mutant PH1306DELTAN
additional information
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generation of N-terminal deletion mutant PH1306DELTAN
additional information
Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
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generation of N-terminal deletion mutant PH1306DELTAN
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