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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

Engineering

Engineering on EC 5.4.99.2 - methylmalonyl-CoA mutase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
-
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
-
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
-
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
-
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
-
lower turnover than wild-type enzyme
H244A
-
lower turnover than wild-type enzyme
H610A
-
weakened affinity to the cofactor and much lower turnover than wild-type enzyme
H610N
-
weakened affinity to the cofactor and much lower turnover than wild-type enzyme
R207Q
-
active site residue, mutation lowering kcat 10000-fold and increasing KM for methylmalonyl-CoA over 30fold
R207Q/Y86F
-
double mutant designed to mimic active site of isobutyryl-CoA mutase
Y243A
-
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
-
active site residue, mutation lowering kcat and increasing KM for methylmalonyl-CoA
additional information