4.1.3.17: 4-hydroxy-4-methyl-2-oxoglutarate aldolase
This is an abbreviated version!
For detailed information about 4-hydroxy-4-methyl-2-oxoglutarate aldolase, go to the full flat file.
Word Map on EC 4.1.3.17
Reaction
Synonyms
4-hydroxy-4-methyl-2-ketoglutarate aldolase, 4-hydroxy-4-methyl-2-oxoglutarate aldolase, 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, aldolase, 4-hydroxy-4-methyl-2-oxoglutarate, gamma-methyl-gamma-hydroxy-alpha-ketoglutaric aldolase, HMG aldolase, HMG/CHA aldolase, KDPG aldolase, MHK aldolase, MHKG aldolase, pyruvate aldolase
ECTree
4.1.3.17 4-hydroxy-4-methyl-2-oxoglutarate aldolaseAdvanced search results
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results (Engineering
Engineering on EC 4.1.3.17 - 4-hydroxy-4-methyl-2-oxoglutarate aldolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E199A
-
site-directed mutagenesis, the mutant shows reduced activity and reduced affinity for Co2+ compared to the wild-type enzyme
G144V
the variant has a 10fold increase in KM and a 73fold decrease in kcat for the 4-hydroxy-4-methyl-2-oxoglutarate cleavage reaction and the kcat increases 2-fold in the presence of phosphate
H75A
the variant has a 2fold increase in KM and a 1.4fold increase in kcat for the 4-hydroxy-4-methyl-2-oxoglutarate catalyzed reaction and does not have a significant effect on the pyruvate methyl proton exchange rate compared to the wild type enzyme
K147A
the mutation has significant effects on the steady state kinetics of the aldolase 4-hydroxy-4-methyl-2-oxoglutarate reaction with decreasing the kcat by 1114fold compared to the wild type enzyme
N71A
the mutation has significant effects on the steady state kinetics of the aldolase 4-hydroxy-4-methyl-2-oxoglutarate reaction with decreasing the kcat by 1114fold compared to the wild type enzyme
R123K
R195A
the substitution moderately effects the 4-hydroxy-4-methyl-2-oxoglutarate cleavage reaction with a 7fold increase in KM and a 2fold decrease in kcat. The activation of kcat and the pyruvate methyl proton exchange rate by Pi is each reduced by 5fold
R40A
the variant has a 2fold decrease in kcat and is still activated to a similar extent as the wild type enzyme in the 4-hydroxy-4-methyl-2-oxoglutarate aldolase cleavage reaction
T145A
the variant is activated in the presence of phosphate resulting in a 12fold increase in kcat for the 4-hydroxy-4-methyl-2-oxoglutarate catalyzed reaction and a 24fold increase in the pyruvate methyl proton exchange rate compared to the wild type enzyme
R123K
the mutation reduces the kcat of the 4-hydroxy-4-methyl-2-oxoglutarate catalyzed reaction by 181fold and reduces the pyruvate methyl proton exchange rate by 20fold compared to the wild type enzyme
