EC Number   |
Protein Variants |
Reference |
|---|
    4.1.3.17 | E199A |
site-directed mutagenesis, the mutant shows reduced activity and reduced affinity for Co2+ compared to the wild-type enzyme |
727049 |
| 4.1.3.17 | 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 |
749095 |
| 4.1.3.17 | 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 |
749095 |
| 4.1.3.17 | 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 |
749095 |
| 4.1.3.17 | 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 |
749095 |
| 4.1.3.17 | R123A |
no activity |
715556 |
| 4.1.3.17 | R123K |
retains some activity |
715556 |
| 4.1.3.17 | 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 |
749095 |
| 4.1.3.17 | 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 |
749095 |
| 4.1.3.17 | 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 |
749095 |
