EC Number   |
Protein Variants |
Reference |
|---|
    1.4.1.9 | A113G |
mutant enzyme with altered substrate specificity. 17.9fold decrease in turnover number for L-Leu, 1.2fold decrease in turnover-number for L-Ile, 13.8fold increase in turnover number of L-norleucine, 1.7fold decrease in turnover-number for L-norvaline, 3fold decrease in turnover number for alpha-keto-isocaproate, 1.2fold decrease in turnover number for alpha-ketocaproate, 1.3fold increase in turnover number for alpha-ketocaproate, 3.6fold decrease in Km-value for L-Leu, 3.3fold increase in Km-value for L-Ile, 1.1fold decrease in Km-value for L-norleucine, 3.5fold increase in Km-value for L-norvaline, 1.9fold increase in Km-value for alpha-keto-isocaproate, 2.5fold increase in Km-value for alpha-keto-beta-methylvalerate, 2.4fold decrease in Km-value for alpha-ketocaproate, 1.2fold increase in Km-value for NAD+, 1.2fold increase in Km-value for NADH as compared to wild-type enzyme. L-Ethionine and L-Phe are not substrates of the wild-type enzyme but are deaminated by mutant enzyme. Phenylpyruvate is not a substrate of the wild-type enzyme, but is aminated by mutant enzyme |
656569 |
| 1.4.1.9 | A113G/V291L |
mutant enzyme with altered substrate specificity. 67.6fold decrease in turnover number for L-Leu, 20fold decrease in turnover-number for L-Ile, 2.2fold decrease in turnover number of L-norleucine, 44.8fold decrease in turnover-number for L-norvaline, 9.7fold decrease in turnover number for alpha-keto-isocaproate, 7.6fold decrease in turnover number for alpha-ketocaproate, 4.6fold decrease in turnover number for alpha-ketocaproate, 6.9fold increase in Km-value for L-Leu, 13.8fold increase in Km-value for L-Ile, 5.5fold increase in Km-value for L-norleucine, 9fold increase in Km-value for L-norvaline, 34fold increase in Km-value for alpha-keto-isocaproate, 18.2fold increase in Km-value for alpha-keto-beta-methylvalerate, 6fold increase in Km-value for alpha-ketocaproate, 4.4fold increase in Km-value for NAD+, 2fold decrease in Km-value for NADH as compared to wild-type enzyme. L-Ethionine and L-Phe are not substrates of the wild-type enzyme but are deaminated by mutant enzyme. Phenylpyruvate is not a substrate of the wild-type enzyme, but is aminated by mutant enzyme |
656569 |
| 1.4.1.9 | A43V/D124E |
mutant shows improved efficiency of L-tert-leucine synthesis, 5fold increase in catalyic efficiency compared to wild-type |
741718 |
| 1.4.1.9 | A94E |
proportion of residual activity of A94E is 19% of that of wild type after incubation at 70 °C for 10 min |
763402 |
| 1.4.1.9 | D126E |
2fold increase in kcat/Km value for trimethylpyruvate |
762665 |
| 1.4.1.9 | D153 N/H191 N |
25fold improved affinity for NADH and with 50fold enhanced catalytic efficiency |
762918 |
| 1.4.1.9 | D153N |
affinity for NADH is improved, 11.3fold decrease in Km value for NADH |
762918 |
| 1.4.1.9 | D203A |
dual specificity for NAD+ and NADP+ |
349686 |
| 1.4.1.9 | D203A/I204R |
high affinity for NADP+ |
349686 |
| 1.4.1.9 | D203A/I204R/D210R |
high affinity for NADP+ |
349686 |
