EC Number   |
Protein Variants |
Reference |
|---|
    1.5.1.10 | C154S |
site-directed mutagenesis |
741780 |
| 1.5.1.10 | C154S/Y99F |
site-directed mutagenesis |
741780 |
| 1.5.1.10 | D126A |
site-directed mutagenesis |
741780 |
| 1.5.1.10 | D126A/C154S |
site-directed mutagenesis |
741780 |
| 1.5.1.10 | D126A/Y99F |
site-directed mutagenesis |
741780 |
| 1.5.1.10 | more |
construction of 3 Spe3-Lys9 mutants, with defects in the spe3-part, the lys9-part, or both, which are auxotrophic for lysine and spermidine, spermidine, and lysine, respectively, transcription levels and phenotype overview, the polyamine auxotrophy due to defect spe3 cannot be overcome by spermine addition, while the mutan with lys 9 defect grows slowly at 30°C with lysine addition, but dies upon lysine starvation, the mutant with defects in both gene parts is avirulent and lethal |
658579 |
| 1.5.1.10 | more |
construction of an enzyme-deficient mutant strain: disruption and inactivation of gene lys7 by double-recombination method leads to lysine auxotrophy and accumulation of piperideine-6-carboxylic acid, and with L-lysine as sole N-source and supplementation of DL-alpha-aminoadipic acid, also of pipecolic acid, transformation of the mutant strain with lys7 can restore enzyme activity |
657593 |
| 1.5.1.10 | more |
kinetic parameters of the mutants in the reaction direction of glutamate formation exhibit modest decreases. The pH-rate profiles obtained with all mutant enzymes decrease at low and high pH, suggesting acid and base catalytic groups are still present in all enzymes. Solvent kinetic deuterium isotope effects are all larger than those observed for wild-type enzyme |
741780 |
| 1.5.1.10 | Y99F |
site-directed mutagenesis |
741780 |
