EC Number |
Protein Variants |
Reference |
---|
1.1.1.3 | G378E |
feedback resistance of the enzyme |
246394 |
1.1.1.3 | G378S |
construction of a homoserine dehydrogenase mutant HDG378S, encoded by hom1, in Corynebacterium glutamicum strain IWJ001, one of the best L-isoleucine producing strains. Strain HDG378S is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. Overexpression of lysC1, hom1 and thrB1 increased L-threonine and L-lysine production in Corynebacterium glutamicum ATCC13869 by 96folds and 21.2folds, respectively, overview |
-, 738802 |
1.1.1.3 | G433R |
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield) |
-, 760402 |
1.1.1.3 | H309A |
decrease of catalytic activity and elimination of substrate inhibition |
246402 |
1.1.1.3 | K105A |
site-directed double-primer PCR mutagenesis |
-, 739791 |
1.1.1.3 | K105R |
site-directed double-primer PCR mutagenesis |
-, 739791 |
1.1.1.3 | K195A |
site-directed mutagenesis, inactive mutant. In the crystal structure, the positions of Lys195 and L-Hse are significantly retained with those of the wild-type enzyme, enzyme crystal structure analysis |
761404 |
1.1.1.3 | K205A |
site-directed double-primer PCR mutagenesis |
-, 739791 |
1.1.1.3 | K57Aa |
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme |
-, 741408 |
1.1.1.3 | K99A |
site-directed mutagenesis, inactive mutant. In the crystal structure, the productive geometry of the ternary complex is almost preserved with one new water molecule taking over the hydrogen bonds associated with Lys99, mutant enzyme crystal structure analysis |
761404 |