EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.3 | L200F |
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 degree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions |
-, 741465 |
| 1.1.1.3 | L200F/D215A |
site-directed mutagenesis |
-, 741465 |
| 1.1.1.3 | L200F/D215E |
site-directed mutagenesis |
-, 741465 |
| 1.1.1.3 | L200F/D215G |
site-directed mutagenesis |
-, 741465 |
| 1.1.1.3 | L200F/D215K |
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 dgree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions |
-, 741465 |
| 1.1.1.3 | more |
construction of a hom disruption mutant by insertional inactivation via double crossover leading to up to 4.3fold and 2fold increases in intracellular free L-lysine concentration and specific cephamycin C production, respectively, during stationary phase in chemically defined medium, overview |
-, 688167 |
| 1.1.1.3 | more |
construction of a hybrid enzyme AKIII-HDHI+ by fusing a wild-type monofunctional aspartate kinase AKIII enzyme to the thrA2+ gene, encoding the homoserine dehydrogenase including the interface region of the wild-type bifunctional enzyme, the hybrid enzyme shows highly improved kinetic properties for homoserine dehydrogenase activity, and is not sensitive to L-threonine inhibition |
654640 |
| 1.1.1.3 | more |
construction of transgenic Arabidopsis thaliana plants by transformation with gene akthr2 via Agrobacterium tumefaciens infection, determination of expression patterns of the gene akthr1 ans akthr2 in the transgenic plants |
657018 |
| 1.1.1.3 | more |
design of an artificial allosteric enzyme to sense an unnatural signal for a precise and dynamical control of fluxes of growth-essential but byproduct pathways in metabolic engineering of industrial microorganisms. The natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine |
739779 |
| 1.1.1.3 | more |
engineering of a Corynebacterium glutamicum strain HL1049 for effective production of methionine by elimination of the threonine synthesis gene and desensitizing the homoserine dehydrogenase versus inhibition by threonine, analysis of the amino acid spectrum of the engineered strain, overview |
688822 |
