EC Number |
Protein Variants |
Reference |
---|
1.4.1.16 | A69R |
mutation to the correspondung residue of Symbiobacteium thermophilum DAPDH. Mutation improves the catalytic efficiencies toward 2-keto acids and does not affect the catalytic efficiency toward meso-DAP |
-, 762982 |
1.4.1.16 | F146W |
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates |
724026 |
1.4.1.16 | F146W/M152Q |
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates |
724026 |
1.4.1.16 | H227C |
site-directed saturation mutagenesis, the mutant shows 15.1fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
1.4.1.16 | H227I |
mutant accepts substrates D-2-phenylglycine and D-homophenylalanine |
762879 |
1.4.1.16 | H227V |
mutant shows high activity toward phenylpyruvic acid and 2-oxo-4-phenylbutyric acid |
762879 |
1.4.1.16 | H227V |
site-directed saturation mutagenesis, the mutant shows 35.1fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
1.4.1.16 | K159R |
mutation decreases the kcat/KM value with meso-DAP, the catalytic efficiency toward pyruvic acid increases by 24% |
763313 |
1.4.1.16 | M152A |
the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme |
742276 |
1.4.1.16 | M152D |
inactive |
742276 |