EC Number   |
Protein Variants |
Reference |
|---|
    1.4.1.16 | T70S |
catalytic ability of T70S does not change much |
763313 |
| 1.4.1.16 | Q154L/D158G/T173I/R199M/H249N |
construction of a thermostable, NADP+-dependent D-amino acid dehydrogenase (DAADH) from the meso-diaminopimelate dehydrogenase of strain A1 by introducing five point mutations into amino acid residues located in the active site. In the presence of NADP+, the mutant enzyme catalyzes the oxidative deamination of several D-amino acids, including D-cyclohexylalanine, D-isoleucine, and D-2-aminooctanoate, but not of meso-diaminopimelate. The corresponding 2-oxo acids are aminated in the presence of NADPH and ammonia in the reverse reaction, mutant substrate specificity, overview. The mutant enzyme is also more thermostable than its parental meso-diaminopimelate dehydrogenase |
-, 724643 |
| 1.4.1.16 | R71S |
for pyruvic acid, R71S shows few changes in kcat/Km values |
762982 |
| 1.4.1.16 | R71E |
for reductive amination, the mutant shows a 1.5fold increase in Km and 0.24fold decrease in kcat. For oxidative deamination, a 50% decrease in the kcat/Km value is observed |
762982 |
| 1.4.1.16 | more |
in order to enlarge the substrate binding pocket of the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum to accommodate larger 2-keto acids, e.g. phenylalanine, four amino acid residues, Phe146, Thr171, Arg181, and His227, are targeted for site saturation mutagenesis |
724034 |
| 1.4.1.16 | M152D |
inactive |
742276 |
| 1.4.1.16 | M152E |
inactive |
742276 |
| 1.4.1.16 | M152W |
inactive |
742276 |
| 1.4.1.16 | H227I |
mutant accepts substrates D-2-phenylglycine and D-homophenylalanine |
762879 |
| 1.4.1.16 | T171H |
mutant accepts substrates D-2-phenylglycine and D-homophenylalanine |
762879 |
