EC Number   |
Protein Variants |
Reference |
|---|
    5.1.1.18 | C113S |
site-directed mutagenesis, the C113S mutant exhibits a KM for L-serine which is 3.5fold higher than for the wild-type enzyme and a 3.3fold lower specific activity. ATP binding to the mutant in the presence of L-serine occurs with a 5fold higher EC50 compared to wild-type, with conserved binding cooperativity. Phenotype, overview |
747202 |
| 5.1.1.18 | C113S |
site-directed mutagenesis, the mutant is resistant to regulation by nitrosylation by NO |
682561 |
| 5.1.1.18 | C2D/C6D |
site-directed mutagenesis |
704657 |
| 5.1.1.18 | D213A |
site-directed mutagenesis, the mutation abolishes the enzyme activation by Mg2+ and Na+ |
726663 |
| 5.1.1.18 | D318N |
site-directed mutagenesis |
747202 |
| 5.1.1.18 | E207A |
site-directed mutagenesis, the mutation abolishes the enzyme activation by Mg2+ and Na+ |
726663 |
| 5.1.1.18 | E219A/D225A |
neither the serine racemase nor the dehydratase activities of the E219A/D225A serine racemase mutant are affected by the addition of Mg2+. The kcat/Km values of the mutant decrease to 16% (for L-Ser) and 23% (for D-Ser) of those of the wild type protein in the racemase reaction and to 36% (for L-Ser) and 26% (for D-Ser) in the dehydratase reaction |
714697 |
| 5.1.1.18 | H150S |
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme |
746724 |
| 5.1.1.18 | H150S/N152S |
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme |
746724 |
| 5.1.1.18 | H150S/P151S |
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme |
746724 |
