EC Number   |
Protein Variants |
Reference |
|---|
    6.3.4.4 | C328D |
the mutant shows reduced Km and increased turnover number for L-aspartate compared to the wild type protein |
727078 |
| 6.3.4.4 | C328D/C368D |
the mutant shows reduced Km and turnover number for L-aspartate compared to the wild type protein |
727078 |
| 6.3.4.4 | C328S |
the mutant exhibits no change in the aspartate Km value but reduced turnover number compared to the wild type protein |
727078 |
| 6.3.4.4 | C328S/C368S |
the mutant shows a 4fold reduced Km for aspartate and reduced turnover number compared to the wild type protein |
727078 |
| 6.3.4.4 | C368S |
the mutant exhibits a 1.7fold increase in the aspartate Km value compared to the wild type protein |
727078 |
| 6.3.4.4 | D13A |
mutant enzyme D13A shows no measurable activity, mutant enzymes E14A and H41N exhibit 1% of the activity of the wild-type enzyme and 2-7fold increases in Km of substrates. The mutant enzyme K16Q has 34% of the activity of wild-type enzyme and Km values for substrates are virtually unchanged from those of the wild-type enzyme |
1559 |
| 6.3.4.4 | D21A |
directed mutagenesis |
651884 |
| 6.3.4.4 | D231A |
wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization |
1566 |
| 6.3.4.4 | D333E |
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme |
1561 |
| 6.3.4.4 | D333N |
mutant enzymes D333N, D333E, and D333Q show decreased turnover numbers and increased Km values for GTP. The three mutants each have higher affinity for XTP and ITP than does the wild-type enzyme |
1561 |
