EC Number   |
Protein Variants |
Reference |
|---|
    3.5.1.18 | E134A |
Glu134 replaced by alanine |
669532 |
| 3.5.1.18 | E134D |
Glu134 replaced by aspartate |
669532 |
| 3.5.1.18 | E134D |
the free energy of substrate binding in the mutant enzyme is compared with the substrate binding free energy in the wild-type enzyme. In the case of E134D mutation, the shorter side chain length of the Asp residue at the 134 position (compared to Glu134 in the wild-type enzyme) makes the negatively charged carboxylate group of the Asp134 residue more distant from the negatively charged substrate, N-succinyl-LL-2,6-diaminoheptanedioate. In addition, the metal centers contribute more favorably toward the substrate binding in the E134D mutant as compared to that in wild-type enzyme, which indicates a stronger substrate binding with the metal centers in the mutant. The increased metal-substrate binding in the E134D mutant is a result of the shorter side chain of Asp134, which allows the negatively charged N-succinyl-LL-2,6-diaminoheptanedioate to come closer to the metal centers in E134D as compared to that in wild-type enzyme |
-, 754476 |
| 3.5.1.18 | H349A |
site-directed mutagenesis, inactive mutant |
712506 |
| 3.5.1.18 | H349A |
the free energy of substrate binding in the mutant enzyme is compared with the substrate binding free energy in the wild-type enzyme. Compared to wild-type enzyme, a relatively weaker substrate binding is observed in the histidine mutant Compared to wild-type enzyme, a relatively weaker substrate binding is observed in the histidine mutant. The computed values of the free energy of substrate binding in this study suggest no substrate binding in the H349A mutant |
-, 754476 |
| 3.5.1.18 | H67A |
site-directed mutagenesis, the mutant shows 180fold decreased activity compred to the wild-type enzyme. Approximately 70% of the maximal catalytic activity is recovered after the addition of 1 equiv of Zn2+ |
712506 |
| 3.5.1.18 | H67A |
the free energy of substrate binding in the mutant enzyme is compared with the substrate binding free energy in the wild-type enzyme. Compared to wild-type enzyme, a relatively weaker substrate binding is observed in the histidine mutant. The computed values of the free energy of substrate binding in this study suggest a less favorable substrate binding in the H67A mutant compared to wild-type enzyme |
-, 754476 |
| 3.5.1.18 | H67A/H349A |
the proton transfer process is not possible in the mutant, the catalytic activities are effectively quenched (as determined by relaxed potential energy scan) |
-, 754476 |
| 3.5.1.18 | more |
construction of dimerization domain deletion mutants, that all show no activity |
735140 |
| 3.5.1.18 | T325A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme |
735140 |
