EC Number   |
Protein Variants |
Reference |
|---|
    1.2.1.3 | A505P |
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residue is important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type |
744371 |
| 1.2.1.3 | A505P/Q506K |
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residues are important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type. Structure analysis of the protomer of ALDH7A1 with the mutated residues Ala505 and Gln506, PDB ID 4ZUL |
744371 |
| 1.2.1.3 | ALDH-H3tail |
aldehyde dehydrogenase class 1 with the addition of the C-terminal tail of class 3, KM-value for propionaldehyde is 2.6fold higher than the KM-value of the wild-type enzyme, KM-value for NAD+ is 2fold higher than the KM-value of the wild-type enzyme |
654655 |
| 1.2.1.3 | ALDH1-5AA |
aldehyde dehydrogenase class 1 with the addition of five amino acids at the C-terminus, KM-value for propionaldehyde is 67% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 73% of the KM-value of the wild-type enzyme |
654655 |
| 1.2.1.3 | C247S |
the mutant shows slightly reduced activity compared to the wild type enzyme |
724222 |
| 1.2.1.3 | C253S |
the mutation abolishes enzymatic activity |
724222 |
| 1.2.1.3 | C274A |
the mutation leads to a drastic loss of the activity |
-, 722210 |
| 1.2.1.3 | C274S |
the mutation leads to a drastic loss of the activity |
-, 722210 |
| 1.2.1.3 | C289D |
enzyme activity is nearly abolished in this mutant |
724399 |
| 1.2.1.3 | C289P |
enzyme activity is nearly abolished in this mutant |
724399 |
