EC Number |
Protein Variants |
Reference |
---|
1.1.1.95 | A143A |
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme |
667649 |
1.1.1.95 | A144V |
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme |
667649 |
1.1.1.95 | A373T |
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive |
698189 |
1.1.1.95 | A374V |
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme |
667649 |
1.1.1.95 | D317A |
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme |
667649 |
1.1.1.95 | D386A |
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme |
667649 |
1.1.1.95 | D463A |
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine |
-, 696285 |
1.1.1.95 | E108A |
in contrast to wild-type mutant existed as monomer even at pH 7 |
725917 |
1.1.1.95 | E299A |
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme |
667649 |
1.1.1.95 | E302A |
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme |
667649 |