EC Number   |
Protein Variants |
Reference |
|---|
    2.5.1.65 | F225A |
site-directed mutagenesis, the Km value toward O-phospho-L-serine is not significantly different between the wild-type ApOPSS and the F225A mutant, the kcat value of the wild-type ApOPSS is 4.2fold higher toward O-phospho-L-serine and 15fold higher toward O-acetyl-L-erine than that of the F225A mutant, respectively. The mutation from phenylalanine to alanine at position 225 affects the catalytic activity, not substrate binding |
-, 738193 |
| 2.5.1.65 | K127A |
mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate |
722990 |
| 2.5.1.65 | K204A |
to improve crystallization of CysM alone, a putative surface residue in CysM (Lys204) is mutated to alanine using site-directed mutagenesis |
-, 702213 |
| 2.5.1.65 | more |
construction of truncated variant CysK2NT |
-, 738534 |
| 2.5.1.65 | Q224A |
0.04% of wild-type activity |
722990 |
| 2.5.1.65 | R220A |
700fold lower activity with O-phospho-L-serine as substrate compared to the wild type enzyme |
687773 |
| 2.5.1.65 | R220A |
significant loss in specificity for substrate O-phosphoserine. The purified R220A mutant shows an absorption spectrum identical to wild type CysM with an absorption band at 412 nm reflecting the Schiff base between Lys51 and PLP. Formation of the aminoacrylate intermediate from O-phospho-L-serine in the mutant is severely compromised, with an approximately 700fold slower rate |
-, 687773 |
| 2.5.1.65 | R243A |
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme |
-, 738534 |
| 2.5.1.65 | R297A |
0.3% of wild-type activity |
722990 |
| 2.5.1.65 | R297A |
site-directed mutagenesis, highly reduced activity with phospho-L-serine compared to the wild-type enzyme |
659728 |
