EC Number |
Protein Variants |
Reference |
---|
6.3.3.6 | K443A |
at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity |
721605 |
6.3.3.6 | K443M |
at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity |
721605 |
6.3.3.6 | E380A |
kcat/Km is 74.3fold lower compared to wild-type value |
721613 |
6.3.3.6 | E380D |
retains a functional general base with a pKa of about 7.4 for kcat. The acidic region of the log (kcat/Km) versus pH profiles displays an ionizable group with a pKa of about 7.7. kcat/Km is 1.4fold lower compared to wild-type value |
721613 |
6.3.3.6 | E380Q |
variant displays a plateau in the acidic region. The acidic region of the log (kcat/Km) versus pH profiles becomes pH-independent for E380Q. kcat/Km is 3.8fold lower compared to wild-type value |
721613 |
6.3.3.6 | Y345A |
mutant exhibits a 5fold increase in Km of (2S,5S)-5-carboxymethylproline and a 165fold decrease in specificity constant compared to wild-type enzyme. kcat/Km is 165fold lower compared to wild-type value |
721613 |
6.3.3.6 | Y345A/E380A |
kcat/Km is 87fold lower compared to wild-type value |
721613 |
6.3.3.6 | Y345F |
pH-dependent kcat and kcat/Km plots retain the bell-shaped curve of wild-type CPS with similar pK values. kcat/Km is 1.7fold lower compared to wild-type value |
721613 |
6.3.3.6 | Y345F/E380D |
kcat/Km is 87fold lower compared to wild-type value |
721613 |
6.3.3.6 | Y345F/E380Q |
kcat/Km is 95fold lower compared to wild-type value |
721613 |