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	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	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