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Results 1 - 10 of 10
EC Number
Amino acid exchange
Commentary
Reference
E380A
kcat/Km is 74.3fold lower compared to wild-type value
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
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
K443A
at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity
K443M
at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity
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
Y345A/E380A
kcat/Km is 87fold lower compared to wild-type value
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
Y345F/E380D
kcat/Km is 87fold lower compared to wild-type value
Y345F/E380Q
kcat/Km is 95fold lower compared to wild-type value
Results 1 - 10 of 10