Protein Variants | Comment | Organism |
---|---|---|
L193E | site-directed mutagenesis, the mutant is active on Pro-Pro in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
L193E/V302D | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
L193R | site-directed mutagenesis, the mutation in the S1 site eliminates the allosteric behaviour of the enzyme, the mutant is active on Pro-Pro and Gly-Pro in presence of zinc ions in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
L193R/V302D | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
L193T | site-directed mutagenesis, the mutant is active on Pro-Pro and Gly-Pro in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
V302D | site-directed mutagenesis, the mutation in the S1 site eliminates the allosteric behaviour of the enzyme. The mutant is active on Pro-Pro in presence of zinc ions in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
V302K | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
V302T | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of wild-type and mutant enzymes | Lactococcus lactis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | activates | Lactococcus lactis | |
Zn2+ | activates | Lactococcus lactis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lactococcus lactis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Arg-Pro + H2O | - |
Lactococcus lactis | Arg + Pro | - |
? | |
Leu-Pro + H2O | - |
Lactococcus lactis | Leu + Pro | - |
? | |
Lys-Pro + H2O | - |
Lactococcus lactis | Lys + Pro | - |
? | |
additional information | wild-type Lactococcus lactis prolidase preferably hydrolyzes Xaa-Pro dipeptides where Xaa is a hydrophobic amino acid. Anionic Glu-Pro and Asp-Pro dipeptides cannot be hydrolyzed at any observable rates, and the hydrolysis of cationic Arg-Pro and Lys-Pro dipeptides is at about one tenth of the rate of Leu-Pro, no activity with tripeptides Leu-Leu-Pro and Leu-Val-Pro, substrate specificity of wild-type and mutant enzymes, the enzyme activity depends highly on the metal ion, overview | Lactococcus lactis | ? | - |
? | |
Phe-Pro + H2O | - |
Lactococcus lactis | Phe + Pro | - |
? | |
Val-Pro + H2O | - |
Lactococcus lactis | Val + Pro | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
temperature optimum of the wild-type enzyme | Lactococcus lactis |
60 | - |
temperature optimum of the mutant enzymes L193R, V302D, and L193T | Lactococcus lactis |
70 | - |
temperature optimum of the mutant enzymes L193E/V302D and L193R/V302D, the wild-type enzyme is inactive | Lactococcus lactis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
wild-type enzyme | Lactococcus lactis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 8.5 | activity profiles of wild-type and mutant enzymes, overview | Lactococcus lactis |