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Literature summary extracted from
- S1 site residues of Lactococcus lactis prolidase affect substrate specificity and allosteric behaviour (2009), Biochim. Biophys. Acta, 1794, 1715-1724.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.13.9 | 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 |
| 3.4.13.9 | L193E/V302D | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
| 3.4.13.9 | 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 |
| 3.4.13.9 | L193R/V302D | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
| 3.4.13.9 | 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 |
| 3.4.13.9 | 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 |
| 3.4.13.9 | V302K | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
| 3.4.13.9 | V302T | site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme | Lactococcus lactis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.13.9 | additional information | - |
additional information | kinetics of wild-type and mutant enzymes | Lactococcus lactis |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.13.9 | Mn2+ | activates | Lactococcus lactis |  |
| 3.4.13.9 | Zn2+ | activates | Lactococcus lactis | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.13.9 | Lactococcus lactis | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.13.9 | Arg-Pro + H2O | - |
Lactococcus lactis | Arg + Pro | - |
? | |
| 3.4.13.9 | Leu-Pro + H2O | - |
Lactococcus lactis | Leu + Pro | - |
? | |
| 3.4.13.9 | Lys-Pro + H2O | - |
Lactococcus lactis | Lys + Pro | - |
? | |
| 3.4.13.9 | 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 | ? | - |
? | |
| 3.4.13.9 | Phe-Pro + H2O | - |
Lactococcus lactis | Phe + Pro | - |
? | |
| 3.4.13.9 | Val-Pro + H2O | - |
Lactococcus lactis | Val + Pro | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.13.9 | 50 | - |
temperature optimum of the wild-type enzyme | Lactococcus lactis |
| 3.4.13.9 | 60 | - |
temperature optimum of the mutant enzymes L193R, V302D, and L193T | Lactococcus lactis |
| 3.4.13.9 | 70 | - |
temperature optimum of the mutant enzymes L193E/V302D and L193R/V302D, the wild-type enzyme is inactive | Lactococcus lactis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.13.9 | 6.5 | - |
wild-type enzyme | Lactococcus lactis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.13.9 | 4 | 8.5 | activity profiles of wild-type and mutant enzymes, overview | Lactococcus lactis |
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