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Literature summary for 3.4.13.9 extracted from
- Characterization of recombinant prolidase from Lactococcus lactis - changes in substrate specificity by metal cations, and allosteric behavior of the peptidase (2008), FEBS J., 275, 271-280.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the enzyme from strain NRRL B-1821 in Escherichia coli, method optimization | Lactococcus lactis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the recombinant enzyme shows an allosteric behaviour, overview | Lactococcus lactis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mn2+ | two preferred metal cations: zinc and manganese, the substrate Leu-Pro is preferred with zinc, whereas Arg-Pro is preferred with manganese | Lactococcus lactis |  |
| additional information | the substrate specificity is dependent on the catalytic metal cation, molecular modeling, overview | Lactococcus lactis | |
| Zn2+ | two preferred metal cations: zinc and manganese, the substrate Leu-Pro is preferred with zinc, whereas Arg-Pro is preferred with manganese | Lactococcus lactis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40000 | - |
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry | Lactococcus lactis |
| 40164 | - |
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry | Lactococcus lactis |
| 80000 | - |
about, recombinant enzyme, gel filtration | Lactococcus lactis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactococcus lactis | A8WBX8 | gene pepQ; gene pepQ | - |
| Lactococcus lactis NRRL B-1821 | A8WBX8 | gene pepQ; gene pepQ | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant strain NRRL B-1821 enzyme 11.8fold from Escherichia coli by ammonium sulfate fractionation and anion exchange chromatography, method optimization | Lactococcus lactis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 197.2 | - |
purified recombinant enzyme | Lactococcus lactis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Arg-Pro + H2O | the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.57 for Arg-Pro | Lactococcus lactis | Arg + Pro | - |
? | |
| Arg-Pro + H2O | the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.57 for Arg-Pro | Lactococcus lactis NRRL B-1821 | Arg + Pro | - |
? | |
| Leu-Pro + H2O | the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.53 for Leu-Pro | Lactococcus lactis | Leu + Pro | - |
? | |
| Leu-Pro + H2O | the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.53 for Leu-Pro | Lactococcus lactis NRRL B-1821 | Leu + Pro | - |
? | |
| Lys-Pro + H2O | - |
Lactococcus lactis | Lys + Pro | - |
? | |
| additional information | substrate specificity, dependent on the catalytic metal cation, overview, no activity with Pro-Pro, Glu-Pro, Gly-Pro, Asp-Pro, Leu-Leu-Pro, and Leu-Val-Pro, molecular modeling, overview | Lactococcus lactis | ? | - |
? | |
| additional information | substrate specificity, dependent on the catalytic metal cation, overview, no activity with Pro-Pro, Glu-Pro, Gly-Pro, Asp-Pro, Leu-Leu-Pro, and Leu-Val-Pro, molecular modeling, overview | Lactococcus lactis NRRL B-1821 | ? | - |
? | |
| Phe-Pro + H2O | - |
Lactococcus lactis | Phe + Pro | - |
? | |
| Phe-Pro + H2O | - |
Lactococcus lactis NRRL B-1821 | Phe + Pro | - |
? | |
| Val-Pro + H2O | - |
Lactococcus lactis | Val + Pro | - |
? | |
| Val-Pro + H2O | - |
Lactococcus lactis NRRL B-1821 | Val + Pro | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry | Lactococcus lactis |
| More | molecular modeling, overview | Lactococcus lactis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| prolidase | - |
Lactococcus lactis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Lactococcus lactis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | 60 | 67% of maximal activity at 60°C, no activity at 70°C | Lactococcus lactis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 55 | 30 min, purified recombinant enzyme, over 50% remaining activity | Lactococcus lactis |
| 60 | - |
30 min, purified recombinant enzyme, 22% remaining activity | Lactococcus lactis |
| 67 | - |
denaturation temperature | Lactococcus lactis |
| 70 | - |
30 min, purified recombinant enzyme, inactivation | Lactococcus lactis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
recombinant enzyme | Lactococcus lactis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8 | pH profile, overview | Lactococcus lactis |
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