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Literature summary extracted from

  • Yang, S.I.; Tanaka, T.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.13.9 expression of the enzyme from strain NRRL B-1821 in Escherichia coli, method optimization 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 the recombinant enzyme shows an allosteric behaviour, overview Lactococcus lactis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.13.9 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
3.4.13.9 additional information the substrate specificity is dependent on the catalytic metal cation, molecular modeling, overview Lactococcus lactis
3.4.13.9 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.13.9 40000
-
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry Lactococcus lactis
3.4.13.9 40164
-
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry Lactococcus lactis
3.4.13.9 80000
-
about, recombinant enzyme, gel filtration Lactococcus lactis

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.9 Lactococcus lactis A8WBX8 gene pepQ; gene pepQ
-
3.4.13.9 Lactococcus lactis NRRL B-1821 A8WBX8 gene pepQ; gene pepQ
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.13.9 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.13.9 197.2
-
purified recombinant enzyme Lactococcus lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.13.9 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
-
?
3.4.13.9 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
-
?
3.4.13.9 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
-
?
3.4.13.9 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
-
?
3.4.13.9 Lys-Pro + H2O
-
Lactococcus lactis Lys + Pro
-
?
3.4.13.9 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 ?
-
?
3.4.13.9 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 ?
-
?
3.4.13.9 Phe-Pro + H2O
-
Lactococcus lactis Phe + Pro
-
?
3.4.13.9 Phe-Pro + H2O
-
Lactococcus lactis NRRL B-1821 Phe + Pro
-
?
3.4.13.9 Val-Pro + H2O
-
Lactococcus lactis Val + Pro
-
?
3.4.13.9 Val-Pro + H2O
-
Lactococcus lactis NRRL B-1821 Val + Pro
-
?

Subunits

EC Number Subunits Comment Organism
3.4.13.9 dimer 2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry Lactococcus lactis
3.4.13.9 More molecular modeling, overview Lactococcus lactis

Synonyms

EC Number Synonyms Comment Organism
3.4.13.9 prolidase
-
Lactococcus lactis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.13.9 50
-
assay at Lactococcus lactis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.13.9 35 60 67% of maximal activity at 60°C, no activity at 70°C Lactococcus lactis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.13.9 30 55 30 min, purified recombinant enzyme, over 50% remaining activity Lactococcus lactis
3.4.13.9 60
-
30 min, purified recombinant enzyme, 22% remaining activity Lactococcus lactis
3.4.13.9 67
-
denaturation temperature Lactococcus lactis
3.4.13.9 70
-
30 min, purified recombinant enzyme, inactivation Lactococcus lactis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.13.9 7
-
recombinant enzyme Lactococcus lactis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.13.9 6 8 pH profile, overview Lactococcus lactis