Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Zhang, G.; Chen, J.A.; Tanaka, T.
    Deregulation of allosteric response of Lactococcus lactis prolidase and its effects on enzyme activity (2009), Biochim. Biophys. Acta, 1794, 968-975.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.13.9 expressed in Escherichia coli Top10F' cells Lactococcus lactis

Protein Variants

EC Number Protein Variants Comment Organism
3.4.13.9 H303S/S307G inactive Lactococcus lactis
3.4.13.9 R293S the mutation results in the disappearance of the allosteric behaviour yielding a Hill constant of 0.98 while the wild type has a constant of 1.58 and suppresses the substrate inhibition that is observed in other mutants and wild type enzyme, the Km value for L-Leu-L-Pro is 2.9fold larger and Vmax is approximately 50% less as compared to the wild type enzyme Lactococcus lactis
3.4.13.9 R293S/S307G mutant shows strongly reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis
3.4.13.9 S307D mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis
3.4.13.9 S307G mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis
3.4.13.9 S307R mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.13.9 L-Leu-L-Pro
-
 Lactococcus lactis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.13.9 1.7
-
 L-Leu-L-Pro mutant enzyme S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C Lactococcus lactis
3.4.13.9 8
-
 L-Leu-L-Pro wild type enzyme, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C Lactococcus lactis
3.4.13.9 10.1
-
 L-Leu-L-Pro mutant enzyme R293S/S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C Lactococcus lactis
3.4.13.9 14.7
-
 L-Leu-L-Pro mutant enzyme S307R, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C Lactococcus lactis
3.4.13.9 18
-
 L-Leu-L-Pro mutant enzyme S307D, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C Lactococcus lactis
3.4.13.9 23.3
-
 L-Leu-L-Pro mutant enzyme R293S, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C Lactococcus lactis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.13.9 Zn2+ required for optimum activity Lactococcus lactis

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.9 Lactococcus lactis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.13.9 DEAE Sephacel column chromatography 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 0.33
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 0.48
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 0.64
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 1.1
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 1.4
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 1.4
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 1.7
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 2
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 2.7
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 3 3.9 mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 3.2
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 3.2
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 4.3
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 4.4
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 4.8
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 5
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 5.2
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 5.3
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 5.9
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 6.2
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 7
-
 mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 7.8
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 8.2
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 8.9
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 9.6
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 9.6
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 10.6
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 11.6
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 11.9
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 12.4
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 12.8
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 13.4
-
 mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 13.6
-
 mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 18.4
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 22.7
-
 mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 25.6
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 27.3
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 27.6
-
 mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 30.9
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 31.5
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 32.3
-
 mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 32.7
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 36.9
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 42.3
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 46.7
-
 mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 48.3
-
 mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 53.7
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 56.2
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 64.9
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 67.7
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 78.2
-
 mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 81.8
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 87.8
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 100.8
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 111.4
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 159.7
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 166.1
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 234.5
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 463.7
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
3.4.13.9 468.7
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.13.9 L-Arg-L-Pro + H2O 12.0% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2 Lactococcus lactis L-Arg + L-Pro
-
 ?
3.4.13.9 L-Leu-L-Pro + H2O 100% activity in the presence of 1 mM ZnCl2 Lactococcus lactis L-Leu + L-Pro
-
 ?
3.4.13.9 L-Lys-L-Pro + H2O 6.6% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2 Lactococcus lactis L-Lys + L-Pro
-
 ?
3.4.13.9 L-Phe-L-Pro + H2O 23.8% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2 Lactococcus lactis L-Phe + L-Pro
-
 ?
3.4.13.9 L-Val-L-Pro + H2O 14.4% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2 Lactococcus lactis L-Val + L-Pro
-
 ?
3.4.13.9 additional information does not degrade L-Glu-L-Pro, Gly-L-Pro, L-Pro-L-Pro, L-Leu-L-Leu-L-Pro, L-Leu-L-Val-L-Pro, and L-Asp-L-Pro Lactococcus lactis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.13.9 prolidase
-
 Lactococcus lactis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.13.9 15.3
-
 L-Leu-L-Pro wild type enzyme, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C Lactococcus lactis