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Literature summary for 3.4.13.9 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
Search for more literature for 3.4.13.9

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
H303S/S307G inactive Lactococcus lactis
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
R293S/S307G mutant shows strongly reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis
S307D mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis
S307G mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis
S307R mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme Lactococcus lactis

Inhibitors

Inhibitors Comment Organism Structure
L-Leu-L-Pro
-
 Lactococcus lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
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
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
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

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

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE Sephacel column chromatography Lactococcus lactis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.33
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
0.48
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
0.64
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
1.1
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
1.4
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
1.4
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
1.7
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
2
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
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 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
3.2
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
3.2
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
4.3
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
4.4
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
4.8
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
5
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
5.2
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
5.3
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
5.9
-
 mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
6.2
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
7
-
 mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
7.8
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
8.2
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
8.9
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
9.6
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
9.6
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
10.6
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
11.6
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
11.9
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
12.4
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
12.8
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
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
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
18.4
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
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
25.6
-
 mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
27.3
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
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
30.9
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C Lactococcus lactis
31.5
-
 mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
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
32.7
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
36.9
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
42.3
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
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
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
53.7
-
 mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
56.2
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
64.9
-
 mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
67.7
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
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
81.8
-
 mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
87.8
-
 mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
100.8
-
 mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
111.4
-
 wild type enzyme, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
159.7
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C Lactococcus lactis
166.1
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C Lactococcus lactis
234.5
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C Lactococcus lactis
463.7
-
 wild type enzyme, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C Lactococcus lactis
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
L-Leu-L-Pro + H2O 100% activity in the presence of 1 mM ZnCl2 Lactococcus lactis L-Leu + L-Pro
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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

Synonyms Comment Organism
prolidase
-
 Lactococcus lactis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
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