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Literature summary for 3.4.13.9 extracted from

  • Theriot, C.M.; Semcer, R.L.; Shah, S.S.; Grunden, A.M.
    Improving the catalytic activity of hyperthermophilic Pyrococcus horikoshii prolidase for detoxification of organophosphorus nerve agents over a broad range of temperatures (2011), Archaea, 2011, 565127.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
A195T/G306S mutation causes an increase in Tm-value of 0.1°C. Mutation causes an 1.7fold increase of the catalytic efficiency towards Leu-Pro Pyrococcus horikoshii
E127G/E252D mutation causes an decrease in Tm-value of 2.1°C. Mutation causes an 1.3fold increase of the catalytic efficiency towards Leu-Pro Pyrococcus horikoshii
E36V mutation causes an increase in Tm-value of 0.6°C. Mutation causes an 1.1fold increase of the catalytic efficiency towards Leu-Pro Pyrococcus horikoshii
additional information randomly mutated enzymes are prepared Tt obtain a better enzyme for organophosphorus nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity Pyrococcus horikoshii
Y301C/K342N mutation causes an decrease in Tm-value of 0.5°C. Mutation causes an 1.2fold decrease of the catalytic efficiency towards Leu-Pro Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.81
-
Leu-Pro pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii
0.92
-
Leu-Pro pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
0.98
-
Leu-Pro pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
1.6
-
Leu-Pro pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
2.92
-
Leu-Pro pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58691
-
-
Pyrococcus horikoshii DSM 12428 O58691
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type enzyme and mutant enzymes A195T/G306S, Y301C/K342N, E127G/E252D and E36V Pyrococcus horikoshii

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
809
-
substratwe: Leu-Pro, pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
1119
-
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
1245
-
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii
1597
-
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
2146
-
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Pro + H2O
-
Pyrococcus horikoshii Ala + Pro
-
?
Gly-Pro + H2O
-
Pyrococcus horikoshii Gly + Pro
-
?
Gly-Pro + H2O
-
Pyrococcus horikoshii DSM 12428 Gly + Pro
-
?
Leu-Pro + H2O
-
Pyrococcus horikoshii Leu + Pro
-
?
Leu-Pro + H2O
-
Pyrococcus horikoshii DSM 12428 Leu + Pro
-
?
Met-Pro + H2O
-
Pyrococcus horikoshii Met + Pro
-
?
Met-Pro + H2O
-
Pyrococcus horikoshii DSM 12428 Met + Pro
-
?
Phe-Pro + H2O
-
Pyrococcus horikoshii Phe + Pro
-
?
Phe-Pro + H2O
-
Pyrococcus horikoshii DSM 12428 Phe + Pro
-
?
Val-Pro + H2O
-
Pyrococcus horikoshii Val + Pro
-
?
Val-Pro + H2O
-
Pyrococcus horikoshii DSM 12428 Val + Pro
-
?

Synonyms

Synonyms Comment Organism
PH0974 locus name Pyrococcus horikoshii
Ph1prol
-
Pyrococcus horikoshii
prolidase
-
Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
100
-
wild-type enzyme and mutant enzymes A195T/G306S, Y301C/K342N, E127G/E252D and E36V Pyrococcus horikoshii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
112
-
Tm-value for mutant enzyme E127G/E252D is 112.2°C Pyrococcus horikoshii
114
-
Tm-value for wild-type enzyme is 114.3°C, Tm-value for mutant enzyme A195T/G306S is 114.4°C, Tm-value for mutant enzyme Y301C/K342N is 113.8°C Pyrococcus horikoshii
115
-
Tm-value for mutant enzyme E36V is 112.2°C Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1079
-
Leu-Pro pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
1492
-
Leu-Pro pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
1660
-
Leu-Pro pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii
2129
-
Leu-Pro pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
2861
-
Leu-Pro pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Pyrococcus horikoshii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
980
-
Leu-Pro pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii
1172
-
Leu-Pro pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
1331
-
Leu-Pro pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
1522
-
Leu-Pro pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
2049
-
Leu-Pro pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii