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Literature summary 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)

EC Number Cloned (Comment) Organism
3.4.13.9 expression in Escherichia coli Pyrococcus horikoshii

Protein Variants

EC Number Protein Variants Comment Organism
3.4.13.9 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
3.4.13.9 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
3.4.13.9 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
3.4.13.9 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
3.4.13.9 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.13.9 0.81
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii
3.4.13.9 0.92
-
 Leu-Pro pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
3.4.13.9 0.98
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
3.4.13.9 1.6
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
3.4.13.9 2.92
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.9 Pyrococcus horikoshii O58691
-
-
3.4.13.9 Pyrococcus horikoshii DSM 12428 O58691
-
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.13.9 809
-
 substratwe: Leu-Pro, pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
3.4.13.9 1119
-
 substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
3.4.13.9 1245
-
 substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii
3.4.13.9 1597
-
 substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
3.4.13.9 2146
-
 substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.4.13.9 PH0974 locus name Pyrococcus horikoshii
3.4.13.9 Ph1prol
-
 Pyrococcus horikoshii
3.4.13.9 prolidase
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.13.9 100
-
 wild-type enzyme and mutant enzymes A195T/G306S, Y301C/K342N, E127G/E252D and E36V Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.13.9 112
-
 Tm-value for mutant enzyme E127G/E252D is 112.2°C Pyrococcus horikoshii
3.4.13.9 114
-
 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
3.4.13.9 115
-
 Tm-value for mutant enzyme E36V is 112.2°C Pyrococcus horikoshii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.13.9 1079
-
 Leu-Pro pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
3.4.13.9 1492
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
3.4.13.9 1660
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii
3.4.13.9 2129
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
3.4.13.9 2861
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.13.9 7
-
 assay at Pyrococcus horikoshii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.13.9 980
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme Y301C/K342N Pyrococcus horikoshii
3.4.13.9 1172
-
 Leu-Pro pH 7.0, 70°C, wild-type enzyme Pyrococcus horikoshii
3.4.13.9 1331
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme E36V Pyrococcus horikoshii
3.4.13.9 1522
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme E127G/E252D Pyrococcus horikoshii
3.4.13.9 2049
-
 Leu-Pro pH 7.0, 70°C, mutant enzyme A195T/G306S Pyrococcus horikoshii