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Literature summary for 2.7.9.2 extracted from

  • Theriot, C.; Tove, S.; Grunden, A.
    Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii (2010), Appl. Microbiol. Biotechnol., 86, 177-188 .
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
AMP pH 6.5, 50°C Pyrococcus horikoshii
1
-
phosphoenolpyruvate pH 6.5, 50°C Pyrococcus horikoshii
35
-
phosphate pH 6.5, 50°C Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
670000
-
more than 670000 Da Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.3
-
pH 6.5, 50°C, ATP-dependent pyruvate consumption Pyrococcus horikoshii
13.3
-
pH 6.5, 50°C, AMP-dependent kinase activity Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + phosphoenolpyruvate + phosphate CMP, GMP, IMP, UMP, CDP, GDP, IDP, and UDP are inert as the acceptor. Diphosphate can not be substituted for phosphate. The enzyme does not catalyze the diphosphate-dependent formation of pyruvate from phosphoenolpyruvate and AMP Pyrococcus horikoshii ATP + pyruvate + H2O
-
r
ATP + pyruvate + H2O
-
Pyrococcus horikoshii AMP + phosphoenolpyruvate + phosphate
-
r

Subunits

Subunits Comment Organism
? x * 78000, SDS-PAGE Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
assay at Pyrococcus horikoshii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
the enzyme retains its full activity upon heating at 90°C for 30 min Pyrococcus horikoshii
100
-
the enzyme retains 92% of full activity upon heating at 90°C for 30 min Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Pyrococcus horikoshii

General Information

General Information Comment Organism
metabolism the enzyme that may be responsible for the production of ATP from AMP formed by ADP-dependent glucokinase and phosphofructokinase reactions in the modified Embden-Meyerhof pathway of Pyrococcus furiosus Pyrococcus horikoshii