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Literature summary for 2.7.9.2 extracted from
- Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii (2010), Appl. Microbiol. Biotechnol., 86, 177-188 .
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 |
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Release 2023.1 (January 2023)
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