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Literature summary for 3.4.11.B4 extracted from
- New deblocking aminopeptidases from Pyrococcus horikoshii (2005), Biosci. Biotechnol. Biochem., 69, 1854-1860.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Pyrococcus horikoshii |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| amastatin | - |
Pyrococcus horikoshii |  |
| EDTA | - |
Pyrococcus horikoshii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates | Pyrococcus horikoshii | |
| Zn2+ | activates | Pyrococcus horikoshii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 41000 | - |
8 * 41000, SDS-PAGE | Pyrococcus horikoshii |
| 42000 | - |
8 * 42000, SDS-PAGE | Pyrococcus horikoshii |
| 330000 | - |
gel filtration | Pyrococcus horikoshii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus horikoshii | O59196 | - |
- |
| Pyrococcus horikoshii | O59485 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pyrococcus horikoshii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Ala-Ala + H2O | the activity (turnover number) with N-acetyl-Ala-Ala is 11500fold lower compared to the activity with Ala-Ala | Pyrococcus horikoshii | L-alanine + L-alanine | - |
? | |
| Ala-Ala + H2O | the turnover number with N-acetyl-Ala-Ala is 350fold lower compared to the activity with Ala-Ala | Pyrococcus horikoshii | L-alanine + L-alanine | - |
? | |
| Ala-Ala-Ala + H2O | the activity (turnover number) with N-acetyl-Ala-Ala-Ala is 1700fold lower compared to the activity with Ala-Ala-Ala | Pyrococcus horikoshii | Ala-Ala + L-alanine | - |
? | |
| Ala-Ala-Ala + H2O | the turnover number with N-acetyl-Ala-Ala-Ala is 540fold lower compared to the activity with Ala-Ala-Ala | Pyrococcus horikoshii | Ala-Ala + L-alanine | - |
? | |
| additional information | low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme exhibits aminopeptidase and with lower efficiency deblocking activity (hydrolysis of acetylated amino acids from the N-terminus of peptides). No activity with Ala-Pro-Ala, D-Ala-Ala and D-Ala-D-Ala-D-Ala | Pyrococcus horikoshii | ? | - |
? | |
| additional information | low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme exhibits aminopeptidase and with lower efficiency deblocking activity (hydrolysis of N-acetylated amino acids from the N-terminus of peptides). No activity with Ala-Pro-Ala, D-Ala-Ala and D-Ala-D-Ala-D-Ala | Pyrococcus horikoshii | ? | - |
? | |
| N-acetyl-Ala-Ala-Ala + H2O | the turnover number with N-acetyl-Ala-Ala-Ala is 540fold lower compared to the activity with Ala-Ala-Ala | Pyrococcus horikoshii | Ala-Ala + N-acetyl-L-alanine | - |
? | |
| N-acetyl-L-Ala-Ala + H2O | the turnover number with N-acetyl-Ala-Ala is 350fold lower compared to the activity with Ala-Ala | Pyrococcus horikoshii | N-acetyl-L-alanine + L-alanine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| octamer | 8 * 42000, SDS-PAGE | Pyrococcus horikoshii |
| octamer | 8 * 41000, SDS-PAGE | Pyrococcus horikoshii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DAPPh2 | - |
Pyrococcus horikoshii |
| DAPPh3 | - |
Pyrococcus horikoshii |
| deblocking aminopeptidase | - |
Pyrococcus horikoshii |
| PH1527 | - |
Pyrococcus horikoshii |
| PH1821 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
assay at | Pyrococcus horikoshii |
| 100 | - |
- |
Pyrococcus horikoshii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | 110 | 80°C: about 50% of maximal activity, 110°C: about 70% of maximal activity | Pyrococcus horikoshii |
| 85 | 110 | 85°C: about 40% of maximal activity, 110°C: about 90% of maximal activity | Pyrococcus horikoshii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 98 | - |
2 h, over 70% of the activbity remains | Pyrococcus horikoshii |
| 98 | - |
2 h, over 70% of the activity remains | Pyrococcus horikoshii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 7.5 | - |
Pyrococcus horikoshii |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.3 | 8.5 | pH 6.3: about 20% of maximal activity, pH 8.5: about 55% of maximal activity | Pyrococcus horikoshii |
| 6.3 | 8.5 | pH 6.3: about 20% of maximal activity, pH 8.5: about 70% of maximal activity | Pyrococcus horikoshii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | Pyrococcus horikoshii has three similar aminopeptidases with deblocking activity. These enzymes appear to play important roles in hydrolyzing small peptides in Pyrococcus horikoshii cells | Pyrococcus horikoshii |
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