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Literature summary extracted from
- New deblocking aminopeptidases from Pyrococcus horikoshii (2005), Biosci. Biotechnol. Biochem., 69, 1854-1860.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.B4 | expression in Escherichia coli | Pyrococcus horikoshii |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.B4 | amastatin | - |
Pyrococcus horikoshii |  |
| 3.4.11.B4 | EDTA | - |
Pyrococcus horikoshii | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.B4 | Co2+ | activates | Pyrococcus horikoshii | |
| 3.4.11.B4 | Zn2+ | activates | Pyrococcus horikoshii | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B4 | 41000 | - |
8 * 41000, SDS-PAGE | Pyrococcus horikoshii |
| 3.4.11.B4 | 42000 | - |
8 * 42000, SDS-PAGE | Pyrococcus horikoshii |
| 3.4.11.B4 | 330000 | - |
gel filtration | Pyrococcus horikoshii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.B4 | Pyrococcus horikoshii | O59196 | - |
- |
| 3.4.11.B4 | Pyrococcus horikoshii | O59485 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.B4 | - |
Pyrococcus horikoshii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.B4 | 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 | - |
? | |
| 3.4.11.B4 | 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 | - |
? | |
| 3.4.11.B4 | 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 | - |
? | |
| 3.4.11.B4 | 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 | - |
? | |
| 3.4.11.B4 | 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 | ? | - |
? | |
| 3.4.11.B4 | 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 | ? | - |
? | |
| 3.4.11.B4 | 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 | - |
? | |
| 3.4.11.B4 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.B4 | octamer | 8 * 42000, SDS-PAGE | Pyrococcus horikoshii |
| 3.4.11.B4 | octamer | 8 * 41000, SDS-PAGE | Pyrococcus horikoshii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.B4 | DAPPh2 | - |
Pyrococcus horikoshii |
| 3.4.11.B4 | DAPPh3 | - |
Pyrococcus horikoshii |
| 3.4.11.B4 | deblocking aminopeptidase | - |
Pyrococcus horikoshii |
| 3.4.11.B4 | PH1527 | - |
Pyrococcus horikoshii |
| 3.4.11.B4 | PH1821 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B4 | 85 | - |
assay at | Pyrococcus horikoshii |
| 3.4.11.B4 | 100 | - |
- |
Pyrococcus horikoshii |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B4 | 80 | 110 | 80°C: about 50% of maximal activity, 110°C: about 70% of maximal activity | Pyrococcus horikoshii |
| 3.4.11.B4 | 85 | 110 | 85°C: about 40% of maximal activity, 110°C: about 90% of maximal activity | Pyrococcus horikoshii |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B4 | 98 | - |
2 h, over 70% of the activbity remains | Pyrococcus horikoshii |
| 3.4.11.B4 | 98 | - |
2 h, over 70% of the activity remains | Pyrococcus horikoshii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B4 | 7 | 7.5 | - |
Pyrococcus horikoshii |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B4 | 6.3 | 8.5 | pH 6.3: about 20% of maximal activity, pH 8.5: about 55% of maximal activity | Pyrococcus horikoshii |
| 3.4.11.B4 | 6.3 | 8.5 | pH 6.3: about 20% of maximal activity, pH 8.5: about 70% of maximal activity | Pyrococcus horikoshii |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.11.B4 | 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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Release 2023.1 (January 2023)
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