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Literature summary extracted from
- Biochemical characterization of deblocking aminopeptidases from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (2011), Biosci. Biotechnol. Biochem., 75, 1160-1166.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.B6 | expression in Escherichia coli | Thermococcus kodakarensis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.B6 | EDTA | - |
Thermococcus kodakarensis |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B6 | 120000 | - |
trimer, gel filtration | Thermococcus kodakarensis |
| 3.4.11.B6 | 450000 | - |
octadecamer, gel filtration | Thermococcus kodakarensis |
| 3.4.11.B6 | 670000 | - |
dodecamer, gel filtration | Thermococcus kodakarensis |
| 3.4.11.B6 | 690000 | - |
dodecamer, gel filtration | Thermococcus kodakarensis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.B6 | Thermococcus kodakarensis | Q5JH87 | - |
- |
| 3.4.11.B6 | Thermococcus kodakarensis | Q5JHA5 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.B6 | - |
Thermococcus kodakarensis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.B6 | Ala-Ala-Ala 4-nitroanilide + H2O | about 10% of the activity with L-leucyl 4-nitroanilide | Thermococcus kodakarensis | L-alanine + Ala-Ala-Ala 4-nitroanilide | - |
? | |
| 3.4.11.B6 | Ala-Ala-Ala-4-nitroanilide + H2O | about 10% of the activity with Leu-4-nitroanilide | Thermococcus kodakarensis | L-alanine + Ala-Ala-Ala 4-nitroanilide | - |
? | |
| 3.4.11.B6 | L-leucyl 4-nitroanilide + H2O | highest specific activity compared to other substrates tested | Thermococcus kodakarensis | L-leucine + 4-nitroaniline | - |
? | |
| 3.4.11.B6 | N-acetyl-Ala-Ala-Ala + H2O | about 65% of the activity with L-leucyl 4-nitroanilide | Thermococcus kodakarensis | N-acetyl-L-alanine + Ala-Ala | - |
? | |
| 3.4.11.B6 | N-acetyl-Ala-Ala-Ala + H2O | about 65% of the activity with Leu-4-nitroanilide | Thermococcus kodakarensis | N-acetyl-L-alanine + Ala-Ala | - |
? | |
| 3.4.11.B6 | N-acetyl-L-leucyl 4-nitroanilide + H2O | about 30% of the activity with L-leucyl 4-nitroanilide | Thermococcus kodakarensis | N-acetyl-L-leucine + 4-nitroaniline | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.B6 | dodecamer | the enzyme displays a trimer, octadecamer and dodecamer assembly. The dodecamer structure is the main one | Thermococcus kodakarensis |
| 3.4.11.B6 | dodecamer | the enzyme displays an octadecamer and dodecamer assembly. The dodecameric structure is the main one | Thermococcus kodakarensis |
| 3.4.11.B6 | octadecamer | the enzyme displays a trimer, octadecamer and dodecamer assembly. The dodecamer structure is the main one | Thermococcus kodakarensis |
| 3.4.11.B6 | octadecamer | the enzyme displays an octadecamer and dodecamer assembly. The dodecameric structure is the main one | Thermococcus kodakarensis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.B6 | deblocking aminopeptidase | ambiguous | Thermococcus kodakarensis |
| 3.4.11.B6 | TK0775 | - |
Thermococcus kodakarensis |
| 3.4.11.B6 | TK0781 | - |
Thermococcus kodakarensis |
| 3.4.11.B6 | TkDAP1 | - |
Thermococcus kodakarensis |
| 3.4.11.B6 | TkDAP2 | - |
Thermococcus kodakarensis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B6 | 80 | - |
substrate: Ala-Ala-Ala 4-nitroanilide | Thermococcus kodakarensis |
| 3.4.11.B6 | 80 | - |
substrate: N-acetyl-Ala-Ala-Ala | Thermococcus kodakarensis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B6 | 60 | 100 | 60°C: about 40% of maximal activity, 100°C: about 70% of maximal activity | Thermococcus kodakarensis |
| 3.4.11.B6 | 60 | 100 | 60°C: about 60% of maximal activity, 100°C: about 70% of maximal activity | Thermococcus kodakarensis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B6 | 7.4 | - |
substrate: Ala-Ala-Ala 4-nitroanilide | Thermococcus kodakarensis |
| 3.4.11.B6 | 7.4 | - |
substrate: N-acetyl-Ala-Ala-Ala | Thermococcus kodakarensis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B6 | 6.2 | 8 | pH 6.2: about 35% of maximal activity, pH 8.0: about 50% of maximal activity, substrate: Ala-Ala-Ala 4-nitroanilide | Thermococcus kodakarensis |
| 3.4.11.B6 | 6.2 | 8.5 | pH 6.2: about 50% of maximal activity, pH 8.5: about 50% of maximal activity, substrate: N-acetyl-Ala-Ala-Ala | Thermococcus kodakarensis |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 3.4.11.B6 | Thermococcus kodakarensis | not induced by heat and oxidative stress | additional information |
| 3.4.11.B6 | Thermococcus kodakarensis | induced by heat and oxidative stress | up |
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