Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Co2+ | activates | Pyrococcus horikoshii |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Pyrococcus horikoshii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
bestatin | - |
Pyrococcus horikoshii | |
EDTA | - |
Pyrococcus horikoshii | |
HEPES | - |
Pyrococcus horikoshii | |
additional information | the enzyme is insensitive to the papain and trypsin inhibitor antipain, to the chymotrypsin inhibitor chymostatin, to the cysteine protease inhibitor E-64, to the serine and cysteine protease inhibitor leupeptin, to the aspartate protease inhibitor pepstatin, and to the serine protease inhibitors Pefabloc SC and aprotinin. Puromycin, an inhibitor of some exopeptidases, has no effect on the activity of PhTET2 | Pyrococcus horikoshii | |
phosphoramidon | weak inhibition | Pyrococcus horikoshii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
475000 | - |
tetrahedral dodecameric complex, sedimentation velocity experiments | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O59196 | - |
- |
Pyrococcus horikoshii OT-3 | O59196 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus horikoshii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Ala-Ala 4-nitroanilide + H2O | 2.9% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Ala-Ala + 4-nitroaniline | - |
? | |
Ala-Ala 4-nitroanilide + H2O | 2.9% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii OT-3 | Ala-Ala + 4-nitroaniline | - |
? | |
Ala-Ala-Ala 4-nitroanilide + H2O | 1.3% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Ala-Ala-Ala + 4-nitroaniline | - |
? | |
Ala-Ala-Phe 4-nitroanilide + H2O | 1.2% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Ala-Ala-Phe + 4-nitroaniline | - |
? | |
Asn-7-amido-4-methylcoumarin + H2O | 0.3% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Asn + 7-amino-4-methylcoumarin | - |
? | |
Gln-7-amido-4-methylcoumarin + H2O | 2.8% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Gln + 7-amino-4-methylcoumarin | - |
? | |
Gln-7-amido-4-methylcoumarin + H2O | 2.8% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii OT-3 | Gln + 7-amino-4-methylcoumarin | - |
? | |
glycyl 4-nitroanilide + H2O | 0.3% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | glycine + 4-nitroaniline | - |
? | |
L-alanyl 4-nitroanilide + H2O | 14.3% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | L-alanine + 4-nitroaniline | - |
? | |
L-arginyl 4-nitroanilide + H2O | 0.1% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | L-arginine + 4-nitroaniline | - |
? | |
L-isoleucyl 4-nitroanilide + H2O | 10.8% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | L-isoleucine + 4-nitroaniline | - |
? | |
L-leucyl 4-nitroanilide + H2O | - |
Pyrococcus horikoshii | L-leucine + 4-nitroaniline | - |
? | |
L-lysyl 4-nitroanilide + H2O | 0.2% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | L-lysine + 4-nitroaniline | - |
? | |
L-methionyl 4-nitroanilide + H2O | 26.3% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | L-methionine + 4-nitroaniline | - |
? | |
L-phenylalanyl 4-nitroanilide + H2O | 0.8% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | L-phenylalanine + 4-nitroaniline | - |
? | |
L-prolyl 4-nitroanilide + H2O | 0.9% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | L-proline + 4-nitroaniline | - |
? | |
additional information | when assayed with short chromogenic peptides, PhTET2 is active as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. The enzyme can cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. The hydrolytic mechanism is found to be nonprocessive. The enzyme has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity | Pyrococcus horikoshii | ? | - |
? | |
additional information | when assayed with short chromogenic peptides, PhTET2 is active as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. The enzyme can cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. The hydrolytic mechanism is found to be nonprocessive. The enzyme has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity | Pyrococcus horikoshii OT-3 | ? | - |
? | |
Orn-7-amido-4-methylcoumarin + H2O | 0.1% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Orn + 7-amino-4-methylcoumarin | - |
? | |
Ser-7-amido-4-methylcoumarin + H2O | 12.8% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Ser + 7-amino-4-methylcoumarin | - |
? | |
Ser-7-amido-4-methylcoumarin + H2O | 12.8% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii OT-3 | Ser + 7-amino-4-methylcoumarin | - |
? | |
Thr-7-amido-4-methylcoumarin + H2O | 6.1% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Thr + 7-amino-4-methylcoumarin | - |
? | |
Tyr-7-amido-4-methylcoumarin + H2O | 0.9% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Tyr + 7-amino-4-methylcoumarin | - |
? | |
Tyr-7-amido-4-methylcoumarin + H2O | 0.9% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii OT-3 | Tyr + 7-amino-4-methylcoumarin | - |
? | |
Val-7-amido-4-methylcoumarin + H2O | 2.1% of the activity with Leu-4-nitroanilide | Pyrococcus horikoshii | Val + 7-amino-4-methylcoumarin | - |
? |
Subunits | Comment | Organism |
---|---|---|
dodecamer | 12 * 39014, calculated from sequence | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
PH1527 | locus name | Pyrococcus horikoshii |
PhTET2 | - |
Pyrococcus horikoshii |
tetrahedral aminopeptidase 2 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
100 | - |
- |
Pyrococcus horikoshii |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
at temperatures lower than 70 °C, less than 10% of the maximum activity was detected | Pyrococcus horikoshii |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
half-life: 10.03 h | Pyrococcus horikoshii |
90 | - |
half-life: 3.00 h | Pyrococcus horikoshii |
95 | - |
half-life: 59.4 min | Pyrococcus horikoshii |
100 | - |
half-life: 24.8 min | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
substrate: Leu-4-nitroanilide, PIPES buffer | Pyrococcus horikoshii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | substrate: Leu-4-nitroanilide, PIPES buffer, strong activity was still detectable at pH 6 and 9 | Pyrococcus horikoshii |