EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.11.B8 | expression in Escherichia coli | Pyrococcus horikoshii |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.11.B8 | - |
Pyrococcus horikoshii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.B8 | Co2+ | activates | Pyrococcus horikoshii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.11.B8 | Pyrococcus horikoshii | O58255 | - |
- |
3.4.11.B8 | Pyrococcus horikoshii OT-3 | O58255 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.11.B8 | - |
Pyrococcus horikoshii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.11.B8 | Ala-Ala + H2O | - |
Pyrococcus horikoshii | Ala + Ala | - |
? | |
3.4.11.B8 | Ala-Ala + H2O | - |
Pyrococcus horikoshii OT-3 | Ala + Ala | - |
? | |
3.4.11.B8 | Ala-Ala 4-nitroanilide + H2O | the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide | Pyrococcus horikoshii | Ala + Ala 4-nitroanilide | - |
? | |
3.4.11.B8 | Ala-Ala-Ala + H2O | the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide | Pyrococcus horikoshii | Ala + Ala-Ala | - |
? | |
3.4.11.B8 | Ala-Ala-Ala + H2O | the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala-4-nitroanilide | Pyrococcus horikoshii | Ala + Ala-Ala | - |
? | |
3.4.11.B8 | Ala-Ala-Ala + H2O | the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide | Pyrococcus horikoshii OT-3 | Ala + Ala-Ala | - |
? | |
3.4.11.B8 | Ala-Ala-Ala + H2O | the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala-4-nitroanilide | Pyrococcus horikoshii OT-3 | Ala + Ala-Ala | - |
? | |
3.4.11.B8 | Ala-Ala-Ala 4-nitroanilide + H2O | best substraet for the dodecameric form of the enzyme | Pyrococcus horikoshii | Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide | - |
? | |
3.4.11.B8 | Ala-Ala-Ala 4-nitroanilide + H2O | best substrat for the dodecameric form of the enzyme | Pyrococcus horikoshii | Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide | - |
? | |
3.4.11.B8 | Asp-Ala + H2O | - |
Pyrococcus horikoshii | Asp + Ala | - |
? | |
3.4.11.B8 | Asp-Ala + H2O | - |
Pyrococcus horikoshii OT-3 | Asp + Ala | - |
? | |
3.4.11.B8 | additional information | PhTET1 activity cannot be detected by using chromogenic aminoacyl compounds (7-amino-4-methylcoumarin (AMC) or p-nitroanilide), probably because the X-AMC and X-4-nitroanilide molecules cannot fit into the active site pocket or because these compounds fit but are not hydrolyzed. HPLC analysis of Ala-Ala-p-nitroanilide degradation by the two PhTET1 oligomers shows that the generation of Ala-4-nitroanilide is not linear with time, suggesting product inhibition. PhTET1 can cleave the N-terminal amino acid of larger peptides, even when the 4-nitroanilide moiety is in the C-terminal position, and can also hydrolyze dipeptides like Ala-Ala or Asp-Ala. Therefore, PhTET1 seems to be unable to cleave a peptidic bond when 4-nitroanilide or 7-amino-4-methylcoumarin is in the P1' position, making activity assays difficult. Activity of the dodecamer enzyme form increases with substrate chain length. No hydrolytic activity toward N-acetyl-Leu-4-nitroanilide and N-succinyl-Ala-Ala 4-nitroanilide | Pyrococcus horikoshii | ? | - |
? | |
3.4.11.B8 | additional information | PhTET1 activity cannot be detected by using chromogenic aminoacyl compounds (7-amino-4-methylcoumarin (AMC) or p-nitroanilide), probably because the X-AMC and X-4-nitroanilide molecules cannot fit into the active site pocket or because these compounds fit but are not hydrolyzed. HPLC analysis of Ala-Ala-p-nitroanilide degradation by the two PhTET1 oligomers shows that the generation of Ala-4-nitroanilide is not linear with time, suggesting product inhibition. PhTET1 can cleave the N-terminal amino acid of larger peptides, even when the 4-nitroanilide moiety is in the C-terminal position, and can also hydrolyze dipeptides like Ala-Ala or Asp-Ala. Therefore, PhTET1 seems to be unable to cleave a peptidic bond when 4-nitroanilide or 7-amino-4-methylcoumarin is in the P1' position, making activity assays difficult. Activity of the dodecamer enzyme form increases with substrate chain length. No hydrolytic activity toward N-acetyl-Leu-4-nitroanilide and N-succinyl-Ala-Ala 4-nitroanilide | Pyrococcus horikoshii OT-3 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.11.B8 | dodecamer | the enzyme assembles as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. The internal organization of the PhTET1 particles reveals highly self-compartmentalized systems made of networks of access channels extended by vast catalytic chambers. The two edifices display aminopeptidase activity. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex | Pyrococcus horikoshii |
3.4.11.B8 | dodecamer | the quaternary structures of PhTET1 reveal an elaborated self-compartmentalized organization for a peptidase complex. The enzyme assembles as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex. PhTET1 assembles into two different quaternary structures because of quasi-equivalent contacts previously identified in viral capsids. The dodecameric complex is in general more active than the 24-subunit edifice | Pyrococcus horikoshii |
3.4.11.B8 | tetracosamer | the enzyme assembles as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. The internal organization of the PhTET1 particles reveals highly self-compartmentalized systems made of networks of access channels extended by vast catalytic chambers. The two edifices display aminopeptidase activity. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex | Pyrococcus horikoshii |
3.4.11.B8 | tetracosamer | the quaternary structures of PhTET1 reveal an elaborated self-compartmentalized organization for a peptidase complex. The enzyme assembles as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex. PhTET1 assembles into two different quaternary structures because of quasi-equivalent contacts previously identified in viral capsids. The dodecameric complex is in general more active than the 24-subunit edifice | Pyrococcus horikoshii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.11.B8 | peptidase TET1 | - |
Pyrococcus horikoshii |
3.4.11.B8 | PH0519 | - |
Pyrococcus horikoshii |
3.4.11.B8 | PhTET1 | - |
Pyrococcus horikoshii |
3.4.11.B8 | TET1 | - |
Pyrococcus horikoshii |
3.4.11.B8 | tetrahedral aminopeptidase 1 | - |
Pyrococcus horikoshii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.11.B8 | 90 | - |
assay at | Pyrococcus horikoshii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.11.B8 | 7.5 | - |
assay | Pyrococcus horikoshii |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.11.B8 | metabolism | the enzyme plays a key roles in the regulation of many cellular processes | Pyrococcus horikoshii |