EC Number   |
Subunits |
Reference |
|---|
   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 |
-, 745279 |
| 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 |
-, 745279 |
| 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 |
-, 745279 |
| 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 |
-, 745279 |
