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Literature summary extracted from

  • Schoehn, G.; Vellieux, F.M.; Asuncion Dura, M.; Receveur-Brechot, V.; Fabry, C.M.; Ruigrok, R.W.; Ebel, C.; Roussel, A.; Franzetti, B.
    An archaeal peptidase assembles into two different quaternary structures A tetrahedron and a giant octahedron (2006), J. Biol. Chem., 281, 36327-36337 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.B8 expression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.B8
-
Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.B8 Co2+ activates Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.B8 Pyrococcus horikoshii O58255
-
-
3.4.11.B8 Pyrococcus horikoshii OT-3 O58255
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.B8
-
Pyrococcus horikoshii

Substrates and Products (Substrate)

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 ?
-
?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.B8 90
-
assay at Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.B8 7.5
-
assay Pyrococcus horikoshii

General Information

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