BRENDA - Enzyme Database show
show all sequences of 3.4.11.B8

An archaeal peptidase assembles into two different quaternary structures A tetrahedron and a giant octahedron

Schoehn, G.; Vellieux, F.M.; Asuncion Dura, M.; Receveur-Brechot, V.; Fabry, C.M.; Ruigrok, R.W.; Ebel, C.; Roussel, A.; Franzetti, B.; J. Biol. Chem. 281, 36327-36337 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Pyrococcus horikoshii
Crystallization (Commentary)
Crystallization
Organism
-
Pyrococcus horikoshii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
activates
Pyrococcus horikoshii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus horikoshii
O58255
-
-
Pyrococcus horikoshii OT-3
O58255
-
-
Purification (Commentary)
Commentary
Organism
-
Pyrococcus horikoshii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Ala-Ala + H2O
-
745279
Pyrococcus horikoshii
Ala + Ala
-
-
-
?
Ala-Ala + H2O
-
745279
Pyrococcus horikoshii OT-3
Ala + Ala
-
-
-
?
Ala-Ala 4-nitroanilide + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide
745279
Pyrococcus horikoshii
Ala + Ala 4-nitroanilide
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide
745279
Pyrococcus horikoshii
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala-4-nitroanilide
745279
Pyrococcus horikoshii
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide
745279
Pyrococcus horikoshii OT-3
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala-4-nitroanilide
745279
Pyrococcus horikoshii OT-3
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala 4-nitroanilide + H2O
best substraet for the dodecameric form of the enzyme
745279
Pyrococcus horikoshii
Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide
-
-
-
?
Ala-Ala-Ala 4-nitroanilide + H2O
best substrat for the dodecameric form of the enzyme
745279
Pyrococcus horikoshii
Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide
-
-
-
?
Asp-Ala + H2O
-
745279
Pyrococcus horikoshii
Asp + Ala
-
-
-
?
Asp-Ala + H2O
-
745279
Pyrococcus horikoshii OT-3
Asp + Ala
-
-
-
?
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
745279
Pyrococcus horikoshii
?
-
-
-
-
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
745279
Pyrococcus horikoshii OT-3
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
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; 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
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; 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
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
assay at
Pyrococcus horikoshii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay
Pyrococcus horikoshii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pyrococcus horikoshii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
-
Pyrococcus horikoshii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
activates
Pyrococcus horikoshii
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus horikoshii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Ala-Ala + H2O
-
745279
Pyrococcus horikoshii
Ala + Ala
-
-
-
?
Ala-Ala + H2O
-
745279
Pyrococcus horikoshii OT-3
Ala + Ala
-
-
-
?
Ala-Ala 4-nitroanilide + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide
745279
Pyrococcus horikoshii
Ala + Ala 4-nitroanilide
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide
745279
Pyrococcus horikoshii
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala-4-nitroanilide
745279
Pyrococcus horikoshii
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide
745279
Pyrococcus horikoshii OT-3
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala + H2O
the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala-4-nitroanilide
745279
Pyrococcus horikoshii OT-3
Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala 4-nitroanilide + H2O
best substraet for the dodecameric form of the enzyme
745279
Pyrococcus horikoshii
Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide
-
-
-
?
Ala-Ala-Ala 4-nitroanilide + H2O
best substrat for the dodecameric form of the enzyme
745279
Pyrococcus horikoshii
Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide
-
-
-
?
Asp-Ala + H2O
-
745279
Pyrococcus horikoshii
Asp + Ala
-
-
-
?
Asp-Ala + H2O
-
745279
Pyrococcus horikoshii OT-3
Asp + Ala
-
-
-
?
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
745279
Pyrococcus horikoshii
?
-
-
-
-
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
745279
Pyrococcus horikoshii OT-3
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
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; 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
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; 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
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
assay at
Pyrococcus horikoshii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay
Pyrococcus horikoshii
General Information
General Information
Commentary
Organism
metabolism
the enzyme plays a key roles in the regulation of many cellular processes
Pyrococcus horikoshii
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme plays a key roles in the regulation of many cellular processes
Pyrococcus horikoshii
Other publictions for EC 3.4.11.B8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745279
Schoehn
An archaeal peptidase assembl ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
J. Biol. Chem.
281
36327-36337
2006
-
-
1
1
-
-
-
-
-
1
-
-
-
4
-
-
1
-
-
-
-
-
13
2
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
13
2
1
-
-
-
1
-
-
-
-
1
1
-
-
-