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Literature summary extracted from
- Pyrococcus horikoshii TET2 peptidase assembling process and associated functional regulation (2013), J. Biol. Chem., 288, 22542-22554 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.B9 | wild-type and mutant enzymes (R217S/R220S/F224S/H248S/I292A) are expressed Escherichia coli strain BL21. Wild-type and mutant (R217S, R220S, F224S, H248S, and I292A) Phtet2 genes are generated from synthetic DNA fragments optimized for codon usage in Escherichia coli and cloned in the overexpression plasmid pET41c. The resulting constructs are transformed in the Escherichia coli strain BL21 (DE3) for the recombinant expression of wild-type and mutated PhTET2 proteins | Pyrococcus horikoshii |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.11.B9 | R217S/R220S/F224S/H248S/I292A | the mutant is A model to study the oligomerization process | Pyrococcus horikoshii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.B9 | 1 | - |
L-leucyl 4-nitroanilide | pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii |  |
| 3.4.11.B9 | 1.1 | - |
L-leucyl 4-nitroanilide | pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 1.5 | - |
Met-Lys-bradykinin | pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 1.9 | - |
Met-Lys-bradykinin | pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B9 | 78000 | - |
gel filtration, dimer | Pyrococcus horikoshii |
| 3.4.11.B9 | 468000 | - |
gel filtration dodecamer | Pyrococcus horikoshii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.B9 | Pyrococcus horikoshii | O59196 | - |
- |
| 3.4.11.B9 | Pyrococcus horikoshii OT-3 | O59196 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.B9 | - |
Pyrococcus horikoshii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.B9 | L-leucyl 4-nitroanilide + H2O | - |
Pyrococcus horikoshii | L-leucine + 4-nitroaniline | - |
? | |
| 3.4.11.B9 | L-leucyl 4-nitroanilide + H2O | - |
Pyrococcus horikoshii OT-3 | L-leucine + 4-nitroaniline | - |
? | |
| 3.4.11.B9 | Met-Lys-bradykinin + H2O | i.e. MKRPPGFSPFR. The dodecamer is more active than the dimer. Km values of the dimer and the dodecamer are identical. The kcat value of the dimer is significantly lower than the one of the dodecamer. Oligomerization allows the TET2 peptidase to better process long polypeptides | Pyrococcus horikoshii | ? | - |
? | |
| 3.4.11.B9 | Met-Lys-bradykinin + H2O | i.e. MKRPPGFSPFR. The dodecamer is more active than the dimer. Km values of the dimer and the dodecamer are identical. The kcat value of the dimer is significantly lower than the one of the dodecamer. Oligomerization allows the TET2 peptidase to better process long polypeptides | Pyrococcus horikoshii OT-3 | ? | - |
? | |
| 3.4.11.B9 | additional information | the catalytic efficiency of the dimer on a long peptide is lower than the one of the dodecamer. The dodecameric form of PhTET2 is more efficient at processing long peptides than the dimeric form. Under extreme physiological temperatures, free TET2 dimers, which are catalytically active against small peptides, can be accumulated in the Pyrococcus cells as precursors of the TET2 complex | Pyrococcus horikoshii | ? | - |
? | |
| 3.4.11.B9 | additional information | the catalytic efficiency of the dimer on a long peptide is lower than the one of the dodecamer. The dodecameric form of PhTET2 is more efficient at processing long peptides than the dimeric form. Under extreme physiological temperatures, free TET2 dimers, which are catalytically active against small peptides, can be accumulated in the Pyrococcus cells as precursors of the TET2 complex | Pyrococcus horikoshii OT-3 | ? | - |
? | |
| 3.4.11.B9 | VDLTGNRLTY + H2O | the dodecamer is more active than the dimer. Km values of the dimer and the dodecamer are identical. The kcat value of the dimer is significantly lower than the one of the dodecamer. Oligomerization allows the TET2 peptidase to better process long polypeptides | Pyrococcus horikoshii | ? | - |
? | |
| 3.4.11.B9 | VDLTGNRLTY + H2O | the dodecamer is more active than the dimer. Km values of the dimer and the dodecamer are identical. The kcat value of the dimer is significantly lower than the one of the dodecamer. Oligomerization allows the TET2 peptidase to better process long polypeptides | Pyrococcus horikoshii OT-3 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.B9 | dimer | PhTET2 assembling is a highly ordered process in which hexamers represent the main intermediate. Peptide degradation assays demonstrate that oligomerization triggers the activity of the TET enzyme. In vivo, the dimeric precursor co-exists together with assembled TET complexes. The dimer is stable under high temperature conditions | Pyrococcus horikoshii |
| 3.4.11.B9 | dodecamer | PhTET2 assembling is a highly ordered process in which hexamers represent the main intermediate. Peptide degradation assays demonstrate that oligomerization triggers the activity of the TET enzyme. In vivo, the dimeric precursor co-exists together with assembled TET complexes | Pyrococcus horikoshii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.B9 | PH1527 | locus name | Pyrococcus horikoshii |
| 3.4.11.B9 | PhTET2 | - |
Pyrococcus horikoshii |
| 3.4.11.B9 | tetrahedral aminopeptidase 2 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B9 | 40 | - |
assay at | Pyrococcus horikoshii |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B9 | 80 | - |
1 h, the dimeric enzyme form does not show any sign of structural alteration. The extreme thermal stabilization of the TET particles is not achieved through dodecamerization | Pyrococcus horikoshii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.B9 | 1.5 | - |
Met-Lys-bradykinin | pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 144.5 | - |
Met-Lys-bradykinin | pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 421.5 | - |
L-leucyl 4-nitroanilide | pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 511 | - |
L-leucyl 4-nitroanilide | pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.B9 | 7.5 | - |
assay at | Pyrococcus horikoshii |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.11.B9 | physiological function | dimeric and dodecameric forms may perform different physiological roles | Pyrococcus horikoshii |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.B9 | 0.55 | - |
Met-Lys-bradykinin | pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 76.05 | - |
Met-Lys-bradykinin | pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 383.2 | - |
L-leucyl 4-nitroanilide | pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
| 3.4.11.B9 | 511 | - |
L-leucyl 4-nitroanilide | pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A) | Pyrococcus horikoshii | |
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