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Literature summary extracted from

  • Dura, M.A.; Rosenbaum, E.; Larabi, A.; Gabel, F.; Vellieux, F.M.; Franzetti, B.
    The structural and biochemical characterizations of a novel TET peptidase complex from Pyrococcus horikoshii reveal an integrated peptide degradation system in hyperthermophilic Archaea (2009), Mol. Microbiol., 72, 26-40.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.15 the 12-subunit PhTET3 complex is crystallized and its 3D structure is solved at a resolution of 1.9 A by molecular replacement Pyrococcus horikoshii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.15 amastatin 0.002 mM, 77% inhibition Pyrococcus horikoshii
3.4.11.15 bestatin 0.5 mM, 34% inhibition Pyrococcus horikoshii
3.4.11.15 Ca2+ 1 mM,% inhibition Pyrococcus horikoshii
3.4.11.15 Cd2+ 1 mM,% inhibition Pyrococcus horikoshii
3.4.11.15 CHAPS buffer
-
 Pyrococcus horikoshii
3.4.11.15 chymostatin 1 mM, 22% inhibition Pyrococcus horikoshii
3.4.11.15 Cu2+ 1 mM,% inhibition Pyrococcus horikoshii
3.4.11.15 EDTA 0.02 mM, 85% inhibition Pyrococcus horikoshii
3.4.11.15 Mg2+ 1 mM,% inhibition Pyrococcus horikoshii
3.4.11.15 Mn2+ 1 mM,% inhibition Pyrococcus horikoshii
3.4.11.15 additional information the enzyme is insensitive to the papain and trypsin inhibitor antipain, to the cysteine proteases inhibitor E-64, to the serine and cysteine proteases inhibitor leupeptin, to the aspartate proteases inhibitor pepstatin, and to the metalloendopeptidases inhibitor phosphoramidon. Puromycin, an inhibitor of some exopeptidases, has practically no effect on the activity of PhTET3 Pyrococcus horikoshii
3.4.11.15 pefabloc 5 mM, 20% inhibition Pyrococcus horikoshii
3.4.11.15 Zn2+ 1 mM,% inhibition Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.15 Co2+ 1 mM, 2.4fold activation Pyrococcus horikoshii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.15 40000
-
 12 * 40000, SDS-PAGE, the active sites of the PhTET complexes are located inside the particles, in the catalytic chambers that are enclosed by the tetrahedron apices. The walls of these chambers are positively charged, and each one contains three active sites arranged in a circular way. Adjacent to the active sites, the specificity pockets appear as small cavities. The geometry of these pockets is different in each PhTET complex, as well as their location in the particles relative to the active sites. In PhTET3, the specificity pocket is formed by the side-chains of D262, T240, T295 and T297, which leads to a negative charge Pyrococcus horikoshii
3.4.11.15 500000
-
 dodecameric complex, gel filtration Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.15 Pyrococcus horikoshii O59485
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.15 L-alanyl-L-alanine 4-nitroanilide + H2O L-alanine 4-nitroanilide accumulates very fast in the reaction mixture, and the L-alanine 4-nitroanilide/4-nitroaniline ratio diminishes from 123 at 5 min to 69 at 25 min, therefore indicating that the enzyme is mostly cleaving the substrate to L-alanine 4-nitroanilide, and then also this last product to give 4-nitroaniline Pyrococcus horikoshii L-alanine + L-alanine 4-nitroanilide
-
 ?
3.4.11.15 L-alanyl-L-alanyl-L-alanine 4-nitroanilide + H2O L-alanyl-L-alanine 4-nitroanilide is produced, but also consumed by the enzyme while 4-nitroaniline is generated after a lag phase. At 26 min the ratios L-alanyl-L-alanine 4-nitroaniline/4-nitroaniline and L-alanyl 4-nitroanilide/4-nitroaniline are 8 and 33 respectively Pyrococcus horikoshii L-alanine + L-alanyl-L-alanine 4-nitroanilide
-
 ?
3.4.11.15 L-arginine 4-nitroanilide + H2O 66.6% of the activity compared to L-lysine 4-nitroanilide Pyrococcus horikoshii L-arginine + 4-nitroaniline
-
 ?
3.4.11.15 L-glutamate 4-nitroanilide + H2O 20.1% of the activity compared to L-lysine 4-nitroanilide Pyrococcus horikoshii L-glutamate + 4-nitroaniline
-
 ?
3.4.11.15 L-leucine 4-nitroanilide + H2O 11.4% of the activity compared to L-lysine 4-nitroanilide Pyrococcus horikoshii L-leucine + 4-nitroaniline
-
 ?
3.4.11.15 L-lysine 4-nitroanilide + H2O
-
 Pyrococcus horikoshii L-lysine + 4-nitroaniline
-
 ?
3.4.11.15 additional information poor activity is detected against L-ornithinyl- and L-glutaminyl-7-amido-4-methylcoumarin, and L-aspartyl-, L-methionyl- and L-alanyl 4-nitroanilide, while the enzyme shows very poor or no activity against the other aminoacyl-4-nitroanilides or aminoacyl-7-amido-4-methylcoumarines assayed. No activity can be measured against any of the N-terminal blocked derivatives Pyrococcus horikoshii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.15 dodecamer 12 * 40000, SDS-PAGE, the active sites of the PhTET complexes are located inside the particles, in the catalytic chambers that are enclosed by the tetrahedron apices. The walls of these chambers are positively charged, and each one contains three active sites arranged in a circular way. Adjacent to the active sites, the specificity pockets appear as small cavities. The geometry of these pockets is different in each PhTET complex, as well as their location in the particles relative to the active sites. In PhTET3, the specificity pocket is formed by the side-chains of D262, T240, T295 and T297, which leads to a negative charge Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
3.4.11.15 PH1821
-
 Pyrococcus horikoshii
3.4.11.15 PhTET3
-
 Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.11.15 80
-
 half-life: 17.83 min Pyrococcus horikoshii
3.4.11.15 90
-
 half-life: 3.44 min Pyrococcus horikoshii
3.4.11.15 95
-
 half-life: 55.1 min Pyrococcus horikoshii
3.4.11.15 100
-
 half-life: 27 min Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.15 7.4
-
-
 Pyrococcus horikoshii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.11.15 6 8.5 pH 6: about 50% of maximal activity, pH 8.0: about 90% of maximal activity Pyrococcus horikoshii