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Enzyme Nomenclature
Information on EC 3.4.11.B9 - TET2 peptidase
for references in articles please use BRENDA:EC3.4.11.B9preliminary BRENDA-supplied EC number
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EC Tree
3.4.11.B9 TET2 peptidaseSpecify your search results
The expected taxonomic range for this enzyme is: Pyrococcus horikoshii
Reaction Schemes
The enzyme functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids.
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FrvX
PH1527
PhTET2
tetrahedral aminopeptidase 2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The enzyme functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids.
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ala-Ala-Ala 4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
1.3% of the activity with Leu-4-nitroanilide
-
-
?
Asn-7-amido-4-methylcoumarin + H2O
Asn + 7-amino-4-methylcoumarin
0.3% of the activity with Leu-4-nitroanilide
-
-
?
glycyl 4-nitroanilide + H2O
glycine + 4-nitroaniline
0.3% of the activity with Leu-4-nitroanilide
-
-
?
L-glutamyl 4-nitroanilide + H2O
L-glutamine + 4-nitroaniline
-
-
-
?
L-isoleucyl 4-nitroanilide + H2O
L-isoleucine + 4-nitroaniline
10.8% of the activity with Leu-4-nitroanilide
-
-
?
L-phenylalanyl 4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
0.8% of the activity with Leu-4-nitroanilide
-
-
?
Orn-7-amido-4-methylcoumarin + H2O
Orn + 7-amino-4-methylcoumarin
0.1% of the activity with Leu-4-nitroanilide
-
-
?
Thr-7-amido-4-methylcoumarin + H2O
Thr + 7-amino-4-methylcoumarin
6.1% of the activity with Leu-4-nitroanilide
-
-
?
Val-7-amido-4-methylcoumarin + H2O
Val + 7-amino-4-methylcoumarin
2.1% of the activity with Leu-4-nitroanilide
-
-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
2.9% of the activity with Leu-4-nitroanilide
-
-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
2.9% of the activity with Leu-4-nitroanilide
-
-
?
Ala-Ala-Phe 4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe 4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
1.2% of the activity with Leu-4-nitroanilide
-
-
?
Gln-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
2.8% of the activity with Leu-4-nitroanilide
-
-
?
Gln-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
2.8% of the activity with Leu-4-nitroanilide
-
-
?
L-alanyl 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
?
L-alanyl 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
14.3% of the activity with Leu-4-nitroanilide
-
-
?
L-alanyl 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
?
L-arginyl 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
-
-
-
?
L-arginyl 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
0.1% of the activity with Leu-4-nitroanilide
-
-
?
L-arginyl 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
-
-
-
?
L-leucyl 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucyl 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-lysyl 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
0.2% of the activity with Leu-4-nitroanilide
-
-
?
L-lysyl 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
-
-
?
L-methionyl 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
-
-
?
L-methionyl 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
26.3% of the activity with Leu-4-nitroanilide
-
-
?
L-methionyl 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
-
-
?
L-prolyl 4-nitroanilide + H2O
L-proline + 4-nitroaniline
-
-
-
?
L-prolyl 4-nitroanilide + H2O
L-proline + 4-nitroaniline
0.9% of the activity with Leu-4-nitroanilide
-
-
?
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
-
-
?
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
-
-
?
Ser-7-amido-4-methylcoumarin + H2O
Ser + 7-amino-4-methylcoumarin
12.8% of the activity with Leu-4-nitroanilide
-
-
?
Ser-7-amido-4-methylcoumarin + H2O
Ser + 7-amino-4-methylcoumarin
12.8% of the activity with Leu-4-nitroanilide
-
-
?
Tyr-7-amido-4-methylcoumarin + H2O
Tyr + 7-amino-4-methylcoumarin
0.9% of the activity with Leu-4-nitroanilide
-
-
?
Tyr-7-amido-4-methylcoumarin + H2O
Tyr + 7-amino-4-methylcoumarin
0.9% of the activity with Leu-4-nitroanilide
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
when assayed with short chromogenic peptides, PhTET2 is active as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. The enzyme can cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. The hydrolytic mechanism is found to be nonprocessive. The enzyme has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity
-
-
?
additional information
?
-
when assayed with short chromogenic peptides, PhTET2 is active as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. The enzyme can cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. The hydrolytic mechanism is found to be nonprocessive. The enzyme has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme is insensitive to the papain and trypsin inhibitor antipain, to the chymotrypsin inhibitor chymostatin, to the cysteine protease inhibitor E-64, to the serine and cysteine protease inhibitor leupeptin, to the aspartate protease inhibitor pepstatin, and to the serine protease inhibitors Pefabloc SC and aprotinin. Puromycin, an inhibitor of some exopeptidases, has no effect on the activity of PhTET2
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
L-leucyl 4-nitroanilide
pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A)
1.1
L-leucyl 4-nitroanilide
pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A)
1.5
Met-Lys-bradykinin
pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A)
1.9
Met-Lys-bradykinin
pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
421.5
L-leucyl 4-nitroanilide
pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A)
511
L-leucyl 4-nitroanilide
pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A)
1.5
Met-Lys-bradykinin
pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A)
144.5
Met-Lys-bradykinin
pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
383.2
L-leucyl 4-nitroanilide
pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A)
511
L-leucyl 4-nitroanilide
pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A)
0.55
Met-Lys-bradykinin
pH 7.5, 40°C, mutant dimer (R217S/R220S/F224S/H248S/I292A)
76.05
Met-Lys-bradykinin
pH 7.5, 40°C, mutant dodecamer (R217S/R220S/F224S/H248S/I292A)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
substrate: Leu-4-nitroanilide, PIPES buffer, strong activity was still detectable at pH 6 and 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
at temperatures lower than 70 °C, less than 10% of the maximum activity was detected
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme sequentially degrades peptides produced by the proteasome to single amino acids
metabolism
-
the enzyme sequentially degrades peptides produced by the proteasome to single amino acids
-
physiological function
dimeric and dodecameric forms may perform different physiological roles
physiological function
-
dimeric and dodecameric forms may perform different physiological roles
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TET_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
353
0
39014
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
475000
tetrahedral dodecameric complex, sedimentation velocity experiments
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
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
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
-
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
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
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of TET from the thermophilic archaeon Pyrococcus horikoshii at 1.6 A resolution in native form and in complex with the inhibitor amastatin
hexagonal crystals of FrvX are obtained after 2 days by the sitting drop vapor diffusion method. The monomer has a typical clan MH fold. The quaternary structure is built by dimers with a length of 100 A that form the edges of the tetrahedron. All 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by pores with a maximal diameter of 10 A, allowing only small peptides and unfolded proteins access to the active site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R217S/R220S/F224S/H248S/I292A
R217S/R220S/F224S/H248S/I292A
the mutant is A model to study the oligomerization process
R217S/R220S/F224S/H248S/I292A
-
the mutant is A model to study the oligomerization process
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the gene encoding FrvX is amplified by PCR from genomic DNA and cloned into a pET-28a vector introducing a N-terminal His6 tag. The protein is expressed in Escherichia coli Rosetta TM (DE3) cells
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dura, M.A.; Receveur-Brechot, V.; Andrieu, J.P.; Ebel, C.; Schoehn, G.; Roussel, A.; Franzetti, B.
Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii
Biochemistry
44
3477-3486
2005
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii OT-3 (O59196)
brenda
Russo, S.; Baumann, U.
Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase
J. Biol. Chem.
279
51275-51281
2004
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii OT-3 (O59196)
brenda
Appolaire, A.; Rosenbaum, E.; Dura, M.; Colombo, M.; Marty, V.; Savoye, M.; Godfroy, A.; Schoehn, G.; Girard, E.; Gabel, F.; Franzetti, B.
Pyrococcus horikoshii TET2 peptidase assembling process and associated functional regulation
J. Biol. Chem.
288
22542-22554
2013
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O59196)
brenda
Borissenko, L.; Groll, M.
Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes
J. Mol. Biol.
346
1207-1219
2005
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii OT-3 (O59196)
brenda
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