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Ala-Ala-Pro-p-nitroanilide + H2O
Ala-Ala-Pro + p-nitroaniline
-
-
-
?
Ala-Arg-Pro-Ala-D-Lys-amide + H2O
Ala-Arg-Pro + Ala-D-Lys-amide
-
-
-
-
?
Ala-Phe-Pro-2-naphthylamide + H2O
Ala-Phe-Pro + 2-naphthylamine
-
-
-
?
Ala-Phe-Pro-beta-naphthylamide + H2O
Ala-Phe-Pro + beta-naphthylamine
-
-
-
?
Ala-Phe-Pro-p-nitroanilide + H2O
Ala-Phe-Pro + p-nitroaniline
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
-
13% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
Arg-Gly-Pro-Phe-Pro-Ile + H2O
Arg-Gly-Pro + Phe-Pro-Ile
-
-
-
-
?
Arg-His-Pro-Lys-Tyr-Lys-Thr-Glu-Leu + H2O
Arg-His-Pro + Lys-Tyr-Lys-Thr-Glu-Leu
-
-
-
-
?
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
-
22% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
Arg-Pro-Pro + Gly-Phe
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg
-
-
-
-
?
Gly-Ala-Pro-2-naphthylamide + H2O
Gly-Ala-Pro + 2-naphthylamine
-
-
-
?
Gly-Ala-Pro-beta-naphthylamide + H2O
Gly-Ala-Pro + beta-naphthylamine
-
-
-
?
Gly-L-Ala-Gly-L-Pro-beta-naphthylamide + H2O
Gly-L-Ala-Gly-L-Pro + beta-naphthylamine
-
-
-
-
?
Gly-L-Ala-L-Pro-4-nitroanilide + H2O
Gly-L-Ala-L-Pro + 4-nitroaniline
-
32% of the activity with L-Ala-L-Ala-L-Pro-4-nitroanilide
-
-
?
Gly-L-Ala-L-Pro-beta-naphthylamide + H2O
Gly-L-Ala-L-Pro + beta-naphthylamine
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
Gly-Val-Pro-Lys-Thr-His-Leu-Glu-Leu + H2O
Gly-Val-Pro + Lys-Thr-His-Leu-Glu-Leu
-
-
-
-
?
Human cystatin C + H2O
?
-
cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus
-
-
?
interleukin 6 + H2O
?
-
cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus
-
-
?
L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Ala-L-Phe-L-Pro-4-nitroanilide + H2O
L-Ala-L-Phe-L-Pro + 4-nitroaniline
-
24% of the activity with L-Ala-L-Ala-L-Pro-4-nitroanilide
-
-
?
L-Asp-L-Ala-L-Pro-4-nitroanilide + H2O
L-Asp-L-Ala-L-Pro + 4-nitroaniline
-
-
-
?
L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O
L-Pro-L-Pro-L-Pro + 4-nitroaniline
-
26% of the activity with L-Ala-L-Ala-L-Pro-4-nitroanilide
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
-
24% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
Phe-Pro-p-nitroanilide + H2O
Phe-Pro + p-nitroaniline
-
13% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
Pro-Asn-Pro-Asn-Gln-Gly-Asn-Phe-Ile + H2O
Pro-Asn-Pro + Asn-Gln-Gly-Asn-Phe-Ile
-
-
-
-
?
Ser-Pro-p-nitroanilide + H2O
Ser-Pro + p-nitroaniline
-
13% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
Val-Glu-Pro-Ile-Pro-Tyr + H2O
Val-Glu-Pro + Ile-Pro-Tyr
-
-
-
-
?
Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys + H2O
Val-Pro-Pro + Gly-Glu-Asp-Ser-Lys
-
-
-
-
?
Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys-Glu-Val-Ala-Ala-Pro-His-Arg-Gln + H2O
Val-Pro-Pro + Gly-Glu-Asp-Ser-Lys-Glu-Val-Ala-Ala-Pro-His-Arg-Gln
-
-
-
-
?
Z-Gly-Ala-Pro-2-naphthylamide + H2O
Z-Gly-Ala-Pro + 2-naphthylamine
-
-
-
?
additional information
?
-
Ala-Phe-Pro-p-nitroanilide + H2O
Ala-Phe-Pro + p-nitroaniline
-
-
-
?
Ala-Phe-Pro-p-nitroanilide + H2O
Ala-Phe-Pro + p-nitroaniline
-
66% of the activity with Ala-Ala-Pro-p-nitroanilide
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
no activity
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
3% of the activity with Ala-Ala-Pro-p-nitroanilide
-
-
?
additional information
?
-
-
the enzyme possesses the absolute requirement for the proline residue in the P1 position. A free alpha-amino group is absolutely required for cleavage after the third proline residue. No cleavage of: benzyloxycarbonyl-Gly-Pro-p-nitroanilide, benzyloxycarbonyl-Ala-Pro-p-nitroanilide, Pro-p-nitroanilide, Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, Tyr-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, Arg-Pro-Hyp-Gly-Phe-Ser-Pro-Phe-Arg, Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-leu-Met-NH2, acetyl-Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys
-
-
?
additional information
?
-
-
the production of prolyl tripeptidyl peptidase may contribute to the pathogenesis of periodontal tissue destruction though the mutual interaction of this enzyme, host and bacterial collagenases, and dipeptidyl peptidases in the degradation of collagen during the course of infection
-
-
?
additional information
?
-
no activity with Pro-2-naphthylamide, Gly-Pro-2-naphthylamide, Z-Gly-Pro-2-naphthylamide, Z-Gly-Ala-Pro-2-naphthylamide, Z-Ala-Gly-Pro-2-naphthylamide, Gly-Ala-Gly-Pro-2-naphthylamide, Z-Gly-Ala-Gly-Pro-2-naphthylamide, and Ala-Gly-Ala-Gly-Pro-2-naphthylamide
-
-
?
additional information
?
-
-
the enzyme releases a tripeptide, X-X-P, from substrates exposing of a free N-terminus and a proline residue in the third position
-
-
?
additional information
?
-
the enzyme releases a tripeptide, X-X-P, from substrates exposing of a free N-terminus and a proline residue in the third position
-
-
?
additional information
?
-
-
the cleavage of a meprin beta (EC 3.4.24.63) substrate leads to generation of the PtP substrate, and the activity of PtP results in release of a chromophore or fluorophore, coupled assay method evaluation, overview
-
-
?
additional information
?
-
the cleavage of a meprin beta (EC 3.4.24.63) substrate leads to generation of the PtP substrate, and the activity of PtP results in release of a chromophore or fluorophore, coupled assay method evaluation, overview
-
-
?
additional information
?
-
-
no activity with Ala-Phe-p-nitroanilide, Ala-Ala-p-nitroanilide, Ala-p-nitroanilide, Pro-p-nitroanilide, benzoyl-Arg-p-nitroanilide, succinyl-Ala-Ala-Ala-p-nitroanilide, succinyl-Ala-Ala-Pro-p-nitroanilide, tosyl-Gly-Pro-Lys-4-nitroanilide
-
-
?
additional information
?
-
-
enzyme exhibits tripeptidyl peptidase and tetrapeptidyl peptidase activity, but no other exo- or endo-activites
-
-
?
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0.069
Ala-Ala-Pro-p-nitroanilide
-
pH 7.5, 37°C
0.17 - 0.85
Ala-Phe-Pro-beta-naphthylamide
0.129
Ala-Phe-Pro-p-nitroanilide
-
pH 7.5, 37°C
0.114
Arg-Pro-p-nitroanilide
-
pH 7.5, 37°C
0.17 - 0.85
Gly-Ala-Pro-2-naphthylamide
0.38 - 0.42
Gly-Ala-Pro-beta-naphthylamide
0.26
Gly-L-Ala-Gly-L-Pro-beta-naphthylamide
-
pH 6.5, 30°C
0.072
Gly-L-Ala-L-Pro-beta-naphthylamide
-
pH 6.5, 30°C
0.084
Lys-Pro-p-nitroanilide
-
pH 7.5, 37°C
additional information
additional information
-
0.17
Ala-Phe-Pro-beta-naphthylamide
E636A mutant
0.85
Ala-Phe-Pro-beta-naphthylamide
E636A mutant
0.17
Gly-Ala-Pro-2-naphthylamide
wild type enzyme, in 20 mM Tris-HCl (pH 7.0), at 37°C
0.38
Gly-Ala-Pro-2-naphthylamide
mutant enzyme E636A, in 20 mM Tris-HCl (pH 7.0), at 37°C
0.42
Gly-Ala-Pro-2-naphthylamide
in 20 mM Tris-HCl buffer (pH 7.0), at 37°C
0.42
Gly-Ala-Pro-2-naphthylamide
wild type enzyme, in 20 mM Tris-HCl (pH 7.0), at 37°C
0.85
Gly-Ala-Pro-2-naphthylamide
mutant enzyme E636A, in 20 mM Tris-HCl (pH 7.0), at 37°C
0.38
Gly-Ala-Pro-beta-naphthylamide
prolyl tripeptidyl aminopeptidase with an N-terminal truncation of 38 residues
0.42
Gly-Ala-Pro-beta-naphthylamide
-
0.42
Gly-Ala-Pro-beta-naphthylamide
prolyl tripeptidyl aminopeptidase with an N-terminal truncation of 38 residues
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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6.8 - 511
Ala-Phe-Pro-beta-naphthylamide
2.65 - 511
Gly-Ala-Pro-2-naphthylamide
2.65 - 354
Gly-Ala-Pro-beta-naphthylamide
43
Gly-L-Ala-Gly-L-Pro-beta-naphthylamide
-
pH 6.5, 30°C
115
Gly-L-Ala-L-Pro-beta-naphthylamide
-
pH 6.5, 30°C
6.8
Ala-Phe-Pro-beta-naphthylamide
E636A mutant
511
Ala-Phe-Pro-beta-naphthylamide
E636A mutant
2.65
Gly-Ala-Pro-2-naphthylamide
mutant enzyme E636A, in 20 mM Tris-HCl (pH 7.0), at 37°C
6.8
Gly-Ala-Pro-2-naphthylamide
mutant enzyme E636A, in 20 mM Tris-HCl (pH 7.0), at 37°C
354
Gly-Ala-Pro-2-naphthylamide
in 20 mM Tris-HCl buffer (pH 7.0), at 37°C
354
Gly-Ala-Pro-2-naphthylamide
wild type enzyme, in 20 mM Tris-HCl (pH 7.0), at 37°C
511
Gly-Ala-Pro-2-naphthylamide
wild type enzyme, in 20 mM Tris-HCl (pH 7.0), at 37°C
2.65
Gly-Ala-Pro-beta-naphthylamide
prolyl tripeptidyl aminopeptidase with an N-terminal truncation of 38 residues
354
Gly-Ala-Pro-beta-naphthylamide
-
354
Gly-Ala-Pro-beta-naphthylamide
prolyl tripeptidyl aminopeptidase with an N-terminal truncation of 38 residues
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Fujimura, S.; Ueda, O.; Shibata, Y.; Hirai, K.
Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens
FEMS Microbiol. Lett.
219
305-309
2003
Prevotella nigrescens
brenda
Banbula, A.; Mak, P.; Bugno, M.; Silberring, J.; Dubin, A.; Nelson, D.; Travis, J.; Potempa, J.
Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of peridontitis
J. Biol. Chem.
274
9246-9252
1999
Porphyromonas gingivalis
brenda
Nakajima, Y.; Ito, K.; Xu, Y.; Yamada, N.; Onohara, Y.; Ito, T.; Yoshimoto, T.
Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis
Acta Crystallogr. Sect. F
F61
1046-1048
2005
Porphyromonas gingivalis
brenda
Umezawa, Y.; Yokoyama, K.; Kikuchi, Y.; Date, M.; Ito, K.; Yoshimoto, T.; Matsui, H.
Novel prolyl tri/tetra-peptidyl aminopeptidase from Streptomyces mobaraensis: substrate specificity and enzyme gene cloning
J. Biochem.
136
293-300
2004
Streptomyces mobaraensis
brenda
Ito, K.; Nakajima, Y.; Xu, Y.; Yamada, N.; Onohara, Y.; Ito, T.; Matsubara, F.; Kabashima, T.; Nakayama, K.; Yoshimoto, T.
Crystal structure and mechanism of tripeptidyl activity of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis
J. Mol. Biol.
362
228-240
2006
Porphyromonas gingivalis (Q7MUW6)
brenda
Xu, Y.; Nakajima, Y.; Ito, K.; Zheng, H.; Oyama, H.; Heiser, U.; Hoffmann, T.; Gaertner, U.T.; Demuth, H.U.; Yoshimoto, T.
Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism
J. Mol. Biol.
375
708-719
2008
Porphyromonas gingivalis (Q7MUW6)
brenda
Schulze, A.; Wermann, M.; Demuth, H.U.; Yoshimoto, T.; Ramsbeck, D.; Schlenzig, D.; Schilling, S.
Continuous assays for meprin alpha and beta using prolyl tripeptidyl aminopeptidase (PtP) from Porphyromonas gingivalis
Anal. Biochem.
559
11-16
2018
Porphyromonas gingivalis, Porphyromonas gingivalis (Q7MUW6)
brenda