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Literature summary for 3.4.14.12 extracted from

  • 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 (1999), J. Biol. Chem., 274, 9246-9252.
    View publication on PubMed
Search for more literature for 3.4.14.12

Activating Compound

Activating Compound Comment Organism Structure
iodoacetamide 5 mM, 2fold stimulation Porphyromonas gingivalis

Inhibitors

Inhibitors Comment Organism Structure
3,4-dichloroisocoumarin 1 mM; 44% inhibition Porphyromonas gingivalis
diisopropyl fluorophosphate 10 mM, complete inhibition Porphyromonas gingivalis
Pefabloc SC 80% inhibition at 1 mg/ml and complete inhibition at 10 mg/ml Porphyromonas gingivalis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
 Porphyromonas gingivalis 9986
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Porphyromonas gingivalis 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Porphyromonas gingivalis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Porphyromonas gingivalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Arg-Pro-Ala-D-Lys-amide + H2O
-
 Porphyromonas gingivalis Ala-Arg-Pro + Ala-D-Lys-amide
-
 ?
Ala-Phe-Pro-p-nitroanilide + H2O
-
 Porphyromonas gingivalis Ala-Phe-Pro + p-nitroaniline
-
 ?
Arg-Gly-Pro-Phe-Pro-Ile + H2O
-
 Porphyromonas gingivalis Arg-Gly-Pro + Phe-Pro-Ile
-
 ?
Arg-His-Pro-Lys-Tyr-Lys-Thr-Glu-Leu + H2O
-
 Porphyromonas gingivalis Arg-His-Pro + Lys-Tyr-Lys-Thr-Glu-Leu
-
 ?
Arg-Pro-Pro-Gly-Phe + H2O
-
 Porphyromonas gingivalis Arg-Pro-Pro + Gly-Phe
-
 ?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
-
 Porphyromonas gingivalis Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg
-
 ?
Gly-Pro-p-nitroanilide + H2O no activity Porphyromonas gingivalis Gly-Pro + p-nitroaniline
-
 ?
Gly-Val-Pro-Lys-Thr-His-Leu-Glu-Leu + H2O
-
 Porphyromonas gingivalis 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 Porphyromonas gingivalis ?
-
 ?
interleukin 6 + H2O cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus Porphyromonas gingivalis ?
-
 ?
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 Porphyromonas gingivalis ?
-
 ?
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 Porphyromonas gingivalis ?
-
 ?
Pro-Asn-Pro-Asn-Gln-Gly-Asn-Phe-Ile + H2O
-
 Porphyromonas gingivalis Pro-Asn-Pro + Asn-Gln-Gly-Asn-Phe-Ile
-
 ?
Val-Glu-Pro-Ile-Pro-Tyr + H2O
-
 Porphyromonas gingivalis Val-Glu-Pro + Ile-Pro-Tyr
-
 ?
Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys + H2O
-
 Porphyromonas gingivalis 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
-
 Porphyromonas gingivalis Val-Pro-Pro + Gly-Glu-Asp-Ser-Lys-Glu-Val-Ala-Ala-Pro-His-Arg-Gln
-
 ?

Subunits

Subunits Comment Organism
More two protein bands which represent different forms of the enzyme are detected by SDS-PAGE: 75800 Da and 81800 Da Porphyromonas gingivalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 pH 7.6, 0.2 M HEPES, stable for at least 12 h Porphyromonas gingivalis
37
-
 pH 7.6, 0.2 M HEPES, stable for at least 12 h Porphyromonas gingivalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8
-
 Porphyromonas gingivalis