EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.14.12 | iodoacetamide | 5 mM, 2fold stimulation | Porphyromonas gingivalis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.14.12 | 3,4-dichloroisocoumarin | 1 mM; 44% inhibition | Porphyromonas gingivalis | |
3.4.14.12 | diisopropyl fluorophosphate | 10 mM, complete inhibition | Porphyromonas gingivalis | |
3.4.14.12 | Pefabloc SC | 80% inhibition at 1 mg/ml and complete inhibition at 10 mg/ml | Porphyromonas gingivalis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.14.12 | cell surface | - |
Porphyromonas gingivalis | 9986 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.14.12 | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.14.12 | Porphyromonas gingivalis | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.14.12 | - |
Porphyromonas gingivalis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.4.14.12 | additional information | - |
- |
Porphyromonas gingivalis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.14.12 | Ala-Arg-Pro-Ala-D-Lys-amide + H2O | - |
Porphyromonas gingivalis | Ala-Arg-Pro + Ala-D-Lys-amide | - |
? | |
3.4.14.12 | Ala-Phe-Pro-p-nitroanilide + H2O | - |
Porphyromonas gingivalis | Ala-Phe-Pro + p-nitroaniline | - |
? | |
3.4.14.12 | Arg-Gly-Pro-Phe-Pro-Ile + H2O | - |
Porphyromonas gingivalis | Arg-Gly-Pro + Phe-Pro-Ile | - |
? | |
3.4.14.12 | Arg-His-Pro-Lys-Tyr-Lys-Thr-Glu-Leu + H2O | - |
Porphyromonas gingivalis | Arg-His-Pro + Lys-Tyr-Lys-Thr-Glu-Leu | - |
? | |
3.4.14.12 | Arg-Pro-Pro-Gly-Phe + H2O | - |
Porphyromonas gingivalis | Arg-Pro-Pro + Gly-Phe | - |
? | |
3.4.14.12 | Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O | - |
Porphyromonas gingivalis | Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg | - |
? | |
3.4.14.12 | Gly-Pro-p-nitroanilide + H2O | no activity | Porphyromonas gingivalis | Gly-Pro + p-nitroaniline | - |
? | |
3.4.14.12 | Gly-Val-Pro-Lys-Thr-His-Leu-Glu-Leu + H2O | - |
Porphyromonas gingivalis | Gly-Val-Pro + Lys-Thr-His-Leu-Glu-Leu | - |
? | |
3.4.14.12 | Human cystatin C + H2O | cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus | Porphyromonas gingivalis | ? | - |
? | |
3.4.14.12 | interleukin 6 + H2O | cleavage of a tripeptide, NH2-Xaa-Xaa-Pro, from the amino terminus | Porphyromonas gingivalis | ? | - |
? | |
3.4.14.12 | 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 | ? | - |
? | |
3.4.14.12 | 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 | ? | - |
? | |
3.4.14.12 | Pro-Asn-Pro-Asn-Gln-Gly-Asn-Phe-Ile + H2O | - |
Porphyromonas gingivalis | Pro-Asn-Pro + Asn-Gln-Gly-Asn-Phe-Ile | - |
? | |
3.4.14.12 | Val-Glu-Pro-Ile-Pro-Tyr + H2O | - |
Porphyromonas gingivalis | Val-Glu-Pro + Ile-Pro-Tyr | - |
? | |
3.4.14.12 | Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys + H2O | - |
Porphyromonas gingivalis | Val-Pro-Pro + Gly-Glu-Asp-Ser-Lys | - |
? | |
3.4.14.12 | 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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.14.12 | More | two protein bands which represent different forms of the enzyme are detected by SDS-PAGE: 75800 Da and 81800 Da | Porphyromonas gingivalis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.14.12 | 25 | - |
pH 7.6, 0.2 M HEPES, stable for at least 12 h | Porphyromonas gingivalis |
3.4.14.12 | 37 | - |
pH 7.6, 0.2 M HEPES, stable for at least 12 h | Porphyromonas gingivalis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.14.12 | 6 | 8 | - |
Porphyromonas gingivalis |