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Literature summary extracted from

  • McDonald, J.K.; Hoisington, A.R.; Eisenhauer, D.A.
    Partial purification and characterization of an ovarian tripeptidyl peptidase: a lysosomal exopeptidase that sequentially releases collagen-related (Gly-Pro-X) triplets (1985), Biochem. Biophys. Res. Commun., 126, 63-71.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.14.9 additional information no inhibition: alkali-inactivated diisopropylfluoride, leupeptin; no inhibition by pepstatin; no inhibition: EDTA Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.14.9 0.45
-
 Gly-Pro-Met 2-naphthylamide
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.14.9 lysosome
-
 Sus scrofa 5764
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.14.9 55000
-
 gel filtration in the presence of 3 M urea Sus scrofa
3.4.14.9 250000
-
 enzyme aggregate, gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.14.9 additional information Sus scrofa exopeptidase involved in intracellular (lysosomal) degradation of collagen fibrils ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.14.9 Sus scrofa
-
 pregnant sow
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.14.9 partial Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.14.9 ovary
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.14.9 0.516
-
-
 Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.14.9 Gly-Pro-Ala 4-nitroanilide + H2O at 20% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis Sus scrofa Gly-Pro-Ala + 4-nitroaniline
-
 ?
3.4.14.9 Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O at 10% the rate of Gly-Pro-Met 4-methylcoumarin 7-amide hydrolysis Sus scrofa ?
-
 ?
3.4.14.9 Gly-Pro-Leu 2-naphthylamide + H2O at 30% the rate of Gly-Pro-Met 2-naphthylamide hydrolysis Sus scrofa Gly-Pro-Leu + 2-naphthylamine
-
 ?
3.4.14.9 Gly-Pro-Met 2-naphthylamide + H2O
-
 Sus scrofa Gly-Pro-Met + 2-naphthylamine
-
 ?
3.4.14.9 Gly-Pro-Met 4-nitroanilide + H2O
-
 Sus scrofa Gly-Pro-Met + 4-nitroaniline
-
 ?
3.4.14.9 Gly-Pro-Met-7-amido-4-methylcoumarin + H2O
-
 Sus scrofa Gly-Pro-Met + 7-amino-4-methylcoumarin
-
 ?
3.4.14.9 additional information N-terminal exopeptidase that removes tripeptide units provided the P3 residue is unsubstituted Sus scrofa ?
-
 ?
3.4.14.9 additional information Met-2-naphthylamide, succinyl-Gly-Pro-Met 2-naphthylamide, Pro-Met-7-amido-4-methylcoumarin, Met-7-amido-4-methylcoumarin, methoxysuccinyl-Gly-Pro-Met-7-amido-4-methylcoumarin, benzyloxy-Arg-Arg-7-amido-4-methylcoumarin, Arg-7-amido-4-methylcoumarin, Pro-Ala-4-nitroanilide, Ala 4-nitroanilide, tert-butyloxycarbonyl-Gly-Pro-Ala 4-nitroanilide, benzoyl-Val-Pro-Arg 4-nitroanilide Sus scrofa ?
-
 ?
3.4.14.9 additional information exopeptidase involved in intracellular (lysosomal) degradation of collagen fibrils Sus scrofa ?
-
 ?
3.4.14.9 poly(Gly-Pro-Ala) + H2O
-
 Sus scrofa Gly-Pro-Ala
-
 ?
3.4.14.9 Val-Pro-Arg 4-nitroanilide + H2O at 11% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis Sus scrofa Val-Pro-Arg + 4-nitroaniline
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.14.9 4.3
-
 hydrolysis of Gly-Pro-Met 4-nitroanilide Sus scrofa
3.4.14.9 4.5
-
 hydrolysis of Gly-Pro-Met 2-naphthylamide Sus scrofa
3.4.14.9 5
-
 hydrolysis of Gly-Pro-Met 4-methylcoumarin 7-amide Sus scrofa