Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.14.9 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
Search for more literature for 3.4.14.9

Inhibitors

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
 pregnant sow
-

Purification (Commentary)

Purification (Comment) Organism
partial Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
ovary
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

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