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Literature summary for 3.4.11.5 extracted from

  • Nordwig, A.; Mayer, H.
    The cleavage of prolyl peptides by kidney peptidases. Detection of a new peptidase capable of removing N-terminal proline (1973), Hoppe-Seyler's Z. Physiol. Chem., 354, 380-383.
    View publication on PubMed
Search for more literature for 3.4.11.5

Inhibitors

Inhibitors Comment Organism Structure
p-chloromercuribenzoate
-
 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
300000
-
 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 discussion of biological significance ?
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney cortex Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
780
-
 Pro-Leu-NH2 Sus scrofa

Storage Stability

Storage Stability Organism
-20°C or 4°C Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-prolyl-peptide + H2O influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis Sus scrofa L-proline + peptide
-
 ?
additional information discussion of biological significance Sus scrofa ?
-
 ?
poly-(L-Pro) + H2O no hydrolysis Sus scrofa proline
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 9.5
-
 Sus scrofa