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Literature summary for 3.4.14.5 extracted from

  • Heins, J.; Welker, P.; Schönlein, C.; Born, I.; Hartrodt, B.; Neubert, K.; Tsuru, D.; Barth, A.
    Mechanism of proline-specific proteinases: (I) Substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum (1988), Biochim. Biophys. Acta, 954, 161-169.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
additional information proline substrates, Pro in P1, with R configuration in P2 are inhibitors of the hydrolysis of proline substrates with an S,S configuration in an uncompetitive or mixed inhibition type Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km values for X-Pro-4-nitroanilides Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
37.99
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information specificity: specific for the S configuration of the amino-acid residue in P1 and P2 position if the penultimate residue is Pro, derivatives of Gly-Pro-4-nitroanilide where the N-terminal amino group is methylated are hydrolyzed Sus scrofa ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover-numbers for X-Pro-4-nitroanilides Sus scrofa