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Literature summary for 3.4.14.5 extracted from

  • Gonschor, H.; Schäfer, W.
    Dipeptidyl peptidase IV. Purification for use in peptide sequencing (1985), Biol. Chem. Hoppe-Seyler, 366, 157-165.
    View publication on PubMed
Search for more literature for 3.4.14.5

Application

Application Comment Organism
analysis the enzyme can be used for peptide sequence analysis Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
 2 * 130000, SDS-PAGE Sus scrofa
240000
-
 gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein Sus scrofa
side-chain modification contains about 18% carbohydrate Sus scrofa

Purification (Commentary)

Purification (Comment) Organism
-
 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
additional information
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-Pro-2-naphthylamide + H2O
-
 Sus scrofa Gly-Pro + 2-naphthylamine
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 130000, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35 45
-
 Sus scrofa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 reversible denaturation below Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8 9
-
 Sus scrofa

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.5 11 reversible denaturation in the range Sus scrofa