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Literature summary for 5.2.1.8 extracted from

  • Fischer, G.; Bang, H.; Mech, C.
    Nachweis einer Enzymkatalyse fur die cis-trans-Isomerisierung der Peptidbindung in prolinhaltigen Peptiden (1984), Biomed. Biochim. Acta, 43, 1101-1111.
    View publication on PubMed

General Stability

General Stability Organism
activity is abolished by incubation with trypsin Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Sus scrofa
Hg2+
-
Sus scrofa
additional information no inhibition: chlorotosylamidophenylbutane, diisopropylphosphorofluoridate Sus scrofa
PCMB
-
Sus scrofa
SDS
-
Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
-
Sus scrofa Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
?
Glutaryl-Ala-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
-
Sus scrofa Glutaryl-Ala-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
?
Glutaryl-Ala-Pro-(cis)-Phe 4-nitroanilide
-
Sus scrofa Glutaryl-Ala-Pro-(trans)-Phe 4-nitroanilide
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
unstable at Sus scrofa