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Literature summary for 3.4.22.30 extracted from

  • Lopez-Arenas, L.; Solis-Mendiola, S.; Hernandez-Arana, A.
    Estimating the degree of expansion in the transition state for protein unfolding: analysis of the pH dependence of the rate constant for caricain denaturation (1999), Biochemistry, 38, 15936-15943.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide
-
Carica papaya

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Carica papaya

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Carica papaya
-
peptides
-
?

Organism

Organism UniProt Comment Textmining
Carica papaya
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity Carica papaya

Reaction

Reaction Comment Organism Reaction ID
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain mechanism Carica papaya

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein + H2O
-
Carica papaya peptides
-
?

Subunits

Subunits Comment Organism
More transition state structure Carica papaya

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
thermal transition state determination Carica papaya

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
thermal denaturing kinetics, autolysis during denaturation is prevented by irreversible blockage of the active-site thiol with idoacetamide Carica papaya

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
pH profile Carica papaya