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Literature summary for 3.4.21.4 extracted from

  • Guyonnet, V.; Tluscik, F.; Long, P.L.; Polanowski, A.; Travis, J.
    Purification and partial characterization of the pancreatic proteolytic enzymes trypsin, chymotrypsin and elastase from the chicken (1999), J. Chromatogr., 852, 217-225.
    View publication on PubMed
Search for more literature for 3.4.21.4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.197
-
 Nalpha-benzoyl-DL-Arg-p-nitroanilide cationic trypsin 1 Gallus gallus
0.244
-
 Nalpha-benzoyl-DL-Arg-p-nitroanilide cationic trypsin 2 Gallus gallus
0.619
-
 Nalpha-benzoyl-DL-Arg-p-nitroanilide anionic trypsin Gallus gallus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23500
-
 x * 23500, SDS-PAGE Gallus gallus
24500
-
 gel filtration Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification autoactivation of trypsinogen is maximal at pH 7.5 Gallus gallus

Purification (Commentary)

Purification (Comment) Organism
3 enzyme form: anionic trypsin, cationic trypsin 1, cationic trypsin 2 Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha-benzoyl-DL-Arg-p-nitroanilide + H2O
-
 Gallus gallus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 23500, SDS-PAGE Gallus gallus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.355
-
 Nalpha-benzoyl-DL-Arg-p-nitroanilide anionic trypsin Gallus gallus
0.473
-
 Nalpha-benzoyl-DL-Arg-p-nitroanilide cationic trypsin 1 Gallus gallus
1
-
 Nalpha-benzoyl-DL-Arg-p-nitroanilide cationic trypsin 2 Gallus gallus