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Literature summary for 3.4.21.4 extracted from

  • Klomklao, S.; Kishimura, H.; Benjakul, S.
    Trypsin from the pyloric ceca of pectoral rattail (Coryphaenoides pectoralis): purification and characterization (2009), J. Agric. Food Chem., 57, 7097-7103.
    View publication on PubMed

General Stability

General Stability Organism
Ca2+ stabilizes the purified enzyme Albatrossia pectoralis

Inhibitors

Inhibitors Comment Organism Structure
EDTA 10% inhibition at 2 mM Albatrossia pectoralis
additional information no inhibition by E-64, N-ethylmaleimide, iodoacetic acid, pepstatin A, and Nalpha-4-tosyl-L-Phe-chloromethylketone Albatrossia pectoralis
NaCl enzyme activity continuously decreases with increasing NaCl concentration of 0-30% Albatrossia pectoralis
Nalpha-tosyl-L-Lys-chloromethyl ketone 91% inhibition at 1 mM Albatrossia pectoralis
Soybean trypsin inhibitor complete inhibition at 1 mg/ml Albatrossia pectoralis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
Nalpha-4-tosyl-L-arginine methyl ester pH 8.5, 45°C Albatrossia pectoralis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ stabilizes the purified enzyme Albatrossia pectoralis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
gel filtration Albatrossia pectoralis

Organism

Organism UniProt Comment Textmining
Albatrossia pectoralis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 89fold from pyloric ceca by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, and again gel filtration Albatrossia pectoralis

Source Tissue

Source Tissue Comment Organism Textmining
cecum
-
Albatrossia pectoralis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.9
-
purified enzyme, pH 8.5, 45°C Albatrossia pectoralis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha-4-tosyl-L-arginine methyl ester + H2O
-
Albatrossia pectoralis Nalpha-4-tosyl-L-arginine + methanol
-
?

Subunits

Subunits Comment Organism
monomer 1 * 24000, SDS-PAGE Albatrossia pectoralis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Albatrossia pectoralis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 60 activity range, 20-25% of maximal activity at 20°C and 60°C, profile, overview Albatrossia pectoralis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
purified enzyme, unstable above, 50% remaining activity at 60°C, inactivation at 80°C Albatrossia pectoralis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
210
-
Nalpha-4-tosyl-L-arginine methyl ester pH 8.5, 45°C Albatrossia pectoralis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Albatrossia pectoralis

pH Range

pH Minimum pH Maximum Comment Organism
5 10 activity range, 20% of maximal activity at pH 5.0 and pH 10.0, profile, overview Albatrossia pectoralis

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 11 purified enzyme, stable, unstable below Albatrossia pectoralis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1400
-
Nalpha-4-tosyl-L-arginine methyl ester pH 8.5, 45°C Albatrossia pectoralis