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Literature summary extracted from

  • Kiser, J.Z.; Post, M.; Wang, B.; Miyagi, M.
    Streptomyces erythraeus trypsin for proteomics applications (2009), J. Proteome Res., 8, 1810-1817.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.4.21.4 biotechnology recombinant Streptomyces erythraeus trypsin is fundamental to the use for proteomics applications Saccharopolyspora erythraea

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.4 expressed in Escherichia coli Saccharopolyspora erythraea

General Stability

EC Number General Stability Organism
3.4.21.4 in the so-called autolysis loop and shows no degradation after 96 h of incubation at 37°C Saccharopolyspora erythraea
3.4.21.4 Streptomyces erythraeus trypsin is resistant to autolytic degradation due to the absence of an arginine or lysine residue Saccharopolyspora erythraea

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.4 Soybean trypsin inhibitor
-
 Saccharopolyspora erythraea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.4 0.55
-
 N-alpha-benzoyl-L-Arg-p-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Saccharopolyspora erythraea
3.4.21.4 0.68
-
 N-alpha-benzoyl-L-Lys-4-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Saccharopolyspora erythraea
3.4.21.4 5.7
-
 N-alpha-benzoyl-L-Lys-4-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Sus scrofa
3.4.21.4 7.06
-
 N-alpha-benzoyl-L-Arg-p-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.4 23630
-
 trypsin inhibitor purified mature enzyme, calculated from amino acid sequence Saccharopolyspora erythraea
3.4.21.4 28620
-
 nickel purified His-tag-proenzyme, calculated from amino acid sequence Saccharopolyspora erythraea
3.4.21.4 35000
-
 trypsin inhibitor purified mature enzyme, SDS-PAGE Saccharopolyspora erythraea
3.4.21.4 40000
-
 nickel purified His-tag-proenzyme, SDS-PAGE Saccharopolyspora erythraea

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.4.21.4 guanidine-HCl the recombinant enzyme retains about 40 and 20% activity in 0.1 and 0.3 M guanidine-HCl Sus scrofa
3.4.21.4 guanidine-HCl the recombinant enzyme retains about 40 and 20% activity in 0.1 and 0.3 M guanidine-HCl Saccharopolyspora erythraea
3.4.21.4 urea the recombinant enzyme retains approximately 50 and 20% of its activity in 2 and 4 M urea, respectively Sus scrofa
3.4.21.4 urea the recombinant enzyme retains approximately 80 and 50% of its activity in 2 and 4 M urea, respectively Saccharopolyspora erythraea

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.4 Saccharopolyspora erythraea Q54137 trypsin-like protease; synonym Saccharopolyspora erythraea
-
3.4.21.4 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.4 Ni2+-TED-resin affinity column chromatography and soybean trypsin inhibitor affinity column chromatography Saccharopolyspora erythraea

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.4 pancreas
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.4 N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
-
 Sus scrofa N-alpha-benzoyl-L-Arg + 4-nitroaniline
-
 ?
3.4.21.4 N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
-
 Saccharopolyspora erythraea N-alpha-benzoyl-L-Arg + 4-nitroaniline
-
 ?
3.4.21.4 N-alpha-benzoyl-L-Lys-p-nitroanilide + H2O
-
 Sus scrofa N-alpha-benzoyl-L-Lys + p-nitroaniline
-
 ?
3.4.21.4 N-alpha-benzoyl-L-Lys-p-nitroanilide + H2O Streptomyces erythraeus trypsin has more than 1 order of magnitude greater amidase activity than mammalian trypsin Saccharopolyspora erythraea N-alpha-benzoyl-L-Lys + p-nitroaniline
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.4 0.56
-
 N-alpha-benzoyl-L-Lys-4-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Sus scrofa
3.4.21.4 1.04
-
 N-alpha-benzoyl-L-Lys-4-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Saccharopolyspora erythraea
3.4.21.4 2.46
-
 N-alpha-benzoyl-L-Arg-p-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Sus scrofa
3.4.21.4 5.73
-
 N-alpha-benzoyl-L-Arg-p-nitroanilide recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C Saccharopolyspora erythraea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.4 7.5 9.5
-
 Sus scrofa
3.4.21.4 7.5 9.5
-
 Saccharopolyspora erythraea

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.4 6 10
-
 Saccharopolyspora erythraea
3.4.21.4 6.5 10
-
 Sus scrofa

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.21.4 6
-
 the recombinant enzyme retains 25% of its maximum activity at pH 6.0 Sus scrofa
3.4.21.4 6
-
 the recombinant enzyme retains 44% of its maximum activity at pH 6.0 Saccharopolyspora erythraea