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Literature summary for 3.4.21.4 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
Search for more literature for 3.4.21.4

Application

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

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Saccharopolyspora erythraea

General Stability

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

Inhibitors

Inhibitors Comment Organism Structure
Soybean trypsin inhibitor
-
 Saccharopolyspora erythraea

KM Value [mM]

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

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

Organic Solvent Stability

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

Organism

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

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
-
 Sus scrofa N-alpha-benzoyl-L-Arg + 4-nitroaniline
-
 ?
N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
-
 Saccharopolyspora erythraea N-alpha-benzoyl-L-Arg + 4-nitroaniline
-
 ?
N-alpha-benzoyl-L-Lys-p-nitroanilide + H2O
-
 Sus scrofa N-alpha-benzoyl-L-Lys + p-nitroaniline
-
 ?
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]

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

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

pH Range

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

pH Stability

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