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Literature summary for 3.4.21.5 extracted from

  • Wu, G.; Deng, X.; Li, X.; Wang, X.; Wang, S.; Xu, H.
    Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli (2011), Appl. Microbiol. Biotechnol., 92, 85-93.
    View publication on PubMed
Search for more literature for 3.4.21.5

Protein Variants

Protein Variants Comment Organism
additional information immobilization of thrombin, determination of optimal conditions, overview. Application of immobilized thrombin for production of S-thanatin, small antimicrobial peptide with 21 amino acid residue, expressed in Escherichia coli strain BL21(DE3) as a fusion protein containing thrombin cleavage site. The immobilizes thrombin in polyacrylamide gel shows excellent cleavage performance within wider ranges of pH value and temperature for reaction than free enzyme, and the residual activity remain above 75% after ten times of usage Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bos taurus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Bos taurus
-
plasma
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Phe-Pip-Arg-4-nitroanilide + H2O i.e. S-2238 Bos taurus D-Phe-Pip-Arg + 4-nitroaniline
-
 ?
S-thanatin + H2O
-
 Bos taurus ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bos taurus