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Literature summary for 3.4.21.4 extracted from

  • Prasad, E.R.; Dutta-Gupta, A.; Padmasree, K.
    Purification and characterization of a Bowman-Birk proteinase inhibitor from the seeds of black gram (Vigna mungo) (2010), Phytochemistry, 71, 363-372.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Vigna mungo trypsin inhibitor purification of the Bowman-Birk proteinase inhibitor from the seeds of black gram, Vigna mungo cv. TAU-1. 8041.5 Da by mass spectrometry, pI 4.3-6.0, stable up to 80°C and at pH 2.0-12.0, analysis of the secondary structural conformation, overview, exhibts non-competitive-type inhibitory activity against both bovine pancreatic trypsin Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzoyl-DL-arginine 4-nitroanilide + H2O a synthetic trypsin substrate Bos taurus N-benzoyl-DL-arginine + 4-nitroaniline
-
?

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
8.2
-
assay at Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0003098
-
Vigna mungo trypsin inhibitor pH 8.2, 37°C Bos taurus