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Literature summary for 3.4.21.62 extracted from

  • Taniguchi, M.; Atiwetin, P.; Hirai, T.; Itoh, M.; Harada, S.; Hara, S.; Kamei, K.
    Interaction of subtilisin BPN and recombinant fungal protease inhibitor F from silkworm with substituted P1 site residues (2006), Biosci. Biotechnol. Biochem., 70, 1262-1264.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
fungal protease inhibitor F specific inhibitor toward subtilisin-type protease. P1 residue most signficantly affects inhibitory specificity. Mutant T29M has stronger subtilisin-inhibitory activity than the wild-type, mutants T29E and T29R are relatively weaker inhibitors. Inhibitory activities of mutants T29F and T29L are as strong as that of the wild-type Bacillus amyloliquefaciens

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Suc-Ala-Ala-Pro-Phe-4-methyl-coumaryl-7-amide + H2O
-
Bacillus amyloliquefaciens ?
-
?

Synonyms

Synonyms Comment Organism
subtilisin BPN’
-
Bacillus amyloliquefaciens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000000339
-
fungal protease inhibitor F mutant T29M Bacillus amyloliquefaciens
0.000000148
-
fungal protease inhibitor F wild-type Bacillus amyloliquefaciens
0.000000285
-
fungal protease inhibitor F mutant T29L Bacillus amyloliquefaciens
0.000000327
-
fungal protease inhibitor F mutant T29F Bacillus amyloliquefaciens
0.000000678
-
fungal protease inhibitor F mutant T29E Bacillus amyloliquefaciens
0.00000245
-
fungal protease inhibitor F mutant T29R Bacillus amyloliquefaciens
0.00000468
-
fungal protease inhibitor F mutant T29G Bacillus amyloliquefaciens