Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.62 extracted from

  • Shaw, A.K.; Pal, S.K.
    Activity of Subtilisin Carlsberg in macromolecular crowding (2007), J. Photochem. Photobiol. B, Biol., 86, 199-206.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Sodium dodecyl sulfate activity of the enzyme is retarded by 2.3 and 244times in 1 mM and 40 mM sodium dodecyl sulfate respectively compared to that in buffer solution. No evidence of sandwich-like subtilisin–sodium dodecyl sulfate complex formation, thus the enzyme does not encroach into the hydrophobic surfactant core of sodium dodecyl sulfate micelle to form an elongated structure. Retains its structural integrity in sodium dodecyl sulfate solution. Micellar crowding in the vicinity of the enzyme Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
-
Bacillus licheniformis ?
-
?
N-CBZ-Gly-Gly-Leu p-nitroanilide + H2O
-
Bacillus licheniformis ?
-
?

Synonyms

Synonyms Comment Organism
subtilisin Carlsberg
-
Bacillus licheniformis