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Literature summary for 3.4.21.62 extracted from

  • Castillo, B.; Bansal, V.; Ganesan, A.; Halling, P.; Secundo, F.; Ferrer, A.; Griebenow, K.; Barletta, G.
    On the activity loss of hydrolases in organic solvents: II. a mechanistic study of subtilisin Carlsberg (2006), BMC Biotechnol., 6, 51.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
1,4-dioxane reduces the enzyme activity. Structural changes, flexibility, hydration, and changes of the enzyme ionization state are not responsible for the low storage stability. Possible depletion or rearrangement of water molecules around the active site, or small structural perturbations around the active site or movements of counter ions Bacillus licheniformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
130
-
sec-phenethyl alcohol after incubation in 1,4-dioxane, co-lyophilization with methyl-beta-cyclodextrin Bacillus licheniformis
319
-
sec-phenethyl alcohol after a 4-day incubation period in 1,4-dioxane, co-lyophilization with methyl-beta-cyclodextrin Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sec-phenethyl alcohol + vinyl butyrate
-
Bacillus licheniformis ?
-
?

Synonyms

Synonyms Comment Organism
subtilisin C.
-
Bacillus licheniformis
subtilisin Carlsberg
-
Bacillus licheniformis

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5
-
Bacillus licheniformis