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Literature summary for 3.2.1.73 extracted from

  • Abel, M.; Planas, A.; Christensen, U.
    Presteady-state kinetics of Bacillus 1,3-1,4-beta-glucanase: binding and hydrolysis of a 4-methylumbelliferyl trisaccharide substrate (2001), Biochem. J., 357, 195-202.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E134A inactive mutant, analysis of substrate binding Bacillus licheniformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.37
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside pH 6.9, 30°C Bacillus licheniformis
0.5
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside pH 7.2, 30°C Bacillus licheniformis
0.6
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside pH 7.8, 30°C Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose + 4 H2O = 5 beta-D-glucopyranose mechanism, kinetic model Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
Bacillus licheniformis 4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucose
-
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