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3.2.1.B35: Thermococcus kodakaraensis beta-glycosidase

This is an abbreviated version!
For detailed information about Thermococcus kodakaraensis beta-glycosidase, go to the full flat file.

Reaction

Exo-type beta-glycosidase activity with cellobiose, cellotriose, cellotetraose or cellopentaose. In vitro it shows high catalytic efficiency with 4-nitrophenyl beta-D-glucopyranoside or 4-nitrophenyl beta-D-mannopyranoside, and lower catalytic efficiency with 4-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-xylopyranoside =

Synonyms

Pyrococcus kodakaraensis beta-glycosidase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.B35 Thermococcus kodakaraensis beta-glycosidase

Engineering

Engineering on EC 3.2.1.B35 - Thermococcus kodakaraensis beta-glycosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D206N
mutation alters the catalytic turn-over rate for glucosidase and mannosidase activities with fucosidase activity remain unchanged
D206Q
catalytically inactive mutant enzyme. The extended side chain of D206Q is predicted to affect the substrate binding during catalysis
E207S
catalytically inactive mutant enzyme
E399S
catalytically inactive mutant enzyme
Q77R
catalytically inactive mutant enzyme. Q77R might have made some changes in three dimensional structure due to its electrostatic effect and lost its catalytic activity