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3.2.1.150: oligoxyloglucan reducing-end-specific cellobiohydrolase

This is an abbreviated version!
For detailed information about oligoxyloglucan reducing-end-specific cellobiohydrolase, go to the full flat file.

Word Map on EC 3.2.1.150

Reaction

alpha-D-xylopyranosyl-(1-6)-[alpha-D-xylopyranosyl-(1-6)-[alpha-D-xylopyranosyl-(1-6)-beta-D-glucopyranosyl-(1-4)]-beta-D-glucopyranosyl-(1-4)]-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose
+
H2O
=
alpha-D-xylopyranosyl-(1-6)-[alpha-D-xylopyranosyl-(1-6)-beta-D-glucopyranosyl-(1-4)]-beta-D-glucopyranose
 +
alpha-D-xylopyranosyl-(1-6)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose

Synonyms

1,4-beta-D-glucan cellobiohydrolase, 1,4-beta-glucan cellobiohydrolase, 1,4-beta-glucan cellobiosidase, avicelase II, beta-1,4-cellobiopyranosidase, beta-1,4-cellobiosidase, beta-1,4-glucan cellobiohydrolase, beta-D-cellobiosidase, C1 cellulase, cellobiohydrolase, cellobiohydrolase I, cellobiohydrolase II, cellobiohydrolase, exo-, cellobiosidase, cellobiosidase, 1,4-beta-glucan, cellulase, C1, cellulose 1,4-beta-cellobiosidase, exo-1,4-beta-D-cellobiohydrolase, exo-beta-1,4-glucan cellobiohydrolase, exocellobiohydrolase, oligoxyloglucan reducing end-specific cellobiohydrolase, oligoxyloglucan reducing-end-specific cellobiohydrolase, OXG-RCBH, spezyme CP

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.150 oligoxyloglucan reducing-end-specific cellobiohydrolase

Engineering

Engineering on EC 3.2.1.150 - oligoxyloglucan reducing-end-specific cellobiohydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D465N
-
inactive OXG-RCBH is co-crystallized with a heptaxyloglucan substrate (XXXG) under conditions similar to the wild-type. There are no differences in the overall structure between the mutant and the wild-type
DELTAG375-H385
-
a deltaloop mutant (deletion mutant of the loop region, Gly375–His385) is constructed. The mutant shows endo-activity with altered substrate recognition. More specifically, cleavage occurs randomly instead of at specific sites, most likely due to the misalignment of the substrate within the subsite. It is supposed that the loop imparts unique substrate specificity with exo-mode hydrolysis in OXG-RCBH
D490N
inactive
E444Q
inactive