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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a (1->4)-beta-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.
enzyme substrate specificity to the tetradecasaccharide, XXXGXXXG, is analyzed. Wild-type OXG-RCBH generates XXXGXX and XG due to its strict specificity
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by using the hanging-drop vapor-diffusion method. X-ray crystal structure of the OXG-RCBH-substrate complex is determined to a resolution of 2.4 A. OXG-RCBH consists of two seven bladed beta-propeller domains. There is a large cleft between the two domains, and a unique loop encloses one side of the active site cleft. Substrate bound to the cleft, and its reducing end is arranged near the loop region that is believed to impart OXG-RCBH with its activity
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
a deltaloop mutant (deletion mutant of the loop region, Gly375His385) 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
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein is expressed as insoluble inclusion bodies. Purified inclusion bodies were solubilized in 8 M urea. Renaturing by dialysis results in enzymatically active enzyme
Purification, characterization, cloning, and expression of a novel xyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase
Yaoi, K.; Kondo, H.; Suzuki, M.; Noro, N.; Tsuda, S.; Mitsuishi, Y.
Crystallization and preliminary X-ray crystallographic study on a xyloglucan-specific exo-beta-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolase
The crystal structure of a xyloglucan-specific endo-beta-1,4-glucanase from Geotrichum sp. M128 xyloglucanase reveals a key amino acid residue for substrate specificity