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3.2.1.74: glucan 1,4-beta-glucosidase

This is an abbreviated version!
For detailed information about glucan 1,4-beta-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.74

Reaction

(Glcbeta(1-4))r
+
H2O
=
(Glcbeta(1-4))r-1
 +
beta-D-glucopyranose

Synonyms

1,4-beta-D-glucan glucanohydrolase, 1,4-beta-D-glucan glucohydrolase, b-glucan glucohydrolase, beta-(1-4)-glucanase, beta-1,4-beta-glucanase, beta-1,4-glucosidase, beta-glucosidase, beta-glucosidase/xylosidase, Bgl, BglA, Carboxymethyl cellulase, CbhA, Cel48A, Cel9A, Cel9D, cellobiase, cellobiohydrolase, Cellulase, Cex, endo-1,4-beta-D-glucanase, endo/exocellulase, Ex-1, exo-1,4-beta-glucanase, exo-1,4-beta-glucosidase, exo-beta-1,4-glucanase, exo-beta-1,4-glucosidase, exo-bets-1,4-glucanase, exocellulase, exocellulase I, exoglucanase, family 9 glycoside hydrolase, family-1 glycosyl hydrolase, FiG, GH9, glucan 1,4-beta-glucosidase, glucohydrolase, NA23_08975, P-42, Rubg3A, Rubg3B, Rucel5B, TSC, Xyn10E

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.74 glucan 1,4-beta-glucosidase

Crystallization

Crystallization on EC 3.2.1.74 - glucan 1,4-beta-glucosidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
combination of the immunoglobulin-like module and the catalytic module and complex of inactive mutant with cellotetraose, modified microbatch crystallization under oil at 0ºC
-
resolution 2.0 A
-
molecular docking studies for the enzyme with the substrates cellobiose and 4-nitrophenyl beta-D-glucopyranoside. The essential catalytic residues of RuBG3B are D272 and E481. Besides D88, K193, H194, and R160 also form hydrogen bonds with substrates and are conservative. The active center for beta-glucosidic and beta-xylosidic substrates are the same and the bifunctional activity should come from one functional domain. RuBG3A and RuBG3B exhibit higher scores in the docking analysis against 4-nitrophenyl-beta-D-glucopyranoside than against 4-nitrophenyl-beta-D-xylopyranoside, indicating a larger affinity between the enzymes and 4-nitrophenyl-beta-D-glucopyranoside, which is consistent with the kinetic parameters
molecular docking studies for the enzyme with the substrates cellobiose and 4-nitrophenyl-beta-D-glucopyranoside. The essential catalytic residues of RuBG3A are D297 and E499. Besides D113, K218, H219, and R185 also form hydrogen bonds with substrates and are condervative. The active center for beta-glucosidic and beta-xylosidic substrates are the same and the bifunctional activity should come from one functional domain. RuBG3A and RuBG3B exhibit higher scores in the docking analysis against 4-nitrophenyl-beta-D-glucopyranoside than against 4-nitrophenyl-beta-D-xylopyranoside, indicating a larger affinity between the enzymes and 4-nitrophenyl-beta-D-glucopyranoside, which is consistent with the kinetic parameters