1QH7

CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE

Summary for 1QH7

• Entry DOI: 10.2210/pdb1qh7/pdb
• Related: 1QH6
• Descriptor: XYLANASE, beta-D-xylopyranose (3 entities in total)
• Functional Keywords: glycosyl hydrolase, hydrolase
• Biological source: Bacillus agaradhaerens
• Total number of polymer chains: 2
• Total formula weight: 46611.35

Authors

Sabini, E.,Sulzenbacher, G.,Dauter, M.,Dauter, Z.,Jorgensen, P.L.,Schulein, M.,Dupont, C.,Davies, G.J.,Wilson, K.S. (deposition date: 1999-05-11, release date: 2000-05-17, Last modification date: 2024-11-13)

Primary citation

Sabini, E.,Sulzenbacher, G.,Dauter, M.,Dauter, Z.,Jorgensen, P.L.,Schulein, M.,Dupont, C.,Davies, G.J.,Wilson, K.S.
Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase.
Chem.Biol., 6:483-492, 1999

PubMed Abstract: The enzymatic hydrolysis of glycosides involves the formation and subsequent breakdown of a covalent glycosyl-enzyme intermediate via oxocarbenium-ion-like transition states. The covalent intermediate may be trapped on-enzyme using 2-fluoro-substituted glycosides, which provide details of the intermediate conformation and noncovalent interactions between enzyme and oligosaccharide. Xylanases are important in industrial applications - in the pulp and paper industry, pretreating wood with xylanases decreases the amount of chlorine-containing chemicals used. Xylanases are structurally similar to cellulases but differ in their specificity for xylose-based, versus glucose-based, substrates.

PubMed: 10381409
DOI: 10.1016/S1074-5521(99)80066-0

Experimental method

X-RAY DIFFRACTION (1.78 Å)