|Title||STEREOSELECTIVE HYDROLYSIS CATALYZED BY RELATED BETA-1,4-GLUCANASES AND BETA-1,4-XYLANASES|
|Publication Type||Journal Article|
|Year of Publication||1992|
|Authors||GEBLER, J, GILKES, NR, Claeyssens, M, WILSON, DB, BEGUIN, P, WAKARCHUK, WW, KILBURN, DG, MILLER, RC, WARREN, RAJ, Withers, SG|
|Journal||JOURNAL OF BIOLOGICAL CHEMISTRY|
|Date Published||JUN 25|
Over 80 beta-1,4-glucanases and beta-1,4-xylanases can be classified into one of eight families on the basis of amino acid sequence similarities in their catalytic domains (Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C., Jr., and Warren, R. A. J. (1991) Microbiol. Rev. 55, 303-315). As a test of this classification, the stereochemical course of hydrolysis of 10 enzymes representative of five families has been determined using proton NMR. These data, together with published data for six additional enzymes, show that representatives of a given enzyme family have the same stereoselectivity: four families catalyze hydrolysis with retention of anomeric configuration, two with inversion. The results support the hypothesis that family members share a common general fold, active site topology, and catalytic mechanism.