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Protein Science, Vol 1, Issue 10 1293-1297, Copyright © 1992 by Cold Spring Harbor Laboratory Press

ARTICLE

Specificity mapping of cellulolytic enzymes: Classification into families of structurally related proteins confirmed by biochemical analysis

M. CLAEYSSENS and B. HENRISSAT
Laboratorium voor Biochemie, Faculteit Wetenschappen, Rijksuniversiteit, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium

The specificities of 15 cellulolytic enzymes have been examined using chromophoric glycosides derived from D-glucose, cellobiose, higher cellooligosaccharides, lactose, D-xylose, and {beta}-(1,4)-xylobiose. Coinciding with a classification based on hydrophobic cluster analysis of amino acid sequences, six families each showing a characteristic specificity pattern were observed. Furthermore, in these cases where the anomeric forms of reaction products were determined, results seem to indicate conservation of intrinsic reaction mechanism (single or double displacement) within each family. On the other hand, the low molecular weight substrates do not discriminate exo- from endocellulases. This functional differentiation is speculated to originate from the presence, in exoenzymes, of a tunnel-shaped active site formed by extra loops in their structure.
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