Polysaccharide Hydrolase Folds: Diversity of Structure and Convergence of Function

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Polysaccharide glycosyl hydrolases are a group of enzymes that hydrolyze the glycosidic bond between carbohydrates or between a carbohydrate and a noncarbohydrate moiety. Here we illustrate that traditional schemes for grouping enzymes, such as by substrate specificity or by organism of origin, are not appropriate when thinking of structure-function relationships and protein engineering. Instead, sequence comparisons and structural studies reveal that enzymes with diverse specificities and from diverse organisms can be placed into groups among which mechanisms are largely conserved and insights are likely to be transferable. In particular, we illustrate how enzymes have been grouped using protein sequence alignment algorithms and hydrophobic cluster analysis. Unfortunately for those who seek to improve cellulase function by design, cellulases are distributed throughout glycosyl hydrolase Families 1,5,6,7,9, and 45. These cellulase families include members from widely different fold types, i.e., the TIM-barrel, βαβ-barrel variant (a TIM-barrel-like structure that is imperfectly superimposable on the TIM-barrel template), β-sandwich, and α-helix circular array. This diversity in cellulase fold structure must be taken into account when considering the transfer and application of design strategies between various cellulases.

Original languageAmerican English
Pages (from-to)315-325
Number of pages11
JournalApplied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Issue number1
StatePublished - 1997

NREL Publication Number

  • NREL/JA-580-21352


  • Amylases
  • Cellulases
  • Glycosyl hydrolases
  • Hydrophobic cluster families
  • Structural folds
  • X-ray structures
  • Xylanases


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