Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases.

ABSTRACT: Glycoside hydrolases (GHs) are greatly diverse in sequences and functions, but systematic studies of GH relationships based on structural information are lacking. Here, we report that GHs have multiple evolutionary origins and are structurally derived from 27 homologous superfamilies and 16 folds, but GHs are highly biased to distribute in a few superfamilies and folds. Six of these superfamilies are widely encoded by archaea, bacteria, and eukaryotes, indicating that they may be the most ancient in origin. Most superfamilies vary in enzyme function, and some, such as the superfamilies of (β/α)₈-barrel and (α/α)₆-barrel structures, exhibit extreme functional diversity; this is highly positively correlated with sequence diversity. More than one-third of glycosidase act

SUBMITTER: Li DD 

PROVIDER: S-EPMC8602953 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature