Hierarchical classification of glycoside hydrolases |
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Authors: | D G Naumoff |
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Institution: | S. N. Winogradsky Institute of Microbiology, Russian Academy of Sciences, Moscow, 117312, Russia. daniil_naumoff@yahoo.com |
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Abstract: | This review deals with structural and functional features of glycoside hydrolases, a widespread group of enzymes present in
almost all living organisms. Their catalytic domains are grouped into 120 amino acid sequence-based families in the international
classification of the carbohydrate-active enzymes (CAZy database). At a higher hierarchical level some of these families are
combined in 14 clans. Enzymes of the same clan have common evolutionary origin of their genes and share the most important
functional characteristics such as composition of the active center, anomeric configuration of cleaved glycosidic bonds, and
molecular mechanism of the catalyzed reaction (either inverting, or retaining). There are now extensive data in the literature
concerning the relationship between glycoside hydrolase families belonging to different clans and/or included in none of them,
as well as information on phylogenetic protein relationship within particular families. Summarizing these data allows us to
propose a multilevel hierarchical classification of glycoside hydrolases and their homologs. It is shown that almost the whole
variety of the enzyme catalytic domains can be brought into six main folds, large groups of proteins having the same three-dimensional
structure and the supposed common evolutionary origin. |
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