 
In molecular biology, glycoside hydrolase family 33 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of ;100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
This family contains sialidases (CAZY GH_33), which hydrolyse alpha-(2- ;3)-, alpha-(2- ;6)-, alpha-(2- ;8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. Sialidases may act as pathogenic factors in microbial infections. The 1.8 A structure of trans-sialidase from leech ("Macrobdella decora", Q27701) in complex with 2-deoxy-2, 3-didehydro-NeuAc was solved. The refined model comprising residues 81-769 has a catalytic beta-propeller domain, a N-terminal lectin-like domain and an irregular beta-stranded domain inserted into the catalytic domain.
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