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・ Glycoside hydrolase family 18
・ Glycoside hydrolase family 19
・ Glycoside hydrolase family 2
・ Glycoside hydrolase family 20
・ Glycoside hydrolase family 22
・ Glycoside hydrolase family 24
・ Glycoside hydrolase family 25
・ Glycoside hydrolase family 26
・ Glycoside hydrolase family 27
・ Glycoside hydrolase family 28
・ Glycoside hydrolase family 29
・ Glycoside hydrolase family 3
・ Glycoside hydrolase family 30
・ Glycoside hydrolase family 31
・ Glycoside hydrolase family 32
Glycoside hydrolase family 33
・ Glycoside hydrolase family 34
・ Glycoside hydrolase family 35
・ Glycoside hydrolase family 36
・ Glycoside hydrolase family 37
・ Glycoside hydrolase family 38
・ Glycoside hydrolase family 39
・ Glycoside hydrolase family 4
・ Glycoside hydrolase family 42
・ Glycoside hydrolase family 43
・ Glycoside hydrolase family 44
・ Glycoside hydrolase family 45
・ Glycoside hydrolase family 46
・ Glycoside hydrolase family 47
・ Glycoside hydrolase family 48


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Glycoside hydrolase family 33 : ウィキペディア英語版
Glycoside hydrolase family 33

In molecular biology, glycoside hydrolase family 33 is a family of glycoside hydrolases.
Glycoside hydrolases 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.〔(Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999. )〕 This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,〔(Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999. )〕 and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.〔(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'', ) 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.
==References==


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