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・ Glycoside hydrolase family 62
・ Glycoside hydrolase family 63
・ Glycoside hydrolase family 65
・ Glycoside hydrolase family 66
・ Glycoside hydrolase family 67
・ Glycoside hydrolase family 68
・ Glycoside hydrolase family 7
・ Glycoside hydrolase family 70
・ Glycoside hydrolase family 71
・ Glycoside hydrolase family 72
・ Glycoside hydrolase family 73
・ Glycoside hydrolase family 75
・ Glycoside hydrolase family 76
・ Glycoside hydrolase family 77
・ Glycoside hydrolase family 78
Glycoside hydrolase family 79
・ Glycoside hydrolase family 8
・ Glycoside hydrolase family 80
・ Glycoside hydrolase family 81
・ Glycoside hydrolase family 83
・ Glycoside hydrolase family 85
・ Glycoside hydrolase family 88
・ Glycoside hydrolase family 89
・ Glycoside hydrolase family 9
・ Glycoside hydrolase family 92
・ Glycoside hydrolase family 97
・ Glycoside hydrolase family 98
・ Glycosidic bond
・ Glycosmis
・ Glycosmis crassifolia


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Glycoside hydrolase family 79 : ウィキペディア英語版
Glycoside hydrolase family 79

In molecular biology, glycoside hydrolase family 79 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. )〕
Glycoside hydrolase family 79 includes endo-beta-N-glucuronidase and heparanase ((CAZY GH_79 )). Heparan sulphate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulphate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular microenvironment. Heparanase degrades HS at specific intrachain sites. The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularisation, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity.
==References==


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