Glycoside_hydrolase_family_108
In molecular biology, glycoside hydrolase family 108 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.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]
Glycoside hydrolase family 108 CAZY GH_108 includes enzymes with lysozyme (N-acetylmuramidase) EC 3.2.1.17 activity. A glutamic acid residue within a conserved Glu-Gly-Gly-Tyr motif is essential for catalytic activity.[8] In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion.[9][10]