@article { ISI:000239089700019,
	title = {Family 4 glycoside hydrolases are special: The first beta-elimination mechanism amongst glycoside hydrolases},
	journal = {BIOCATALYSIS AND BIOTRANSFORMATION},
	volume = {24},
	number = {1-2},
	year = {2006},
	note = {6th Carbohydrate Bioengineering Meeting, Barcelona, SPAIN, APR 03-06, 2005},
	month = {JAN-APR},
	pages = {167-176},
	abstract = {The glycoside hydrolases are a large group of enzymes that can be grouped into two major mechanistic classes based upon the stereochemical outcome of catalysis: retention and inversion of sugar anomeric configuration. Both mechanisms involve nucleophilic displacement at the anomeric center, and both proceed via positively charged oxocarbenium ion-like transition states. Exceptions to this are the Family 4 glycoside hydrolases (GH4), which display an unusual requirement for NAD+ and a divalent metal for activity. In addition, Family 4, uniquely, contains both alpha- and beta-glycosidases. A novel mechanism is proposed for all GH4 members, featuring a redox-elimination-addition sequence, and involving anionic transition states to effect hydrolytic cleavage of the glycosidic linkage.},
	issn = {1024-2422},
	doi = {10.1080/10242420500515926},
	author = {Yip, Vivian L. Y. and Withers, Stephen G.}
}
