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- W1964884818 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 α- and β-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." @default.
- W1964884818 created "2016-06-24" @default.
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- W1964884818 date "2006-01-01" @default.
- W1964884818 modified "2023-10-16" @default.
- W1964884818 title "Family 4 glycoside hydrolases are special: The first β-elimination mechanism amongst glycoside hydrolases" @default.
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- W1964884818 doi "https://doi.org/10.1080/10242420500515926" @default.
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