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- W2065687317 abstract "Among the numerous well-characterized families of glycosidases, family 4 appears to be the anomaly, requiring both catalytic NAD+ and a divalent metal for activity. The unusual cofactor requirement prompted the proposal of a mechanism involving key NAD+-mediated redox steps as well as elimination of the glycosidic oxygen. Primary kinetic isotope effects for the 2- and 3-deutero substrate analogues, isotopic exchange with solvent, and structural analysis of a 6-phospho-β-glucosidase, BglT (E.C. 3.2.1.6), provided evidence in support of the proposed mechanism, which has striking resemblances to that of the sugar dehydratases. Furthermore, analysis of the stereochemical outcome indicated that family 4 enzymes are retaining glycosidases." @default.
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- W2065687317 date "2004-06-19" @default.
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- W2065687317 title "An Unusual Mechanism of Glycoside Hydrolysis Involving Redox and Elimination Steps by a Family 4 β-Glycosidase from <i>Thermotoga maritima</i>" @default.
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- W2065687317 doi "https://doi.org/10.1021/ja047632w" @default.
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