Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 47, Pages 14853-14857Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201707922
Keywords
enzyme catalysis; enzymes; glycosyltransferases; reaction mechanisms; structural biology
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Funding
- MINECO [BFU2016-77427-C2-2-R, CTQ2016-76941-R]
- Basque Government
- MINECO under the Juan de la Cierva Postdoctoral program [FJCI-2015-25725]
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Glycosyltransferases (GTs) are a key family of enzymes that catalyze the synthesis of glycosidic bonds in all living organisms. The reaction involves the transfer of a glycosyl moiety and can proceed with retention or inversion of the anomeric configuration. To date, the catalytic mechanism of retaining GTs is a topic of great controversy, particularly for those enzymes containing a putative nucleophilic residue in the active site, for which the occurrence of a double-displacement mechanism has been suggested. We report native ternary complexes of the retaining glycosyltransferase alpha-1,3-galactosyltransferase (alpha 3GalT) from Bos taurus, which contains such a nucleophile in the active site, in a productive mode for catalysis in the presence of its sugar donor UDP-Gal, the acceptor substrate lactose, and the divalent cation cofactor. This new experimental evidence supports the occurrence of a front-side substrate-assisted S(N)i-type reaction for alpha 3GalT, and suggests a conserved common catalytic mechanism among retaining GTs.
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