Glycosyltransferases: Structures, Functions, and Mechanisms
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Abstract
Glycosyltransferases catalyze glycosidic bond formation using sugar donors containing a nucleoside phosphate or a lipid phosphate leaving group. Only two structural folds, GT-A and GT-B, have been identified for the nucleotide sugar-dependent enzymes, but other folds are now appearing for the soluble domains of lipid phosphosugar-dependent glycosyl transferases. Structural and kinetic studies have provided new insights. Inverting glycosyltransferases utilize a direct displacement S(N)2-like mechanism involving an enzymatic base catalyst. Leaving group departure in GT-A fold enzymes is typically facilitated via a coordinated divalent cation, whereas GT-B fold enzymes instead use positively charged side chains and/or hydroxyls and helix dipoles. The mechanism of retaining glycosyltransferases is less clear. The expected two-step double-displacement mechanism is rendered less likely by the lack of conserved architecture in the region where a catalytic nucleophile would be expected. A mechanism involving a short-lived oxocarbenium ion intermediate now seems the most likely, with the leaving phosphate serving as the base.
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The record
- Venue
- Annual Review of Biochemistry
- Topic
- Glycosylation and Glycoproteins Research
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- University of British Columbia
- Funders
- —
- Keywords
- OxocarbeniumGlycosyltransferaseChemistryGlycosylLeaving groupNucleotideStereochemistryGlycosidic bondEnzymeBiochemistryNucleophileCatalysis
- Has abstract in OpenAlex
- yes