The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Glycosyltransferases: Structures, Functions, and Mechanisms
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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Cites
Molecular genetic basis of the histo-blood group ABO system
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Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase
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Cited by
The abundance and variety of carbohydrate-active enzymes in the human gut microbiota
Kaoutari, A. E., Armougom, F., Gordon, J. I., Raoult, D., & Henrissat, B. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro3050 · Cited by 1,683
Self-citationBennett, E. P., Mandel, U., Clausen, H., Gerken, T. A., Fritz, T. A., & Tabak, L. A. (2012) · Glycobiology · doi:10.1093/glycob/cwr182 · Cited by 876
Payne, C. M., Knott, B. C., Mayes, H. B., Hansson, H., Himmel, M. E., Sandgren, M., Ståhlberg, J., & Beckham, G. T. (2015) · Chemical Reviews · doi:10.1021/cr500351c · Cited by 855
Schnaar, R. L., Gerardy-Schahn, R., & Hildebrandt, H. (2014) · Physiological Reviews · doi:10.1152/physrev.00033.2013 · Cited by 745
Hart, G. W., & Copeland, R. J. (2010) · Cell · doi:10.1016/j.cell.2010.11.008 · Cited by 643
Metadata
- Authors
- Lairson, L. L., Henrissat, B., Davies, G. J., & Withers, S. G.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 77
- Issue
- 1
- Pages
- 521-555
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2112921913
- Cited by
- 2,079
- References
- 5
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lairson, L. L., Henrissat, B., Davies, G. J., & Withers, S. G. (2008). Glycosyltransferases: Structures, Functions, and Mechanisms. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.76.061005.092322
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
