By the same authors

Glycosyltransferases: Structures, functions, and mechanisms

Research output: Contribution to journalLiterature reviewpeer-review

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Glycosyltransferases: Structures, functions, and mechanisms. / Lairson, L. L.; Henrissat, B.; Davies, G. J.; Withers, S. G.

In: ANNUAL REVIEW OF BIOCHEMISTRY, Vol. 77, 2008, p. 521-555.

Research output: Contribution to journalLiterature reviewpeer-review

Harvard

Lairson, LL, Henrissat, B, Davies, GJ & Withers, SG 2008, 'Glycosyltransferases: Structures, functions, and mechanisms', ANNUAL REVIEW OF BIOCHEMISTRY, vol. 77, pp. 521-555. https://doi.org/10.1146/annurev.biochem.76.061005.092322

APA

Lairson, L. L., Henrissat, B., Davies, G. J., & Withers, S. G. (2008). Glycosyltransferases: Structures, functions, and mechanisms. ANNUAL REVIEW OF BIOCHEMISTRY, 77, 521-555. https://doi.org/10.1146/annurev.biochem.76.061005.092322

Vancouver

Lairson LL, Henrissat B, Davies GJ, Withers SG. Glycosyltransferases: Structures, functions, and mechanisms. ANNUAL REVIEW OF BIOCHEMISTRY. 2008;77:521-555. https://doi.org/10.1146/annurev.biochem.76.061005.092322

Author

Lairson, L. L. ; Henrissat, B. ; Davies, G. J. ; Withers, S. G. / Glycosyltransferases: Structures, functions, and mechanisms. In: ANNUAL REVIEW OF BIOCHEMISTRY. 2008 ; Vol. 77. pp. 521-555.

Bibtex - Download

@article{2ece7f539ae7432d8d334aef2d7f273d,
title = "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.",
keywords = "carbohydrate-modifying enzymes, glycobiology, glycosylation, ion pair mechanisms, nucleophilic substitution, N-ACETYLGLUCOSAMINYLTRANSFERASE-I, COLI MALTODEXTRIN PHOSPHORYLASE, LIVER-GLYCOGEN PHOSPHORYLASE, RAY CRYSTAL-STRUCTURE, PASTEURELLA-MULTOCIDA SIALYLTRANSFERASE, RETAINING ALPHA-GALACTOSYLTRANSFERASE, DIMETHYLALLYL DIPHOSPHATE ISOMERASE, PHAGE BETA-GLUCOSYLTRANSFERASE, GROUP-B GLYCOSYLTRANSFERASES, BASE-FLIPPING MECHANISM",
author = "Lairson, {L. L.} and B. Henrissat and Davies, {G. J.} and Withers, {S. G.}",
year = "2008",
doi = "10.1146/annurev.biochem.76.061005.092322",
language = "English",
volume = "77",
pages = "521--555",
journal = "ANNUAL REVIEW OF BIOCHEMISTRY",
issn = "0066-4154",
publisher = "Annual Reviews Inc.",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Glycosyltransferases: Structures, functions, and mechanisms

AU - Lairson, L. L.

AU - Henrissat, B.

AU - Davies, G. J.

AU - Withers, S. G.

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

KW - carbohydrate-modifying enzymes

KW - glycobiology

KW - glycosylation

KW - ion pair mechanisms

KW - nucleophilic substitution

KW - N-ACETYLGLUCOSAMINYLTRANSFERASE-I

KW - COLI MALTODEXTRIN PHOSPHORYLASE

KW - LIVER-GLYCOGEN PHOSPHORYLASE

KW - RAY CRYSTAL-STRUCTURE

KW - PASTEURELLA-MULTOCIDA SIALYLTRANSFERASE

KW - RETAINING ALPHA-GALACTOSYLTRANSFERASE

KW - DIMETHYLALLYL DIPHOSPHATE ISOMERASE

KW - PHAGE BETA-GLUCOSYLTRANSFERASE

KW - GROUP-B GLYCOSYLTRANSFERASES

KW - BASE-FLIPPING MECHANISM

UR - http://www.scopus.com/inward/record.url?scp=49449087287&partnerID=8YFLogxK

U2 - 10.1146/annurev.biochem.76.061005.092322

DO - 10.1146/annurev.biochem.76.061005.092322

M3 - Literature review

VL - 77

SP - 521

EP - 555

JO - ANNUAL REVIEW OF BIOCHEMISTRY

JF - ANNUAL REVIEW OF BIOCHEMISTRY

SN - 0066-4154

ER -