Chemical rescue of α3-galactosyltransferase. Implications in the mechanism of retaining glycosyltransferases

Ana Monegal; Antoni Planas

doi:10.1021/ja0659931

Chemical rescue of α3-galactosyltransferase. Implications in the mechanism of retaining glycosyltransferases

Ana Monegal
, Antoni Planas^*

^*Corresponding author for this work

IQS School of Engineering

Research output: Indexed journal article › Article › peer-review

57 Citations (Web of Science)

Abstract

The mechanism of retaining glycosyltransferases is still poorly understood and the subject of current debate. Both double displacement and front side single displacement (S_Ni) mechanisms have been proposed. A "chemical rescue methodology" is here applied to a retaining α3-galactosyltransferase. Azide as exogenous nucleophile rescues the activity of the inactive E317A mutant to give β-d-galactosylazide. This result fits best with a double displacement mechanism in which Glu317 is the enzyme nucleophile involved in the formation of a glycosyl-enzyme intermediate.

Original language	English
Pages (from-to)	16030-16031
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	50
DOIs	https://doi.org/10.1021/ja0659931
Publication status	Published - 20 Dec 2006

Keywords

Alpha-galactosyltransferase
Blood-group
Alpha-1,3-galactosyltransferase
Phosphorylase
Substrate

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10.1021/ja0659931

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abstract = "The mechanism of retaining glycosyltransferases is still poorly understood and the subject of current debate. Both double displacement and front side single displacement (SNi) mechanisms have been proposed. A {"}chemical rescue methodology{"} is here applied to a retaining α3-galactosyltransferase. Azide as exogenous nucleophile rescues the activity of the inactive E317A mutant to give β-d-galactosylazide. This result fits best with a double displacement mechanism in which Glu317 is the enzyme nucleophile involved in the formation of a glycosyl-enzyme intermediate.",

keywords = "Alpha-galactosyltransferase, Blood-group, Alpha-1,3-galactosyltransferase, Phosphorylase, Substrate",

author = "Ana Monegal and Antoni Planas",

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AU - Monegal, Ana

AU - Planas, Antoni

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N2 - The mechanism of retaining glycosyltransferases is still poorly understood and the subject of current debate. Both double displacement and front side single displacement (SNi) mechanisms have been proposed. A "chemical rescue methodology" is here applied to a retaining α3-galactosyltransferase. Azide as exogenous nucleophile rescues the activity of the inactive E317A mutant to give β-d-galactosylazide. This result fits best with a double displacement mechanism in which Glu317 is the enzyme nucleophile involved in the formation of a glycosyl-enzyme intermediate.

AB - The mechanism of retaining glycosyltransferases is still poorly understood and the subject of current debate. Both double displacement and front side single displacement (SNi) mechanisms have been proposed. A "chemical rescue methodology" is here applied to a retaining α3-galactosyltransferase. Azide as exogenous nucleophile rescues the activity of the inactive E317A mutant to give β-d-galactosylazide. This result fits best with a double displacement mechanism in which Glu317 is the enzyme nucleophile involved in the formation of a glycosyl-enzyme intermediate.

KW - Alpha-galactosyltransferase

KW - Blood-group

KW - Alpha-1,3-galactosyltransferase

KW - Phosphorylase

KW - Substrate

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 50

ER -

Chemical rescue of α3-galactosyltransferase. Implications in the mechanism of retaining glycosyltransferases

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Keywords

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