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Enzyme linked to diabetes

July 10, 2008

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By Marianne Meadahl

A team of scientists at SFU and the University of York studying the human enzyme OGT are close to understanding the role it plays in processes leading to diabetes and neurodegenerative disease.

SFU chemist David Vocadlo, his grad students Matthew Macauley and David Shen and their British colleagues are investigating how OGT (short for O-linked ß-N-acetylglucosamine transferase) acts to add single sugar units to proteins within the cells of the body.

Their most recent findings are featured in the June 8 edition of Nature Structural & Molecular Biology.

"The basic biological roles of these sugar units remain somewhat mysterious—which is part of the allure—but they have been implicated in diabetes and neurodegenerative disease," explains Vocadlo.

The research describes X-ray crystal studies that provide the first detailed atomic-level images of a close relative of the human OGT and functional studies of a human enzyme.

"The insights gained suggest how this enzyme may identify to which proteins it should bind and to which it should add sugar units," says Vocadlo.

Learning which parts of the enzyme play critically important roles for its functioning will enable further experiments to cast light on the biological role of this sugar modification in cells.

Vocadlo is a Michael Smith Foundation for Health Research scholar and holds a Canada Research Chair in chemical glycobiology—the study of how carbohydrates affect critical processes in biological systems.

His research group investigates how certain sugars can serve to maintain health or disrupt the proper functioning of cells, contributing to the onset of diabetes and neurodegeneration.
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