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Updated: Jul 7, 2026

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Published on: December 25, 2021
Highlights of glucosamine-6P synthase catalysis
Philippe Durand1, Béatrice Golinelli-Pimpaneau, Stéphane Mouilleron
1Institut de Chimie des Substances Naturelles-CNRS, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Abstract:
L-Glutamine:d-fructose-6-phosphate amidotransferase, also known as glucosamine-6-phosphate synthase (GlcN6P synthase), which catalyzes the first step in a pathway leading to the formation of uridine 5'-diphospho-N-acetyl-d-glucosamine (UDP-GlcNAc), is a key point in the metabolic control of the biosynthesis of amino sugar-containing macromolecules. The molecular mechanism of the reaction catalyzed by GlcN6P synthase is complex and involves amide bond cleavage followed by ammonia channeling and sugar isomerization. This article provides a comprehensive overview of the present knowledge on this multi-faceted enzyme emphasizing the progress made during the last five years.
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