L-Glutamine: D-fructose-6-phosphate amidotransferase, known under trivial name of
glucosamine-6-phosphate synthase, as the only member of the amidotransferase subfamily of
enzymes, does not display any
ammonia-dependent activity. This
enzyme, catalysing the first committed step in a pathway leading to the eventual formation of
uridine 5'-diphospho-N-acetyl-D-glucosamine (
UDP-GlcNAc), is an important point of metabolic control in biosynthesis of
amino sugar-containing macromolecules. The molecular mechanism of reaction catalysed by
GlcN-6-P synthase is complex and involves both amino transfer and
sugar isomerisation. Substantial alterations to the
enzyme structure and properties have been detected in different neoplastic tissues.
GlcN-6-P synthase is inflicted in phenomenon of
hexosamine-induced
insulin resistance in diabetes. Finally, this
enzyme has been proposed as a promising target in antifungal
chemotherapy. Most of these issues, especially their molecular aspects, have been extensively studied in recent years. This article provides a comprehensive overview of the present knowledge on this multi-facets
enzyme.