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Glucosamine-6-phosphate synthase--the multi-facets enzyme.

Abstract
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.
AuthorsSławomir Milewski
JournalBiochimica et biophysica acta (Biochim Biophys Acta) Vol. 1597 Issue 2 Pg. 173-92 (Jun 03 2002) ISSN: 0006-3002 [Print] Netherlands
PMID12044898 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
Chemical References
  • Antifungal Agents
  • Enzyme Inhibitors
  • Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
  • Glucose
Topics
  • Amino Acid Sequence
  • Animals
  • Antifungal Agents (pharmacology)
  • Bacteria (enzymology)
  • Catalysis
  • Diabetes Mellitus (enzymology)
  • Enzyme Inhibitors (pharmacology)
  • Glucose (metabolism)
  • Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) (antagonists & inhibitors, chemistry, genetics, physiology)
  • Humans
  • Inflammation (enzymology)
  • Insulin Resistance
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Neoplasms (enzymology)
  • Sequence Homology, Amino Acid
  • Ulcer (enzymology)

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