If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: UDP-N-acetyl-D-glucosamine biosynthesis
|Superclasses:||Biosynthesis → Amines and Polyamines Biosynthesis → UDP-N-acetyl-D-glucosamine Biosynthesis|
|Biosynthesis → Cell Structures Biosynthesis → Lipopolysaccharide Biosynthesis → O-Antigen Biosynthesis|
Pathway Summary from MetaCyc:
UDP-N-acetyl-α-D-glucosamine (UDP-GlcNAc) is an essential precursor of cell wall peptidoglycan, lipopolysaccharide and enterobacterial common antigen. This situates UDP-GlcNAc at a branch point in metabolism, each fork leading to synthesis of a major envelope component of the cell [Neidhardt96]. The enzymes of these pathways are targets for development of novel antibacterial compounds (reviewed in [Kotnik07]).
L-glutamine:D-fructose-6-phosphate aminotransferase, or GFAT, catalyzes the first committed step in UDP-GlcNAc biosynthesis from fructose-6-phosphate. The product of this first reaction, D-glucosamine 6-phosphate, can also be transported into the cell and utilized as a source of carbon; thus, expression of GFAT is controlled at several levels. For details on regulation and the mechanism of uncoupling it from the regulation of glmU expression, please see the protein page: L-glutamine:D-fructose-6-phosphate aminotransferase.
D-glucosamine 6-phosphate is then converted to D-glucosamine 1-phosphate by phosphoglucosamine mutase. The two final reactions of the pathway, transfer of an acetyl group from acetyl-CoA to form N-acetyl-α-D-glucosamine 1-phosphate and transfer of a uridyl group to form the final product, UDP-GlcNAc, are carried out by a bifunctional enzyme, GlmU, which contains two domains that carry out each reaction independently.
Pathway Evidence Glyph:
Key to pathway glyph edge colors:
An enzyme catalyzing this reaction is present in this organism
An enzyme catalyzing this reaction was identified in this organism by the Pathway Hole Filler
No enzyme catalyzing this reaction has been identified in this organism
The reaction and any enzyme that catalyzes it (if one has been identified) is unique to this pathway
Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.
Rubio06: Rubio S, Larson TR, Gonzalez-Guzman M, Alejandro S, Graham IA, Serrano R, Rodriguez PL (2006). "An Arabidopsis mutant impaired in coenzyme A biosynthesis is sugar dependent for seedling establishment." Plant Physiol 140(3);830-43. PMID: 16415216
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