Structural highlights
Function
GLMS_ECOLI Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Glucosamine-6-phosphate synthase catalyses the first and rate-limiting step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate in the presence of glutamine. The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule. The 18 A hydrophobic channel sequestered from the solvent connects the glutaminase and isomerase active sites, and provides a means of ammonia transfer from glutamine to sugar phosphate. The C-terminal decapeptide sandwiched between the two domains plays a central role in the transfer. Based on the structure, a mechanism of enzyme action and self-regulation is proposed. It involves large domain movements triggered by substrate binding that lead to the formation of the channel.
Channeling of ammonia in glucosamine-6-phosphate synthase.,Teplyakov A, Obmolova G, Badet B, Badet-Denisot MA J Mol Biol. 2001 Nov 9;313(5):1093-102. PMID:11700065[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Teplyakov A, Obmolova G, Badet B, Badet-Denisot MA. Channeling of ammonia in glucosamine-6-phosphate synthase. J Mol Biol. 2001 Nov 9;313(5):1093-102. PMID:11700065 doi:10.1006/jmbi.2001.5094
