Glucosamine-fructose-6-phosphate aminotransferase (GlmS), also known as glutamine-fructose-6-phosphate transaminase (isomerizing), is an enzyme that catalyzes a key step in the hexosamine biosynthesis pathway . The systematic name for this enzyme class is L-glutamine:D-fructose-6-phosphate isomerase (deaminating) . This enzyme participates in glutamate metabolism and aminosugars metabolism . Specifically, GlmS facilitates the conversion of fructose-6-phosphate and glutamine into glucosamine-6-phosphate and glutamate .
The reaction catalyzed by GlmS is:
L-glutamine + D-fructose 6-phosphate $$\rightleftharpoons$$ L-glutamate + D-glucosamine 6-phosphate
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups .
Recombinant proteins are produced by cloning the gene of interest into an expression vector and expressing it in a host organism like E. coli . The expressed protein is then purified for downstream applications such as structural studies, enzyme assays, or antibody generation . For example, the pap31 gene, as well as the three pap31 gene fragments, were inserted into the pET200D/TOPO expression system in the correct reading frame and current orientation and then confirmed by Sanger sequencing of plasmids isolated from the respective recombinant E. coli BL21 (DE3) clones .
This enzyme catalyzes the initial step in hexosamine metabolism, converting fructose-6-phosphate to glucosamine-6-phosphate using glutamine as the nitrogen source.
KEGG: bhe:BH09920
STRING: 283166.BH09920