quick and sensitive enzyme detection assay based on the diphosphatase-coupled colorimetric method with malachite green, and assay for glucosamine-1-phosphate N-acetyltransferase activity of the bifunctional enzyme, both applicable in microtitter plates
quick and sensitive enzyme detection assay based on the diphosphatase-coupled colorimetric method with malachite green, and assay for glucosamine-1-phosphate N-acetyltransferase activity of the bifunctional enzyme, both applicable in microtitter plates
prokaryotic/microbial sugar nucleotidyl transferases are targets for design of selective inhibitors due to their different metal mechanisms compared to eukaryotes
the identification of a selective inhibitory allosteric binding site in the parasite enzyme and the fact that the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed, makes the enzyme a good target for drug development
biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. As glycosylation is the most important modification for activating peptide drugs, the activated form of N-acetyl-alpha-D-glucosamine is thought to be important for future development of effective drugs
biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. As glycosylation is the most important modification for activating peptide drugs, the activated form of N-acetyl-alpha-D-glucosamine is thought to be important for future development of effective drugs