Glucosamine 6-phosphate has been used to accelerate enzyme-cleavage of DNA plasmids.
Biochem/physiol Actions
D-Glucosamine 6-phosphate, the natural form of glucosamine, is a monosaccharide produced during hexosamine biosynthesis pathway
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The glmS ribozyme is a conserved riboswitch found in numerous Gram-positive bacteria and responds to the cellular concentrations of glucosamine 6-phosphate (GlcN6P). GlcN6P binding promotes site-specific self-cleavage in the 5' UTR of the glmS mRNA, resulting in downregulation of gene
Quarterly reviews of biophysics, 43(4), 423-447 (2010-09-09)
The glmS ribozyme is the first known example of a natural ribozyme that has evolved to require binding of an exogenous small molecule for activity. In Gram-positive bacteria, this RNA domain is part of the messenger RNA (mRNA) encoding the
Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 366(1580), 2942-2948 (2011-09-21)
The glmS ribozyme-riboswitch is the first known example of a naturally occurring catalytic RNA that employs a small molecule as a coenzyme. Binding of glucosamine-6-phosphate (GlcN6P) activates self-cleavage of the bacterial ribozyme, which is part of the mRNA encoding the
The glmS riboswitch regulates gene expression through a self-cleavage activity. The reaction is catalyzed with the assistance of the metabolite cofactor glucosamine-6-phosphate (GlcN6P), whose amino group is proposed to serve as the general acid during the reaction. This reaction is
The structural rationale, synthesis and evaluation of an inhibitor designed to block glucosamine synthesis by competitively inhibiting the action of glutamine: fructose-6-phosphate amidotransferase and subsequently reducing the transformation of any glucosamine-6-phosphate formed to UDP-N-acetylglucosamine are described. The inhibitor 2-acetamido-2,6-dideoxy-6-sulfo-D-glucose (D-glucosamine-6-sulfonate)
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