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N-acetylglucosamine 6-phosphate

Known as: GlcNAc6P 
 
National Institutes of Health

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Broader (1)

Acetylglucosamine
analogs & derivatives

Papers overview

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2016
2016
A dynamic pathway analysis approach reveals a limiting futile cycle in N-acetylglucosamine overproducing Bacillus subtilis
Recent advances in genome engineering have further widened the gap between our ability to implement essentially any genetic… Expand
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2016
2016
Allosteric Activation of Escherichia coli Glucosamine-6-Phosphate Deaminase (NagB) In Vivo Justified by Intracellular Amino Sugar Metabolite Concentrations.
UNLABELLED We have investigated the impact of growth on glucosamine (GlcN) and N-acetylglucosamine (GlcNAc) on cellular… Expand
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2011
2011
Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate deaminase.
The human genome contains two genes encoding for two isoforms of the enzyme glucosamine-6-phosphate deaminase (GNPDA, EC 3.5.99.6… Expand
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Review
2010
Review
2010
Dysregulation of the nutrient/stress sensor O-GlcNAcylation is involved in the etiology of cardiovascular disorders, type-2 diabetes and Alzheimer's disease.
O-GlcNAcylation is widespread within the cytosolic and nuclear compartments of cells. This post-translational modification is… Expand
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2009
2009
An alternative route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in Escherichia coli.
A set of enzymes dedicated to recycling of the amino sugar components of peptidoglycan has previously been identified in… Expand
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2009
2009
Allosteric regulation of glucosamine-6-phosphate deaminase (NagB) and growth of Escherichia coli on glucosamine.
Growth on N-acetylglucosamine (GlcNAc) produces intracellular N-acetylglucosamine-6-phosphate (GlcNAc6P), which affects the… Expand
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2008
2008
Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1.
Glucosamine-6-phosphate (GlcN6P) N-acetyltransferase 1 (GNA1) is a key enzyme in the pathway toward biosynthesis of UDP-N… Expand
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2006
2006
Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli.
We report the crystal structure of the apoenzyme of N-acetylglucosamine-6-phosphate (GlcNAc6P) deacetylase from Escherichia coli… Expand
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2001
2001
The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase.
The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential targets for antifungal agents. GNA1, a novel member of the… Expand
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1992
1992
Purification and characterization of glucosamine-6-phosphate deaminase from dog kidney cortex.
Glucosamine-6-phosphate deaminase (EC 5.3.1.10) from dog kidney cortex was purified to homogeneity, as judged by several criteria… Expand
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