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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

N-acetylglucosamine kinase

N-acetylglucosamine kinase, NAGK, GlcNAc kinase
This gene encodes a member of the N-acetylhexosamine kinase family. The encoded protein catalyzes the conversion of N-acetyl-D-glucosamine to N-acetyl-D-glucosamine 6-phosphate, and is the major mammalian enzyme which recovers amino sugars. [provided by RefSeq, Nov 2011] (from NCBI)
Top mentioned proteins: ACID, STEP, CAN, HAD, V1a
Papers on N-acetylglucosamine kinase
Increased L-arginine Production by Site-directed Mutagenesis of N-acetyl-L-glutamate Kinase and proB Gene Deletion in Corynebacterium crenatum.
New
Xiong et al., Nanchang, China. In Biomed Environ Sci, Dec 2015
OBJECTIVE: In Corynebacterium crenatum, the adjacent D311 and D312 of N-acetyl-L-glutamate kinase (NAGK), as a key rate-limiting enzyme of L-arginine biosynthesis under substrate regulatory control by arginine, were initially replaced with two arginine residues to investigate the L-arginine feedback inhibition for NAGK.
N-Acetyl-D-Glucosamine Kinase Promotes the Axonal Growth of Developing Neurons.
New
Moon et al., Kyŏngju, South Korea. In Mol Cells, Dec 2015
N-acetyl-D-glucosamine kinase (NAGK) plays an enzyme activity-independent, non-canonical role in the dendritogenesis of hippocampal neurons in culture.
Glutamine Assimilation and Feedback Regulation of L-acetyl-N-glutamate Kinase Activity in Chlorella variabilis NC64A Results in Changes in Arginine Pools.
New
Ermilova et al., Saint Petersburg, Russia. In Protist, Nov 2015
The Chlorella PII signaling protein controls, in a glutamine-dependent manner, the key enzyme of the ornithine/arginine biosynthesis pathway, N-acetyl-L-glutamate kinase (NAGK) that leads to arginine formation.
Monomeric Corynebacterium glutamicum N-acetyl glutamate kinase maintains sensitivity to L-arginine but has a lower intrinsic catalytic activity.
New
Zheng et al., Guangzhou, China. In Appl Microbiol Biotechnol, Nov 2015
UNASSIGNED: N-acetyl glutamate kinase (NAGK) is a key enzyme in the synthesis of L-arginine, and L-arginine-sensitive NAGK typically has hexameric architecture.
Identification of an N-acetylglucosamine kinase essential for UDP-N-acetylglucosamine salvage synthesis in Arabidopsis.
New
Sato et al., Japan. In Febs Lett, Nov 2015
Here, we show that the homolog of human GlcNAc kinase (GNK) is conserved in land plants.
Energy Sensing versus 2-Oxoglutarate Dependent ATPase Switch in the Control of Synechococcus PII Interaction with Its Targets NAGK and PipX.
Forchhammer et al., Tübingen, Germany. In Plos One, 2014
PII proteins constitute a superfamily of highly conserved signaling devices, common in all domains of life.
N-acetyl-D-glucosamine kinase interacts with dynein light-chain roadblock type 1 at Golgi outposts in neuronal dendritic branch points.
Moon et al., Kyŏngju, South Korea. In Exp Mol Med, 2014
N-acetylglucosamine kinase (GlcNAc kinase or NAGK) is a ubiquitously expressed enzyme in mammalian cells.
The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms.
Review
Tuchman et al., Washington, D.C., United States. In Int J Mol Sci, 2014
A bifunctional enzyme was identified in certain bacteria, which catalyzes both NAGS and N-acetylglutamate kinase (NAGK) activities, the first two steps of the arginine biosynthetic pathway.
Metabolic pathway engineering using the central signal processor PII.
Forchhammer et al., Tübingen, Germany. In Microb Cell Fact, 2014
PCC6803 strain with a PII-I86N mutation over-accumulated arginine through constitutive activation of the key enzyme N-acetylglutamate kinase (NAGK).
A widespread glutamine-sensing mechanism in the plant kingdom.
Impact
Forchhammer et al., Tübingen, Germany. In Cell, 2014
The plastid-localized PII signaling protein controls, in a glutamine-dependent manner, the key enzyme of the ornithine synthesis pathway, N-acetyl-l-glutamate kinase (NAGK), that leads to arginine and polyamine formation.
From cyanobacteria to plants: conservation of PII functions during plastid evolution.
Review
Forchhammer et al., Tübingen, Germany. In Planta, 2013
We also discuss PII-like proteins and domains, in particular, the similarity between ATP-phosphoribosyltransferase (ATP-PRT) and its PII-like domain and the complex between N-acetyl-L-glutamate kinase (NAGK) and its PII activator protein from oxygenic phototrophs.
The network of P(II) signalling protein interactions in unicellular cyanobacteria.
Review
Forchhammer, Tübingen, Germany. In Adv Exp Med Biol, 2009
At least one of these functions, regulation of arginine biosynthesis by controlling the key enzyme N-acetyl-L: -glutamate kinase (NAGK), was transmitted by the ancestral cyanobacterium, which gave rise to chloroplasts, into the eukaryotic domain and was conserved during the evolution of planta.
PII in higher plants: a modern role for an ancient protein.
Review
Moorhead et al., Calgary, Canada. In Trends Plant Sci, 2009
Previous findings suggest that PII-N-acetylglutamate kinase (NAGK) complex formation controls l-arginine biosynthesis, whereas other work implicates PII in regulating chloroplastic NO2(-) uptake.
Arginine and nitrogen storage.
Review
Rubio et al., Valencia, Spain. In Curr Opin Struct Biol, 2008
When nitrogen is abundant, prokaryotic and eukaryotic oxygen-producing photosynthetic organisms store nitrogen as arginine, by relieving feedback inhibition of the arginine biosynthesis controlling enzyme, N-acetylglutamate kinase (NAGK).
Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation.
GeneRIF
Hinderlich et al., Berlin, Germany. In J Mol Biol, 2007
Phosphorylation of Tyr205 may modulate GlcNAc kinase activity and/or specificity.
Use of a cell-free system to determine UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities in human hereditary inclusion body myopathy.
GeneRIF
Huizing et al., Bethesda, United States. In Glycobiology, 2005
The cell-free system was validated for MNK activity, and it revealed that mutations in one enzymatic domain (in MNK, A631V, M712T) affected not only that domain's enzyme activity, but also the activity of the other domain.
Prediction of MYCN amplification in neuroblastoma using serum DNA and real-time quantitative polymerase chain reaction.
Impact
Sugimoto et al., Kyoto, Japan. In J Clin Oncol, 2005
PATIENTS AND METHODS: Using DNA-based real-time quantitative polymerase chain reaction, we simultaneously quantified MYCN (2p24) and a reference gene, NAGK (2p12), and evaluated MYCN copy number as an MYCN/NAGK (M/N) ratio in 87 NB patients whose MYCN status had been determined by Southern blotting.
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