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Search results 201 to 232 out of 232 for Nagk

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0.027s
Type Details Score
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication
First Author: Uehara T
Year: 2004
Journal: J Bacteriol
Title: The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling.
Volume: 186
Issue: 21
Pages: 7273-9
Publication
First Author: Ramón-Maiques S
Year: 2006
Journal: J Mol Biol
Title: Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa.
Volume: 356
Issue: 3
Pages: 695-713
Publication
First Author: Fernández-Murga ML
Year: 2002
Journal: Acta Crystallogr D Biol Crystallogr
Title: Towards structural understanding of feedback control of arginine biosynthesis: cloning and expression of the gene for the arginine-inhibited N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and crystallization of the recombinant enzyme and preliminary X-ray studies.
Volume: 58
Issue: Pt 6 Pt 2
Pages: 1045-7
Publication
First Author: Fernández-Murga ML
Year: 2004
Journal: J Bacteriol
Title: Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase.
Volume: 186
Issue: 18
Pages: 6142-9
Publication
First Author: Burillo S
Year: 2004
Journal: J Bacteriol
Title: Interactions between the nitrogen signal transduction protein PII and N-acetyl glutamate kinase in organisms that perform oxygenic photosynthesis.
Volume: 186
Issue: 11
Pages: 3346-54
Publication
First Author: Sugiyama K
Year: 2004
Journal: Plant Cell Physiol
Title: Interaction of N-acetylglutamate kinase with a PII-like protein in rice.
Volume: 45
Issue: 12
Pages: 1768-78
Publication
First Author: Maheswaran M
Year: 2004
Journal: J Biol Chem
Title: Complex formation and catalytic activation by the PII signaling protein of N-acetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942.
Volume: 279
Issue: 53
Pages: 55202-10
Protein Domain
Type: Family
Description: The cyclic N-Acetyl-L-glutamate kinase (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of the arginine biosynthesis pathway. In the cyclic one, typified by Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation [, , , , , , ].
Protein Domain
Type: Family
Description: This entry represents N-acetyl-D-glucosamine kinases which catalyse the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P [, ]. This group of proteins belong to the NagK subfamily of the ROK (nagC/xylR) family.
Publication
First Author: Cunin R
Year: 1986
Journal: Microbiol Rev
Title: Biosynthesis and metabolism of arginine in bacteria.
Volume: 50
Issue: 3
Pages: 314-52
Publication
First Author: Islam MA
Year: 2015
Journal: Mol Cells
Title: N-Acetyl-D-Glucosamine Kinase Promotes the Axonal Growth of Developing Neurons.
Volume: 38
Issue: 10
Pages: 876-85
Publication
First Author: Sharif SR
Year: 2016
Journal: Mol Cells
Title: N-Acetyl-D-Glucosamine Kinase Interacts with Dynein-Lis1-NudE1 Complex and Regulates Cell Division.
Volume: 39
Issue: 9
Pages: 669-79
Protein Domain
Type: Family
Description: This entry includes N-acetyl-D-glucosamine kinases (NAGKs) from prokaryotes and eukaryotes. NAGK converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate []. It has been shown to play an enzyme activity-independent role in human neurons [, ].
Publication
First Author: Davis RH
Year: 1986
Journal: Microbiol Rev
Title: Compartmental and regulatory mechanisms in the arginine pathways of Neurospora crassa and Saccharomyces cerevisiae.
Volume: 50
Issue: 3
Pages: 280-313
Publication  
First Author: Negredo A
Year: 1997
Journal: Microbiology
Title: Cloning, analysis and one-step disruption of the ARG5,6 gene of Candida albicans.
Volume: 143 ( Pt 2)
Pages: 297-302
Publication
First Author: Pauwels K
Year: 2003
Journal: Eur J Biochem
Title: The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis.
Volume: 270
Issue: 5
Pages: 1014-24
Protein Domain
Type: Domain
Description: The N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP) is a nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this entry), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This entry also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homologue of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide [,, ].
Publication
First Author: Ramón-Maiques S
Year: 2002
Journal: Structure
Title: Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis.
Volume: 10
Issue: 3
Pages: 329-42
Publication
First Author: Gil-Ortiz F
Year: 2003
Journal: J Mol Biol
Title: The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic.
Volume: 331
Issue: 1
Pages: 231-44
Publication
First Author: Gil F
Year: 1999
Journal: Acta Crystallogr D Biol Crystallogr
Title: N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms.
Volume: 55
Issue: Pt 7
Pages: 1350-2
Publication
First Author: Gil-Ortiz F
Year: 2002
Journal: Acta Crystallogr D Biol Crystallogr
Title: A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase.
Volume: 58
Issue: Pt 10 Pt 2
Pages: 1892-5
Protein Domain
Type: Family
Description: The noncyclic N-Acetyl-L-glutamate kinase (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of the arginine biosynthesis pathway. In this one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. The Escherichia coli NAGK is a homodimer [, , , , , ].
Protein
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 361  
Fragment?: false
Publication
First Author: Miller BG
Year: 2004
Journal: Biochemistry
Title: Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases.
Volume: 43
Issue: 21
Pages: 6387-92
Publication
First Author: Marco-Marín C
Year: 2003
Journal: J Mol Biol
Title: Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase.
Volume: 334
Issue: 3
Pages: 459-76