ArticleThe Journal of biological chemistry2008
The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 39 citations in OpenAlex.
- Architecture remodeling activates the HerA-DUF anti-phage defense system.Molecular cell · 2025Article
- Use of pure recombinant human enzymes to assess the disease-causing potential of missense mutations in urea cycle disorders, applied to N-acetylglutamate synthase deficiency.Journal of inherited metabolic disease · 2024Article
- Datamining approaches for examining the low prevalence of N-acetylglutamate synthase deficiency and understanding transcriptional regulation of urea cycle genes.Journal of inherited metabolic disease · 2024Article
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021Review
- Computer Modeling of N-Acetylglutamate Synthase: From Primary Structure to Elemental Stages of Catalysis.Doklady. Biochemistry and biophysics · 2020Article
- Effect of arginine on oligomerization and stability of N-acetylglutamate synthase.Scientific reports · 2016Article
- The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms.International journal of molecular sciences · 2015Review
- Structures of the N-acetyltransferase domain of Xylella fastidiosa N-acetyl-L-glutamate synthase/kinase with and without a His tag bound to N-acetyl-L-glutamate.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Metabolic engineering of microorganisms for the production of L-arginine and its derivatives.Microbial cell factories · 2014Article
- Expression pattern and biochemical properties of zebrafish N-acetylglutamate synthase.PloS one · 2014Article
- Structure of N-acetyl-L-glutamate synthase/kinase from Maricaulis maris with the allosteric inhibitor L-arginine bound.Biochemical and biophysical research communications · 2013Article
- Structure of the complex of Neisseria gonorrhoeae N-acetyl-L-glutamate synthase with a bound bisubstrate analog.Biochemical and biophysical research communications · 2013Article
- Article
- Functional dissection of N-acetylglutamate synthase (ArgA) of Pseudomonas aeruginosa and restoration of its ancestral N-acetylglutamate kinase activity.Journal of bacteriology · 2012Article
- Article
- Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase.PloS one · 2012Article
- The ygeW encoded protein from Escherichia coli is a knotted ancestral catabolic transcarbamylase.Proteins · 2011Article
- Down-regulation of hepatic urea synthesis by oxypurines: xanthine and uric acid inhibit N-acetylglutamate synthase.The Journal of biological chemistry · 2011Article
- A novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris.PloS one · 2011Article
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Authors and funding
8 authors at 4 institutions in 1 country.
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Abstract
The crystal structures of N-acetylglutamate synthase (NAGS) in the arginine biosynthetic pathway of Neisseria gonorrhoeae complexed with acetyl-CoA and with CoA plus N-acetylglutamate have been determined at 2.5- and 2.6-A resolution, respectively. The monomer consists of two separately folded domains, an amino acid kinase (AAK) domain and an N-acetyltransferase (NAT) domain connected through a 10-A linker. The monomers assemble into a hexameric ring that consists of a trimer of dimers with 32-point symmetry, inner and outer ring diameters of 20 and 100A, respectively, and a height of 110A(.) Each AAK domain interacts with the cognate domains of two adjacent monomers across two 2-fold symmetry axes and with the NAT domain from a second monomer of the adjacent dimer in the ring. The catalytic sites are located within the NAT domains. Three active site residues, Arg316, Arg425, and Ser427, anchor N-acetylglutamate in a position at the active site to form hydrogen bond interactions to the main chain nitrogen atoms of Cys356 and Leu314, and hydrophobic interactions to the side chains of Leu313 and Leu314. The mode of binding of acetyl-CoA and CoA is similar to other NAT family proteins. The AAK domain, although catalytically inactive, appears to bind arginine. This is the first reported crystal structure of any NAGS, and it provides insights into the catalytic function and arginine regulation of NAGS enzymes.
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