ReviewInternational journal of molecular sciences2015
The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms.
Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Causal Effects of Oral Microbiome, Circulating Metabolites, and Inflammatory Proteins on Recurrent Aphthous Stomatitis: A Two-Sample Mendelian Randomization Study.Oral health & preventive dentistry · 2026Article
- Comparative Analysis of Muscle Nutrients, Lipid Metabolism and Intestinal Microbiota inFoods (Basel, Switzerland) · 2026Article
- C-terminal interleukin 1 alpha (IL-1α) overexpression drives EMT and a vulnerability to ferroptosis in HNSCC.Redox biology · 2026Article
- The faecal bulk heterogeneity: implications for homogenisation and spot-sampling strategies for metabolomic investigations.Metabolomics : Official journal of the Metabolomic Society · 2026Article
- Synergistic inhibition ofFrontiers in microbiology · 2026Article
- NMR based human gut metabolomic profiling reveals altered metabolites associated with pulmonary and extra-pulmonary tuberculosis.Metabolomics : Official journal of the Metabolomic Society · 2025Article
- The Potential Mechanisms ofDrug design, development and therapy · 2025Article
- Article
- Properties and biotechnological applications of microbial deacetylase.Applied microbiology and biotechnology · 2023Review
- A novel strategy for L-arginine production in engineered Escherichia coli.Microbial cell factories · 2023Article
- Metabolic engineering of Escherichia coli for efficient production of L-arginine.Applied microbiology and biotechnology · 2022Article
- Lactobacillus rhamnosus GG modifies the metabolome of pathobionts in gnotobiotic mice.BMC microbiology · 2021Article
- Adaptive physiological water conservation explains hypertension and muscle catabolism in experimental chronic renal failure.Acta physiologica (Oxford, England) · 2021Article
- BCDIN3D RNA methyltransferase stimulates Aldolase C expression and glycolysis through let-7 microRNA in breast cancer cells.Oncogene · 2021Article
- Identification of catalytically distinct arylalkylamine N-acetyltransferase splicoforms from Tribolium castaneum.Protein expression and purification · 2020Article
- Early care ofMolecular genetics and metabolism reports · 2020Article
- Metabolic engineering for efficient supply of acetyl-CoA from different carbon sources in Escherichia coli.Microbial cell factories · 2019Article
- Article
- Late-Onset N-Acetylglutamate Synthase Deficiency: Report of a Paradigmatic Adult Case Presenting with Headaches and Review of the Literature.International journal of molecular sciences · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and L-glutamate. In microorganisms and plants, the enzyme functions in the arginine biosynthetic pathway, while in mammals, its major role is to produce the essential co-factor of carbamoyl phosphate synthetase 1 (CPS1) in the urea cycle. Recent work has shown that several different genes encode enzymes that can catalyze NAG formation. 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. Interestingly, these bifunctional enzymes have higher sequence similarity to vertebrate NAGS than those of the classical (mono-functional) bacterial NAGS. Solving the structures for both classical bacterial NAGS and bifunctional vertebrate-like NAGS/K has advanced our insight into the regulation and catalytic mechanisms of NAGS, and the evolutionary relationship between the two NAGS groups.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.