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N-acetylglutamate synthase

N-acetylglutamate synthase, NAGS, Amino-Acid N-Acetyltransferase
The N-acetylglutamate synthase gene encodes a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG) from glutamate and acetyl coenzyme-A. NAG is a cofactor of carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle in mammals. This gene may regulate ureagenesis by altering NAG availability and, thereby, CPSI activity. Deficiencies in N-acetylglutamate synthase have been associated with hyperammonemia. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, STEP, Arylamine N-Acetyltransferase
Papers on N-acetylglutamate synthase
Short-term efficacy of N-carbamylglutamate in a patient with N-acetylglutamate synthase deficiency.
Yoo et al., Seoul, South Korea. In J Hum Genet, Jul 2015
N-acetylglutamate synthase (NAGS) deficiency is a rare inborn error regarding the urea cycle, however, its diagnosis is important as it can be effectively treated by N-carbamylglutamate.
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.
Shi et al., Washington, D.C., United States. In Acta Crystallogr Sect F Struct Biol Commun, 2015
Structures of the catalytic N-acetyltransferase (NAT) domain of the bifunctional N-acetyl-L-glutamate synthase/kinase (NAGS/K) from Xylella fastidiosa bound to N-acetyl-L-glutamate (NAG) with and without an N-terminal His tag have been solved and refined at 1.7 and 1.4 Å resolution, respectively.
The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms.
Tuchman et al., Washington, D.C., United States. In Int J Mol Sci, 2014
N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and L-glutamate.
Early treatment of a child with NAGS deficiency using N-carbamyl glutamate results in a normal neurological outcome.
De Meirleir et al., In Eur J Pediatr, 2014
The results of the metabolic work-up were compatible with carbamyl phosphate synthase 1 (CPS1) or N-acetyl glutamate synthase (NAGS) deficiency.
Hyperammonemic encephalopathy in an adenocarcinoma patient managed with carglumic acid.
Khan et al., Calgary, Canada. In Curr Oncol, 2014
Either that deficiency or an undetermined metabolite could lead to inhibition of N-acetylglutamate synthase (nags), a urea cycle enzyme, resulting in hyperammonemia.
4217C>A polymorphism in carbamoyl-phosphate synthase 1 gene may not associate with hyperammonemia development during valproic acid-based therapy.
Itoh et al., Shizuoka, Japan. In Epilepsy Res, 2014
Polymorphisms in the genes encoding carbamoyl-phosphate synthase 1 (CPS1) and N-acetylglutamate synthase (NAGS) were recently reported to be risk factors for the development of hyperammonemia during valproic acid-based therapy.
Diagnosis and treatment of urea cycle disorder in Japan.
Endo et al., Kumamoto, Japan. In Pediatr Int, 2014
Decreased excretion of nitrogen in the urea cycle due to deficiency of carbamoyl phosphate synthase I (CPSI), ornithine transcarbamylase (OTC), argininosuccinate synthase (ASS), argininosuccinate lyase (ASL), and N-acetyl glutamate synthase (NAGS) causes hyperammonemia.
Dietary management of urea cycle disorders: European practice.
Zweers et al., Glasgow, United Kingdom. In Mol Genet Metab, 2013
RESULTS: Data for 464 patients: N-acetylglutamate synthase (NAGS) deficiency, n=10; carbamoyl phosphate synthetase (CPS1) deficiency, n=29; ornithine transcarbamoylase (OTC) deficiency, n=214; citrullinaemia, n=108; argininosuccinic aciduria (ASA), n=80; arginase deficiency, n=23 was reported.
Aberrant expression and distribution of enzymes of the urea cycle and other ammonia metabolizing pathways in dogs with congenital portosystemic shunts.
Spee et al., Utrecht, Netherlands. In Plos One, 2013
In this study, the gene expression of urea cycle enzymes (carbamoylphosphate synthetase (CPS1), ornithine carbamoyltransferase (OTC), argininosuccinate synthetase (ASS1), argininosuccinate lyase (ASL), and arginase (ARG1)), N-acetylglutamate synthase (NAGS), Glutamate dehydrogenase (GLUD1), and glutamate-ammonia ligase (GLUL) was evaluated in dogs with CPSS before and after surgical closure of the shunt.
Expression pattern and biochemical properties of zebrafish N-acetylglutamate synthase.
Krufka et al., Glassboro, United States. In Plos One, 2013
Six enzymes, N-acetylglutamate synthase (NAGS), carbamylphosphate synthetase III, ornithine transcarbamylase, argininosuccinate synthase, argininosuccinate lyase and arginase 1, and two membrane transporters, ornithine transporter and aralar, comprise the urea cycle.
Recurrent encephalopathy: NAGS (N-acetylglutamate synthase) deficiency in adults.
Prasad et al., London, Canada. In Can J Neurol Sci, 2013
N-acetyl-glutamate synthase (NAGS) deficiency is a rare autosomal recessive urea cycle disorder (UCD) that uncommonly presents in adulthood.
A novel type of N-acetylglutamate synthase is involved in the first step of arginine biosynthesis in Corynebacterium glutamicum.
Kalinowski et al., Bielefeld, Germany. In Bmc Genomics, 2012
BACKGROUND: Arginine biosynthesis in Corynebacterium glutamicum consists of eight enzymatic steps, starting with acetylation of glutamate, catalysed by N-acetylglutamate synthase (NAGS).
Transcriptional regulation of N-acetylglutamate synthase.
Caldovic et al., Washington, D.C., United States. In Plos One, 2011
Sp1, CREB, HNF-1, and NF-Y, known to be responsive to hormones and diet, regulate NAGS transcription
Favourable long-term outcome after immediate treatment of neonatal hyperammonemia due to N-acetylglutamate synthase deficiency.
Wermuth et al., Konstanz, Germany. In Eur J Pediatr, 2010
After the human NAGS gene was identified, mutation analysis revealed that the older sibling on NCG therapy was homozygous for a 971G>A (W324X) mutation.
N-acetylglutamate synthase: structure, function and defects.
Tuchman et al., Washington, D.C., United States. In Mol Genet Metab, 2009
NAGS deficiency in humans leads to hyperammonemia and can be primary, due to mutations in the NAGS gene or secondary due to other mitochondrial aberrations that interfere with the normal function of the same enzyme.
Contrasting features of urea cycle disorders in human patients and knockout mouse models.
Grody et al., Los Angeles, United States. In Mol Genet Metab, 2008
Mouse models for each of the urea cycle disorders exist (with the exception of NAGS deficiency), and for almost all of them, their clinical and biochemical phenotypes rather closely resemble the phenotypes seen in human patients.
Deficiency of the carnitine transporter (OCTN2) with partial N-acetylglutamate synthase (NAGS) deficiency.
Lee et al., Taipei, Taiwan. In J Inherit Metab Dis, 2007
Report patient with OCTN2 mutations/deficiency and N-acetylglutamate synthase deficiency.
A trial with N-carbamylglutamate may not detect all patients with NAGS deficiency and neonatal onset.
Alm et al., Huddinge, Sweden. In J Inherit Metab Dis, 2007
case with genetically verified NAGS deficiency and neonatal onset of severe hyperammonaemia
Urea Cycle Disorders Overview
Summar et al., Seattle, United States. In Unknown Journal, 2003
Severe deficiency or total absence of activity of any of the first four enzymes (CPS1, OTC, ASS, ASL) in the urea cycle or the cofactor producer (NAGS) results in the accumulation of ammonia and other precursor metabolites during the first few days of life.
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