| First Author | Caldovic L | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 299 |
| Issue | 4 | Pages | 581-6 |
| PubMed ID | 12459178 | Mgi Jnum | J:80847 |
| Mgi Id | MGI:2447276 | Doi | 10.1016/s0006-291x(02)02696-7 |
| Citation | Caldovic L, et al. (2002) Cloning and expression of the human N-acetylglutamate synthase gene. Biochem Biophys Res Commun 299(4):581-6 |
| abstractText | N-acetylglutamate synthase (NAGS, E.C. 2.3.1.1) is a mitochondrial enzyme catalyzing the formation of N-acetylglutamate (NAG), an essential allosteric activator of carbamylphosphate synthase I (CPSI), the first enzyme of the urea cycle. Patients with NAGS deficiency develop hyperammonemia because CPSI is inactive without NAG. The human NAGS cDNA was isolated from a liver library based on its similarity to mouse NAGS. The deduced amino acid sequence contains an N-terminal putative mitochondrial targeting signal of 49 amino acids (63% identity with mouse NAGS) followed by a 'variable domain' of 45 amino acids (35% identity) and a 'conserved domain' of 440 amino acids (92% identity). A cDNA sequence containing the 'conserved domain' complements an NAGS-deficient Escherichia coli strain and the recombinant protein has arginine-responsive NAGS catalytic activity. The NAGS gene is expressed in the liver and small intestine; the intestinal transcript is smaller in size than liver transcript. |
