N-acetylglutamate synthase: structure, function and defects
β Scribed by Ljubica Caldovic; Nicholas Ah Mew; Dashuang Shi; Hiroki Morizono; Marc Yudkoff; Mendel Tuchman
- Book ID
- 116988967
- Publisher
- Elsevier Science
- Year
- 2010
- Tongue
- English
- Weight
- 938 KB
- Volume
- 100
- Category
- Article
- ISSN
- 1096-7192
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Communicated by David Rosenblatt N-acetylglutamate synthase (NAGS) deficiency, an autosomal recessive disorder, is the last urea cycle disorder for which molecular testing became available. This is the first comprehensive report of 21 mutations that cause NAGS deficiency and of commonly found polymo
N-acetylglutamate synthase (NAGS) is the key enzyme for the regulation of the hepatic urea cycle and is also highly expressed in kidney and gut. The reaction product, N-acetylglutamate, is an allosteric activator of carbamylphosphate synthetase 1 in the liver, catalyzing the initial step of ammonia
N-acetylglutamate (NAG) is a unique cofactor that is essential for the conversion of ammonia to urea in the liver. N-acetylglutamate synthase (NAGS) catalyzes the formation of NAG. Deficiency of NAGS causes a block in ureagenesis resulting in hyperammonemia. Although a number of mutations have been