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Int. J. Mol. Sci. 2015, 16(6), 13004-13022;

The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms

Center for Genetic Medicine Research and Department of Integrative Systems Biology, Children's National Medical Center, the George Washington University, Washington, DC 20010, USA
Department of Cell Biology and Molecular Genetics and Department of Chemistry and Biochemistry, College of Computer, Mathematical and Natural Sciences, University of Maryland, College Park, MD 20742, USA
Author to whom correspondence should be addressed.
Academic Editor: Charles A. Collyer
Received: 27 February 2015 / Revised: 24 April 2015 / Accepted: 13 May 2015 / Published: 9 June 2015
(This article belongs to the Special Issue Protein Crystallography in Molecular Biology 2015)
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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. View Full-Text
Keywords: arginine biosynthesis; urea cycle; N-acetylglutamate synthase; crystal structures; catalysis and regulation arginine biosynthesis; urea cycle; N-acetylglutamate synthase; crystal structures; catalysis and regulation

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Shi, D.; Allewell, N.M.; Tuchman, M. The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms. Int. J. Mol. Sci. 2015, 16, 13004-13022.

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