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Open AccessArticle

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

1
Center for Genetic Medicine Research and Department of Integrative Systems Biology, Children's National Medical Center, the George Washington University, Washington, DC 20010, USA
2
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
Int. J. Mol. Sci. 2015, 16(6), 13004-13022; https://doi.org/10.3390/ijms160613004
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)
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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MDPI and ACS Style

Shi, D.; Allewell, N.M.; Tuchman, M. The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms. Int. J. Mol. Sci. 2015, 16, 13004-13022. https://doi.org/10.3390/ijms160613004

AMA Style

Shi D, Allewell NM, Tuchman M. The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms. International Journal of Molecular Sciences. 2015; 16(6):13004-13022. https://doi.org/10.3390/ijms160613004

Chicago/Turabian Style

Shi, Dashuang; Allewell, Norma M.; Tuchman, Mendel. 2015. "The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms" Int. J. Mol. Sci. 16, no. 6: 13004-13022. https://doi.org/10.3390/ijms160613004

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