The N-Acetylglutamate Synthase Family: Structures, Function and MechanismsReport as inadecuate




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1

Center for Genetic Medicine Research and Department of Integrative Systems Biology, Childrens 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

Abstract 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





Author: Dashuang Shi 1,* , Norma M. Allewell 2 and Mendel Tuchman 1

Source: http://mdpi.com/



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