Document Type
Journal Article
Publication Date
2015
Journal
International Journal of Molecular Sciences
Volume
Volume 16
Inclusive Pages
13004-13022
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.
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
APA Citation
Shi, D., Allewell, N.M., Tuchman, M. (2015). The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms. International Journal of Molecular Sciences, 16, 13004-13022.
Peer Reviewed
1
Open Access
1
Comments
Reproduced with permission of MDPI. International Journal of Molecular Sciences.