The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms
| Autor: | Norma M. Allewell, Mendel Tuchman, Dashuang Shi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Arginine
N-Acetylglutamate synthase Molecular Sequence Data Amino-Acid N-Acetyltransferase catalysis and regulation urologic and male genital diseases Catalysis Article lcsh:Chemistry Inorganic Chemistry crystal structures Catalytic Domain urea cycle Animals Humans Phosphofructokinase 2 Amino Acid Sequence Physical and Theoretical Chemistry lcsh:QH301-705.5 Molecular Biology Peptide sequence Spectroscopy chemistry.chemical_classification biology ATP synthase Bacteria urogenital system Organic Chemistry N-acetylglutamate synthase General Medicine Carbamoyl phosphate synthetase Computer Science Applications Enzyme lcsh:Biology (General) lcsh:QD1-999 chemistry Biochemistry Urea cycle biology.protein arginine biosynthesis |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 16, Iss 6, Pp 13004-13022 (2015) Volume 16 Issue 6 Pages 13004-13022 |
| ISSN: | 1422-0067 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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