| Name | Amino-acid N-acetyltransferase (ArgA) | Short Name | NH2A_AcTrfase_ArgA |
| Type | Family | Description | This entry represents amino-acid N-acetyltransferase or N-acetylglutamate synthase, which is the product of the argA gene and the first enzyme in arginine biosynthesis. This enzyme displays more diversity between bacteria, fungi and mammals than other enzymes in arginine metabolism, and N-acetylglutamate itself can have different roles in different taxonomic groups: in prokaryotes, lower eukaryotes and plants it is the first intermediate in arginine biosynthesis, while in vertebrates it is an allosteric cofactor for the first enzyme in the urea cycle []. In bacteria, arginine can regulate ornithine biosynthesis via a feedback inhibition mechanism []. This enzyme may also act on aspartate. |
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| First Author | Title | Year | Journal | Volume | Pages |
|---|---|---|---|---|---|
| Caldovic L | N-acetylglutamate and its changing role through evolution. | 2003 | Biochem J | 372 | 279-90 |
| Rajagopal BS | Use of inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains. | 1998 | Appl Environ Microbiol | 64 | 1805-11 |
To cite PlanMine, please refer to the following publication:Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C. |
| This database is part of a project that received funding from the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (grant agreement number 649024). |
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