Iminosuccinic acid
 | |
| Names | |
|---|---|
| IUPAC name
2-Iminobutanedioic acid
| |
| Other names
Iminoaspartic acid; 2-iminobutanedioic acid, iminosuccinate, alpha-iminosuccinate, iminosuccinic acid
| |
| Identifiers | |
3D model (JSmol)
|
|
| ChEBI | |
| ChemSpider | |
| KEGG | |
PubChem CID
|
|
| UNII | |
CompTox Dashboard (EPA)
|
|
| |
| |
| Properties | |
| C4H5NO4 | |
| Molar mass | 131.087 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
| |
Iminoaspartic acid (also known as iminosuccinate or iminoaspartate) is a dicarboxylic acid used in the biosynthesis of nicotinic acid and nicotinamide adenine dinucleotide.
Biosynthesis
The enzyme L-aspartate oxidase oxidises L-aspartic acid:[1]
Subsequent conversions
In Escherichia coli another enzyme, quinolinate synthase, takes iminosuccinic acid with dihydroxyacetone phosphate to form quinolinic acid.[2]
This iron-sulfur protein requires a [4Fe-4S] cluster for activity. The quinolinic acid can be converted to nicotinic acid or incorporated into nicotinamide adenine dinucleotide.[3]
References
- ^ Nasu S, Wicks FD, Gholson RK (1982). "L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase". J. Biol. Chem. 257 (2): 626–32. doi:10.1016/S0021-9258(19)68239-6. PMID 7033218.
- ^ Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M. (2005). "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis" (PDF). FEBS Lett. 579 (17): 3737–3743. doi:10.1016/j.febslet.2005.05.065. PMID 15967443.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Rousset C, Fontecave M, Ollagnier de Choudens S (August 2008). "The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: investigation of cluster ligands". FEBS Letters. 582 (19): 2937–44. Bibcode:2008FEBSL.582.2937R. doi:10.1016/j.febslet.2008.07.032. PMID 18674537.