3''-deamino-3''-oxonicotianamine reductase
| 3″-deamino-3″-oxonicotianamine reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.285 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
3''-deamino-3''-oxonicotianamine reductase (EC 1.1.1.285) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are 3''-deamino-3''-oxonicotianamine, reduced nicotinamide adenine dinucleotide (NADH), and a proton. Its products are 2'-deoxymugineic acid and oxidised (NAD+). This enzyme can also use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-deoxymugineic acid:NAD(P)+ 3-oxidoreductase. It is part of the pathway which converts the siderophore, nicotianamine, to other metal-chelating molecules in higher plants. These allow the plant to efficiently take up metals such as zinc and iron from the soil.[3]
References
- ^ Enzyme 1.1.1.285 at KEGG Pathway Database.
- ^ Shojima S, Nishizawa NK, Fushiya S, Nozoe S, Irifune T, Mori S (August 1990). "Biosynthesis of Phytosiderophores : In Vitro Biosynthesis of 2'-Deoxymugineic Acid from l-Methionine and Nicotianamine". Plant Physiology. 93 (4): 1497–503. doi:10.1104/pp.93.4.1497. PMC 1062701. PMID 16667646.
- ^ Marschner, Horst (2012). Marschner's Mineral Nutrition of Higher Plants. London Waltham, MA: Academic Press. ISBN 978-0-12-384905-2.