2'-deoxymugineic-acid 2'-dioxygenase
| 2'-deoxymugineic-acid 2'-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.24 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2'-deoxymugineic-acid 2'-dioxygenase (EC 1.14.11.24) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are 2'-deoxymugineic acid and oxygen. Its product is mugineic acid (a derivative of azetidine-2-carboxylic acid).[1][2][3]
The enzyme is an alpha-ketoglutarate-dependent hydroxylase with systematic name 2'-deoxymugineic acid,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating). It is also called IDS3.[1] The active site of this non-heme iron protein generates a ferryl intermediate where Fe(IV)=O is the species that transfers its oxygen to the substrate.[4]
This mechanism requires 2-oxoglutaric acid to activate the iron oxygen complex, and this gives succinic acid and carbon dioxide when the second atom of the molecular oxygen is removed.[5]
References
- ^ a b Enzyme 1.14.11.24 at KEGG Pathway Database.
- ^ Nakanishi H, Yamaguchi H, Sasakuma T, Nishizawa NK, Mori S (2000). "Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in the biosynthesis of mugineic acid family phytosiderophores". Plant Mol. Biol. 44 (2): 199–207. doi:10.1023/A:1006491521586. PMID 11117263. S2CID 26139505.
- ^ Mori S; Nakanishi, H; Takahashi, M; Kawasaki, S; Nishizawa, NK; Mori, S (2001). "In vivo evidence that Ids3 from Hordeum vulgare encodes a dioxygenase that converts 2'-deoxymugineic acid to mugineic acid in transgenic rice". Planta. 212 (5–6): 864–71. doi:10.1007/s004250000453. PMID 11346963. S2CID 22984843.
- ^ Mbenza, Naasson M.; Vadakkedath, Praveen G.; McGillivray, Duncan J.; Leung, Ivanhoe K.H. (2017). "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases". Journal of Inorganic Biochemistry. 177: 384–394. doi:10.1016/j.jinorgbio.2017.08.032. PMID 28893416.
- ^ Clifton, Ian J.; Hsueh, Li-Ching; Baldwin, Jack E.; Harlos, Karl; Schofield, Christopher J. (2001). "Structure of proline 3-hydroxylase". European Journal of Biochemistry. 268 (24): 6625–6636. doi:10.1046/j.0014-2956.2001.02617.x. PMID 11737217.