Desacetoxyvindoline 4-hydroxylase
| Desacetoxyvindoline 4-hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.20 | ||||||||
| CAS no. | 132084-83-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Desacetoxyvindoline 4-hydroxylase (EC 1.14.11.20) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are desacetoxyvindoline and oxygen. Its product is deacetylvindoline.[1][2][3]
The enzyme is an alpha-ketoglutarate-dependent hydroxylase[4] with systematic name desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4beta-hydroxylating). Other names in common use include desacetoxyvindoline 4-hydroxylase, desacetyoxyvindoline-17-hydroxylase, D17H, desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase, and (4beta-hydroxylating). It is a non-heme iron protein with ferryl active site where Fe(IV)=O is the species that transfers its oxygen to the substrate.[5]
The mechanism of action 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. Ascorbic acid improves the turnover number of the enzyme.[4][5][6]
The enzyme is part of the biosynthetic pathway to indole and ipecac alkaloids.[1]
References
- ^ a b Enzyme 1.14.11.20 at KEGG Pathway Database.
- ^ Vazquez-Flota FA, De Luca V (1998). "Developmental and light regulation of desacetoxyvindoline 4-hydroxylase in catharanthus roseus (L.) G. Don. . Evidence Of a multilevel regulatory mechanism". Plant Physiol. 117 (4): 1351–61. doi:10.1104/pp.117.4.1351. PMC 34899. PMID 9701591.
- ^ Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM (2006). "A proteomic analysis of arsenical drug resistance in Trypanosoma brucei". Proteomics. 6 (9): 2726–32. doi:10.1002/pmic.200500419. PMID 16526094.
- ^ a b De Carolis E, De Luca V (1993). "Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus". J. Biol. Chem. 268 (8): 5504–11. doi:10.1016/S0021-9258(18)53349-4. PMID 8449913.
- ^ a b 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.