Deacetoxyvindoline 4-hydroxylase

desacetoxyvindoline 4-hydroxylase
Identifiers
EC number	1.14.11.20
CAS number	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 / EGO
Search PMC articles PubMed articles

In enzymology, a deacetoxyvindoline 4-hydroxylase (EC 1.14.11.20) is an enzyme that catalyzes the chemical reaction

deacetoxyvindoline + 2-oxoglutarate + O₂ $\rightleftharpoons$ deacetylvindoline + succinate + CO₂

The 3 substrates of this enzyme are deacetoxyvindoline, 2-oxoglutarate, and O₂, whereas its 3 products are deacetylvindoline, succinate, and CO₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is deacetoxyvindoline,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). This enzyme participates in indole and ipecac alkaloid biosynthesis.

References

• 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. 
• 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. PMID 8449913. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=34899. 

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