Biology:Vomilenine glucosyltransferase
From HandWiki
Short description: Class of enzymes
| vomilenine glucosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.219 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a vomilenine glucosyltransferase (EC 2.4.1.219) is an enzyme that catalyzes the chemical reaction
- UDP-glucose + vomilenine [math]\displaystyle{ \rightleftharpoons }[/math] UDP + raucaffricine
Thus, the two substrates of this enzyme are UDP-glucose and vomilenine, whereas its two products are UDP and raucaffricine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:vomilenine 21-O-beta-D-glucosyltransferase. This enzyme is also called UDPG:vomilenine 21-beta-D-glucosyltransferase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
- "Purification, partial amino acid sequence and structure of the product of raucaffricine-O-beta-D-glucosidase from plant cell cultures of Rauwolfia serpentina". Phytochemistry 50 (7): 1099–109. 1999. doi:10.1016/S0031-9422(98)00689-X. PMID 10234858.
- "Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis". Phytochemistry 54 (7): 657–66. 2000. doi:10.1016/S0031-9422(00)00175-8. PMID 10975500.
- Ruyter CM; Stockigt J (1991). "Enzymatic formation of raucaffricine, the major indole alkaloid of Rauwolfia serpentina cell-suspension cultures". Helv. Chim. Acta 74 (8): 1707–1712. doi:10.1002/hlca.19910740811.
 |  |
