Biology:Vomilenine glucosyltransferase
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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 | ||||||||
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Vomilenine glucosyltransferase (EC 2.4.1.219) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The two substrates of this enzyme characterised from Rauwolfia serpentina are vomilenine and UDP-glucose. Its products are raucaffricine and uridine diphosphate (UDP). Raucaffricine is the major indole alkaloid found in this species of plant.[1][2][3]
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.[4]
References
- ↑ 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. Bibcode: 1991HChAc..74.1707R.
- ↑ "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. Bibcode: 1999PChem..50.1099W.
- ↑ "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. Bibcode: 2000PChem..54..657W.
- ↑ Enzyme 2.4.1.219 at KEGG Pathway Database.
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