Biology:Vinorine synthase
From HandWiki
| vinorine synthase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.3.1.160 | ||||||||
| CAS number | 88844-97-7 | ||||||||
| 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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In enzymology, a vinorine synthase (EC 2.3.1.160) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + 16-epivellosimine [math]\displaystyle{ \rightleftharpoons }[/math] CoA + vinorine
Thus, the two substrates of this enzyme are acetyl-CoA and 16-epivellosimine, whereas its two products are CoA and vinorine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing). This enzyme participates in indole and ipecac alkaloid biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2BGH.
References
- "Properties of vinorine synthase the Rauwolfia enzyme involved in the formation of the ajmaline skeleton". Z. Naturforsch. C: Biosci. 41 (1–2): 103–114. 1986. doi:10.1515/znc-1986-1-217.
- "Acetyltransfer in natural product biosynthesis--functional cloning and molecular analysis of vinorine synthase". Bioorg. Med. Chem. 12 (10): 2787–95. 2004. doi:10.1016/j.bmc.2004.02.029. PMID 15110860.
- Stockigt J; Koepke, J; Bayer, A; Linhard, V; Fritzsch, G; Zhang, B; Michel, H; Stöckigt, J (2004). "Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily". Biochim. Biophys. Acta 1701 (1–2): 129–32. doi:10.1016/j.bbapap.2004.06.011. PMID 15450182.
- "Crystal structure of vinorine synthase, the first representative of the BAHD superfamily". J. Biol. Chem. 280 (14): 13576–83. 2005. doi:10.1074/jbc.M414508200. PMID 15665331.
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