Vinorine synthase

vinorine synthase
Identifiers
EC no.	2.3.1.160
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a vinorine synthase (EC 2.3.1.160) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + 16-epivellosimine ${\displaystyle \rightleftharpoons }$ 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

• Pfitzner A, Polz L, Stockligt J (1986). "Properties of vinorine synthase the Rauwolfia enzyme involved in the formation of the ajmaline skeleton". Z. Naturforsch. C: Biosci. 41 (1–2): 103–114. doi: 10.1515/znc-1986-1-217 . S2CID   9818274.
• Bayer A, Ma X, Stockigt J (2004). "Acetyltransfer in natural product biosynthesis--functional cloning and molecular analysis of vinorine synthase". Bioorg. Med. Chem. 12 (10): 2787–95. 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.
• Ma X, Koepke J, Panjikar S, Fritzsch G, Stockigt J (2005). "Crystal structure of vinorine synthase, the first representative of the BAHD superfamily". J. Biol. Chem. 280 (14): 13576–83. doi: 10.1074/jbc.M414508200 . PMID   15665331.