Jump to content

Vinorine synthase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by BU RoBOT (talk | contribs) at 03:20, 10 August 2016 (References: Sort into more specific stub template based on presence in Category:EC 2.3 or subcategories (Task 25)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

vinorine synthase
Identifiers
EC no.2.3.1.160
CAS no.88844-97-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

acetyl-CoA + 16-epivellosimine 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: 103–114.
  • 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)