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Ligand vinorine Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C2 1 H2 2 N2 O2
vinorine
CLDVMRAEPFQOSD-BASWHVEKSA-N
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)
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vinorine + NADPH + H+ + O2 = vomilenine + NADP+ + H2O
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vinorine + [reduced NADPH-hemoprotein reductase] + O2 = vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
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In Vivo Product in Enzyme-catalyzed Reactions (1 result)
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acetyl-CoA + 16-epivellosimine = CoA + vinorine
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Substrate in Enzyme-catalyzed Reactions (2 results)
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vinorine + NADPH + H+ + O2 = vomilenine + NADP+ + H2O
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vinorine + [reduced NADPH-hemoprotein reductase] + O2 = vomilenine + [oxidized NADPH-hemoprotein reductase] + H2O
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Product in Enzyme-catalyzed Reactions (2 results)
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acetyl-CoA + 16-epivellosimine = CoA + vinorine
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16-epi-vellosimine + acetyl-CoA = vinorine + CoA
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (1 result)
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0.735
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pH 7.0, 30°C, recombinant wild-type enzyme
KM Value (4 results)
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0.0068
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pH 6.5, 30°C, recombinant enzyme
0.0068
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pH 6.5, 30°C, recombinant enzyme
0.01
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pH 7.0, 30°C, recombinant wild-type enzyme
References & Links Literature References (3)
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Enzymic biosynthesis of vomilenine, a key intermediate of the ajmaline pathway, catalyzed by a novel cytochrome P450-dependent enzyme from plant cell cultures of Rauwolfia serpentina
1995
Falkenhagen, H.; Stoeckigt, J.
Z. Naturforsch. C
50
45-53
Acetyltransfer in natural product biosynthesis - functional cloning and molecular analysis of vinorine synthase
2004
Bayer, A.; Ma, X.; Stockigt, J.
Bioorg. Med. Chem.
12
2787-2795
Dual catalytic activity of a cytochrome P450 controls bifurcation at a metabolic branch point of alkaloid biosynthesis in Rauwolfia serpentina
2017
Dang, T.T.; Franke, J.; Tatsis, E.; O'Connor, S.E.
Angew. Chem. Int. Ed. Engl.
56
9440-9444
Links to other databases for vinorine