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Ligand (-)-vetispiradiene Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C1 5 H2 4
(-)-vetispiradiene
WEZDOYDDKIHCLM-QLFBSQMISA-N
Roles as Enzyme Ligand
In Vivo Product in Enzyme-catalyzed Reactions (1 result)
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trans,trans-farnesyl diphosphate = vetispiradiene + diphosphate
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Substrate in Enzyme-catalyzed Reactions (1 result)
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(-)-vetispiradiene + [reduced NADPH-hemoprotein reductase] + O2 = solavetivol + [oxidized NADPH-hemoprotein reductase] + H2O
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Product in Enzyme-catalyzed Reactions (1 result)
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trans,trans-farnesyl diphosphate = vetispiradiene + diphosphate
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (4 results)
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2.1
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wild type enzyme, in 100 mM Tris-HCl, pH 7.5, at 30°C
3.8
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mutant enzyme V482I, in 100 mM Tris-HCl, pH 7.5, at 30°C
12.7
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mutant enzyme V480I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30°C
20.7
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mutant enzyme V482I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30°C
KM Value (4 results)
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0.0062
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mutant enzyme V482I, in 100 mM Tris-HCl, pH 7.5, at 30°C
0.0084
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mutant enzyme V480I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30°C
0.013
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mutant enzyme V482I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30°C
0.014
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wild type enzyme, in 100 mM Tris-HCl, pH 7.5, at 30°C
References & Links Literature References (1)
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Functional characterization of premnaspirodiene oxygenase, a cytochrome P450 catalyzing regio- and stereo-specific hydroxylations of diverse sesquiterpene substrates
2007
Takahashi, S.; Yeo, Y.S.; Zhao, Y.; O'Maille, P.E.; Greenhagen, B.T.; Noel, J.P.; Coates, R.M.; Chappell, J.
J. Biol. Chem.
282
31744-31754
Links to other databases for (-)-vetispiradiene