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Ligand (S)-coreximine Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C1 9 H2 1 NO4
(S)-coreximine
BWUQAWCUJMATJS-HNNXBMFYSA-N
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (3 results)
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(S)-coreximine + [reduced NADPH-hemoprotein reductase] + O2 = (S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
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(S)-coreximine + [reduced NADPH-hemoprotein reductase] + O2 = (S)-cheilanthifoline + [oxidized NADPH-hemoprotein reductase] + H2O
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(S)-coreximine + O2 = (13aS)-2,11-dihydroxy-3,10-dimethoxy-5,8,13,13a-tetrahydroisoquinolino[3,2-a]isoquinolin-7-ium + H2O2
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Product in Enzyme-catalyzed Reactions (1 result)
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reticuline + O2 = (S)-scoulerine + (S)-coreximine + H2O2
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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50% inhibition at 0.2 mM
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Enzyme Kinetic Parameters
References & Links Literature References (3)
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Purification and characterization of the berberine bridge enzyme from Berberis beaniana cell cultures
1985
Steffens, P.; Nagakura, N.; Zenk, M.H.
Phytochemistry
24
2577-2583
Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana
2011
Diaz Chavez, M.L.; Rolf, M.; Gesell, A.; Kutchan, T.M.
Arch. Biochem. Biophys.
507
186-193
Isotope effects suggest a stepwise mechanism for berberine bridge enzyme
2012
Gaweska, H.M.; Roberts, K.M.; Fitzpatrick, P.F.
Biochemistry
51
7342-7347
Links to other databases for (S)-coreximine