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IUBMB CommentsThe enzyme, purified from the California poppy (Eschscholzia californica), is involved in detoxifying the phytoalexin sanguinarine produced by poppy itself (cf. EC 1.5.3.12, dihydrobenzophenanthridine oxidase), when it binds to the cell wall of the poppy cell. The reaction with NADPH is up to three times faster than that with NADH at low concentrations (<10 uM) of the dinucleotide. At higher concentrations the reaction with NADPH is inhibited but not that with NADH .
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chelerythrine + NAD(P)H + H+
dihydrochelerythrine + NAD(P)+
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dihydrochelirubine + NAD(P)+
chelirubine + NAD(P)H + H+
key reaction of benzophenanthridine detoxification. Detoxifying the phytoalexin sanguinarine produced by Eschscholzia californica (California poppy) itself, when it binds to the cell wall of the poppy cell
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ir
dihydrochelirubine + NADP+
chelirubine + NADPH + H+
dihydrochelirubine i.e. 5-methoxy-13-methyl-13,14-dihydro-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridinium. At alkaloid concentration below 0.1 mM, the reaction velocity is about threefold higher with NADPH than with NADH. Higher alkaloid concentrations cause the NADPH-dependent reduction to slow down, but not the NADH-driven reduction
chelirubine i.e. 5-methoxy-13-methyl-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridinium
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ir
dihydrosanguinarine + NAD(P)+
sanguinarine + NAD(P)H + H+
key reaction of benzophenanthridine detoxification. Detoxifying the phytoalexin sanguinarine produced by Eschscholzia californica (California poppy) itself, when it binds to the cell wall of the poppy cell
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ir
dihydrosanguinarine + NAD+
sanguinarine + NADH + H+
dihydrosanguinarine i.e. 13-methyl-13,14-dihydro-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridine. At alkaloid concentration below 0.1 mM, the reaction velocity is about threefold higher with NADPH than with NADH. Higher alkaloid concentrations cause the NADPH-dependent reduction to slow down, but not the NADH-driven reduction
sanguinarine i.e. 13-methyl-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridinium
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ir
dihydrosanguinarine + NADP+
sanguinarine + NADPH + H+
dihydrosanguinarine i.e. 13-methyl-13,14-dihydro-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridine. At alkaloid concentration below 0.1 mM, the reaction velocity is about threefold higher with NADPH than with NADH. Higher alkaloid concentrations cause the NADPH-dependent reduction to slow down, but not the NADH-driven reduction
sanguinarine i.e. 13-methyl-2H,10H-[1,3]dioxolo[4,5-i][1,3]dioxolo[4',5':4,5]benzo[1,2-c]phenanthridinium
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ir
sanguinarine + NADH + H+
dihydrosanguinarine + NAD+
sanguinarine is converted 1.3times faster than chelerythrine. The reduction cannot be reversed by increasing the product concentrations, i.e. even a hundredfold excess of NAD(P)+ does not cause a detectable oxidation of added dihydrosanguinarine
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ir
sanguinarine + NADPH + H+
dihydrosanguinarine + NADP+
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additional information
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additional information
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catalytic mechanism is as follows: the alkanolamine form of sanguinarine is fixed in a binding pocket, mainly consisting of hydrophobic amino acids, by the conserved residue Ser153. Both dioxolane rings of the alkaloid are bound by a triad of H-bonds originating from Cys157 connected to Asp158 and His161 and by the side chain of Lys175. Electron transfer is initiated by attacking the C6 of sanguinarine with the hydride ion of NADPH and the OH group at C6 with a proton originating from Ser153. The anionic form of Ser is then stabilized by the NH3+ group of Lys175. Removal of OH- followed by water formation completes the reduction process
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additional information
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catalytic mechanism is as follows: the alkanolamine form of sanguinarine is fixed in a binding pocket, mainly consisting of hydrophobic amino acids, by the conserved residue Ser153. Both dioxolane rings of the alkaloid are bound by a triad of H-bonds originating from Cys157 connected to Asp158 and His161 and by the side chain of Lys175. Electron transfer is initiated by attacking the C6 of sanguinarine with the hydride ion of NADPH and the OH group at C6 with a proton originating from Ser153. The anionic form of Ser is then stabilized by the NH3+ group of Lys175. Removal of OH- followed by water formation completes the reduction process
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NADH
at alkaloid concentration below 0.1 mM, the reaction velocity is about threefold higher with NADPH than with NADH. Higher alkaloid concentrations cause the NADPH-dependent reduction to slow down, but not the NADH-driven reduction
NADH
below alkaloid substrate concentrations of 10 microM, the reaction velocity is about threefold higher with NADPH than with NADH and increases with the alkaloid concentration. Higher alkaloid concentrations cause the NADPH-dependent reduction to slow down, but not the NADH-driven reduction
NADPH
at alkaloid concentration below 0.1 mM, the reaction velocity is about threefold higher with NADPH than with NADH. Higher alkaloid concentrations cause the NADPH-dependent reduction to slow down, but not the NADH-driven reduction
NADPH
below alkaloid substrate concentrations of 10 microM, the reaction velocity is about threefold higher with NADPH than with NADH and increases with the alkaloid concentration. Higher alkaloid concentrations cause the NADPH-dependent reduction to slow down, but not the NADH-driven reduction
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Weiss, D.; Baumert, A.; Vogel, M.; Roos, W.
Sanguinarine reductase, a key enzyme of benzophenanthridine detoxification
Plant Cell Environ.
29
291-302
2006
Eschscholzia californica (D5JWB3), Eschscholzia californica
brenda
Vogel, M.; Lawson, M.; Sippl, W.; Conrad, U.; Roos, W.
Structure and mechanism of sanguinarine reductase, an enzyme of alkaloid detoxification
J. Biol. Chem.
285
18397-18406
2010
Eschscholzia californica (D5JWB3), Eschscholzia californica
brenda
Mller, H.; Heinze, M.; Heinke, R.; Schmidt, J.; Roos, W.
Self-regulation of phytoalexin production: a non-biosynthetic enzyme controls alkaloid biosynthesis in cultured cells of Eschscholzia californica
Plant Cell Tissue Organ Cult.
119
661-676
2014
Eschscholzia californica (D5JWB3)
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brenda
1.3.1.107 sanguinarine reductase
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