1.3.1.107: sanguinarine reductase
This is an abbreviated version!
For detailed information about sanguinarine reductase, go to the full flat file.
Reaction
Synonyms
SARED1
ECTree
1.3.1.107 sanguinarine reductaseAdvanced search results
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Substrates Products on EC 1.3.1.107 - sanguinarine reductase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chelerythrine + NAD(P)H + H+
dihydrochelerythrine + NAD(P)+
-
-
-
?
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
-
-
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
-
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
-
-
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
-
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
-
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
-
-
ir
sanguinarine + NADPH + H+
dihydrosanguinarine + NADP+
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
