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+ NADPH + H+
? + NADP+
-
-
-
?
1,4-dioxo-2-(trifluoromethyl)-1lambda5,4lambda5-quinoxaline + NADPH + H+
? + NADP+
-
-
-
?
1,4-dioxo-7-(trifluoromethoxy)-1lambda5,2,4lambda5-benzotriazin-3-amine + NADPH + H+
? + NADP+
-
-
-
?
1-oxo-1lambda5,2,4-benzotriazine + NADPH + H+
? + NADP+
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
2 oxidized cytochrome c + NADPH + H+
2 reduced cytochrome c + NADP+
2 oxidized nitroblue tetrazolium + NADPH
2 reduced nitroblue tetrazolium + NADP+ + H+
-
-
-
?
2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone + NADPH
NADP+ + ?
-
i.e. RH1, the enzyme reduces the antitumor drug RH1 to a semiquinone free radical. Following this reduction RH1 undergoes redox cycling under oxic conditions to produce potentially damaging hydroxyl radicals
-
-
?
3-amino-1,4-dioxo-1lambda5,4lambda5-quinoxaline-2-carbonitrile + NADPH + H+
? + NADP+
-
-
-
?
4-nitroacetophenone + NADPH + H+
?
ferricyanide + NADPH + H+
ferrocyanide + NADP+
-
-
-
-
r
ferricytochrome c + azidonitrophenyl-gamma-aminobutyryl-NADPH + H+
ferrocytochrome c + azidonitrophenyl-gamma-aminobutyryl-NADP+
-
-
-
-
r
ferricytochrome c + dithionite
ferrocytochrome c + ?
ferricytochrome c + NADH + H+
ferrocytochrome c + NAD+
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
methyl (1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)carbamate + NADPH + H+
? + NADP+
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)-1,1,1-trifluoromethanesulfonamide + NADPH + H+
? + NADP+
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)acetamide + NADPH + H+
? + NADP+
-
-
-
?
N-(1,4-dioxo-1lambda5,2,4lambda5-benzotriazin-3-yl)methanesulfonamide + NADPH + H+
? + NADP+
-
-
-
?
N-(1-oxo-1lambda5,2,4-benzotriazin-3-yl)acetamide + NADPH + H+
? + NADP+
-
-
-
?
NADH + H+ + ferricytochrome c
NAD+ + ferricytochrome c
-
very low activity with NADH
-
-
?
NADH + H+ + ferricytochrome c
NAD+ + ferrocytochrome c
-
-
-
-
r
NADPH + 5-cyano-2,3-di-p-tolyltetrazolium chloride
NADP+ + (5-cyano-2,3-di-p-tolyltetrazolium chloride) formazan
-
-
formazan is fluorescent
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
NADPH + H+ + 1-[3-(4-phenoxyphenoxy)-2-oxopropyl]indole-5-carboxylic acid
NADP+ + 1-[2-hydroxy-3-(4-phenoxyphenoxy)propyl]indole-5-carboxylic acid
-
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
NADPH + H+ + 2 oxidized cytochrome P450 2B4
NADP+ + 2 reduced cytochrome P450 2B4
-
-
-
?
NADPH + H+ + 2,4,6-trinitrotoluene
NADP+ + nitrite + ?
-
-
-
-
?
NADPH + H+ + 4-nitroacetophenone
?
-
-
-
-
r
NADPH + H+ + 4-nitrobenzaldehyde
?
-
-
-
-
r
NADPH + H+ + 4-nitroso-2,6-dinitrotoluene
NADP+ + 4-hydroxyamino-2,6-dinitrotoluene
-
-
-
-
?
NADPH + H+ + benzalacetone
?
-
-
-
-
r
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
NADPH + H+ + daunorubicin
NADP+ + ?
-
-
-
-
?
NADPH + H+ + dichlorophenolindophenol
NADP+ + reduced dichlorophenolindophenol
-
-
-
?
NADPH + H+ + doxorubicin
NADP+ + 7-deoxydoxorubicinone
-
-
-
?
NADPH + H+ + ferricyanide
NADP+ + ferrocyanide
NADPH + H+ + ferricytochrome b5
NADP+ + ferrocytochrome b5
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
NADPH + H+ + ferrocytochrome b5
NADP+ + ferricytochrome b5
-
-
-
-
?
NADPH + H+ + haloperidol
NADP+ + ?
-
-
-
-
?
NADPH + H+ + menadione
NADP+ + menadiol
NADPH + H+ + n oxidized hemoprotein
NADP+ + n reduced hemoprotein
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
NADPH + H+ + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
NADP+ + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
NADPH + H+ + oxidized 5-cyano-2,3-ditolyl tetrazolium chloride
NADP+ + reduced 5-cyano-2,3-ditolyl tetrazolium chloride
-
-
-
?
NADPH + H+ + oxidized CYP106A1
NADP+ + reduced CYP106A1
NADPH + H+ + oxidized CYP21A2
NADP+ + reduced CYP21A2
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
NADPH + H+ + oxidized eburicol
NADP+ + reduced eburicol
-
-
-
-
?
NADPH + H+ + oxidized lanosterol
NADP+ + reduced lanosterol
-
-
-
-
?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
NADPH + H+ + oxidized tetrazolium
NADP+ + reduced tetrazolium
-
-
-
?
NADPH + H+ + oxidized thiazolyl blue tetrazolium bromide
NADP+ + reduced thiazolyl blue tetrazolium bromide
NADPH + H+ oxidized 2,6-dichlorophenolindophenol
ferrocytochrome c + reduced 2,6-dichlorophenolindophenol
NADPH + hexadecanal
NADP+ + hexadecanol
-
brain, hexadecanal replaceable by p-nitroacetophenone, or p-pyridinecarboxaldehyde, benzalacetone or p-nitrobenzaldehyde
-
?
NADPH + mitoxanthrone
NADP+ + ?
-
-
-
-
?
NADPH + octanal
NADP+ + octanol
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
?
paraquat + NADPH
?
-
paraquat is a toxic herbicide
-
-
?
tirapazamine + NADPH + H+
1,2,4-benzotriazin-3-amine + 1-oxo-1lambda5,2,4-benzotriazin-3-amine + NADP+
-
-
-
?
additional information
?
-
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
lower binding affinity for NADH compared to NADPH
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
3-fold lower activity than with NADPH
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
low rate of internal electron transfer
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: nitroblue tetrazolium salt
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
Coleus scutellarioides
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
Coleus scutellarioides
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
Corbula caribea
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: duroquinone
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: benzylviologen
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: duroquinone
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: benzylviologen
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: benzylviologen
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron donor: azidonitrophenyl-gamma-aminobutyryl-NADPH
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome b5
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: benzoquinone
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: vitamin K3
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: formylated cytochrome c
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
NADPH-cytochrome P450 reductase is a unique universal donor of electrons to practically all known microsomal cytochrome P450s and one of the most important components of the monooxygenase system
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome b5
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: benzoquinone
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: vitamin K3
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
at high ionic strength nonclassical two-site ping pong mechanism, at low ionic strength a sequential bisubstrate mechanism
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: nitroblue tetrazolium salt
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
NADH less than 5% of NADPH activity
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+
-
-
-
?
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+
-
-
-
-
?
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+
-
-
-
-
?
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
component of the cytochrome P450 dependent monooxygenase system
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
Coleus scutellarioides
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
Corbula caribea
-
component of the mixed function oxygenase system
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism, reduced cytochrome P450 is essential for drug metabolism
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism, NADPH-cytochrome P450 deletion mouse is resistant to acetaminophen concentrations at doses toxic for normal mice
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
component of the cytochrome P450 dependent monooxygenase system
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
transfer of electrons during the CYP catalytic cycle
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
CPR shuttles electrons from NADPH through the FAD and FMN-coenzymes into the iron of the prosthetic heme-group of the cytochrome P450
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in the hydroxylation of progesterone at the 11alpha position
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
involved in activation of cytochrome P450 monooxygenase systems
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
involved in activation of cytochrome P450 monooxygenase systems
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 oxidized cytochrome c + NADPH + H+
2 reduced cytochrome c + NADP+
-
-
-
-
?
2 oxidized cytochrome c + NADPH + H+
2 reduced cytochrome c + NADP+
-
-
-
?
4-nitroacetophenone + NADPH + H+
?
-
-
-
-
r
4-nitroacetophenone + NADPH + H+
?
-
-
-
-
r
benzphetamine
?
-
demethylation in the presence of added lipid
-
-
?
benzphetamine
?
-
demethylation in the presence of added lipid
-
-
?
cocaine
?
-
demethylation in the presence of added lipid
-
-
?
cocaine
?
-
demethylation in the presence of added lipid
-
-
?
ferricytochrome c + dithionite
ferrocytochrome c + ?
-
-
-
-
?
ferricytochrome c + dithionite
ferrocytochrome c + ?
-
very low rate of internal electron transfer
-
-
?
ferricytochrome c + NADH + H+
ferrocytochrome c + NAD+
-
-
-
-
r
ferricytochrome c + NADH + H+
ferrocytochrome c + NAD+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
-
-
-
-
r
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
part of the microsomal electron-transport chains and responsible for the transfer of reducing equivalents between NADPH or NADH and cytochrome P-450
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
component of the hydroxylation of lauric acid
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
during hydroxylation of alkanes
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
part of the microsomal electron-transport chains and responsible for the transfer of reducing equivalents between NADPH or NADH and cytochrome P-450
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
during ecdysone hydroxylation
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
during hydroxylation of fatty acids through the bacterial fusion protein P450BM3
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
Coleus scutellarioides
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + ferricyanide
NADP+ + ferrocyanide
-
-
-
-
?
NADPH + H+ + ferricyanide
NADP+ + ferrocyanide
-
-
-
-
?
NADPH + H+ + ferricyanide
NADP+ + ferrocyanide
-
-
-
?
NADPH + H+ + ferricyanide
NADP+ + ferrocyanide
-
-
-
?
NADPH + H+ + ferricyanide
NADP+ + ferrocyanide
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
r
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
-
-
-
?
NADPH + H+ + menadione
NADP+ + menadiol
-
-
-
-
r
NADPH + H+ + menadione
NADP+ + menadiol
-
-
-
-
r
NADPH + H+ + n oxidized hemoprotein
NADP+ + n reduced hemoprotein
-
-
-
-
?
NADPH + H+ + n oxidized hemoprotein
NADP+ + n reduced hemoprotein
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADPH + H+ + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
NADP+ + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
-
-
?
NADPH + H+ + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
NADP+ + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
-
-
-
?
NADPH + H+ + oxidized CYP106A1
NADP+ + reduced CYP106A1
-
-
-
-
?
NADPH + H+ + oxidized CYP106A1
NADP+ + reduced CYP106A1
-
-
-
-
?
NADPH + H+ + oxidized CYP21A2
NADP+ + reduced CYP21A2
-
-
-
-
?
NADPH + H+ + oxidized CYP21A2
NADP+ + reduced CYP21A2
-
-
-
-
?
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
-
-
-
?
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
-
-
-
?
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
-
-
-
?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
-
-
-
-
?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
-
-
-
-
?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
-
-
-
-
?
NADPH + H+ + oxidized thiazolyl blue tetrazolium bromide
NADP+ + reduced thiazolyl blue tetrazolium bromide
-
-
-
-
?
NADPH + H+ + oxidized thiazolyl blue tetrazolium bromide
NADP+ + reduced thiazolyl blue tetrazolium bromide
-
-
-
-
?
NADPH + H+ oxidized 2,6-dichlorophenolindophenol
ferrocytochrome c + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
NADPH + H+ oxidized 2,6-dichlorophenolindophenol
ferrocytochrome c + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
NADPH + O2
NADP+ + O2-
-
slow reaction, presence of menadione, or duroquinone, or vitamin K3 essential
replacement of NADPH by NADH lowers the O2- generation, superoxide anion
?
NADPH + O2
NADP+ + O2-
-
slow reaction, presence of menadione, or duroquinone, or vitamin K3 essential
superoxide anion
?
additional information
?
-
no activity with NADH
-
-
?
additional information
?
-
-
monooxygenase system only present in cells grown on alkanes
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
simultaneous incubation of CYP97C27 and the enzyme with the substrate geranylgeraniol and coenzyme NADPH leads to formation of the product plaunotol
-
-
?
additional information
?
-
-
simultaneous incubation of CYP97C27 and the enzyme with the substrate geranylgeraniol and coenzyme NADPH leads to formation of the product plaunotol
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P450, cytochrome b5 and NADPH cytochrome c P450 reductase
-
-
?
additional information
?
-
-
disruption of redA leads to mutant cells that form yellow mounds that fail to make proper fruiting bodies. The developmental arrest shown by this mutant implicates redA-encoded P450 oxidoreductase in the metabolism of compounds that control cell differentiation
-
-
?
additional information
?
-
-
CYP3A related metabolism in horse is dependent on the expression of the enzyme and also on adequate levels of NADPH P450 reductase and cytochrome b5
-
-
?
additional information
?
-
-
electron transport system composed of cytochrome P-450, cytochrome b5-like hemeproteins, NADPH cytochrome c reductase, and NADH-ferricyanide reductase
-
-
?
additional information
?
-
no activity with NADH
-
-
?
additional information
?
-
no activity with NADH
-
-
?
additional information
?
-
-
no activity with NADH
-
-
?
additional information
?
-
-
hydroxylation of coumarate
-
-
?
additional information
?
-
-
coexpressed with CYP3A4 in insect cell lines, testosterone 6-beta-hydroxylase activity
-
-
?
additional information
?
-
-
coexpressed with two differently modified CYP2D6 cDNAs in Escherichia coli, functional recombinant monooxygenase, bufuralol and metoprolol metabolism
-
-
?
additional information
?
-
-
P450 Red does not contribute to the activation of RH1 (i.e. 2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone) in cells with normal P450 Red activity and plays only a minor role in activating this agent in cells with high levels of this enzyme
-
-
?
additional information
?
-
-
CYPOR is involved in reduction of the prodrug PR-104A
-
-
?
additional information
?
-
-
functional assays studying the effects of specific POR mutations on steroidogenesis shows that several POR variants impair CYP17A1, CYP21A2 and CYP19A1 activities to different degrees
-
-
?
additional information
?
-
-
P450R function is essential for cytochrome P450 activity. The enzyme provides the electrons used in P450-mediated reactions using NADPH as a cofactor. P450R-transfected MDA 231 breast cells display increased sensitivity to mitomycin C and 5-fluorouracil as compared to their empty-vector transfected counterparts. NADPH levels are decreased in P450R-overexpressing cells
-
-
?
additional information
?
-
-
the bioreductive agent RH1 can be reduced by the enzyme. RH1 produces DNA strand breaks and crosslinks in isolated DNA after reduction by P450 Red. P450 Red does not play a significant role in activating RH1 in cells with normal P450 Red activity
-
-
?
additional information
?
-
-
the enzyme donates electrons derived from NADPH to a variety of acceptor proteins, including squalene monooxygenase, 7-dehydro-cholesterol reductase, heme oxygenase, cytochrome b5 , and many microsomal cytochromes P450
-
-
?
additional information
?
-
-
binding of cytochrome P450 2B4 to cytochrome b5 and cytochrome P450 reductase, binding site on cytochrome P450 2B4 for its redox partners, complex formation modelling, overview
-
-
?
additional information
?
-
-
hydroxylation of ecdysone
-
-
?
additional information
?
-
-
monooxygenase system composed of ecdysone 20-monooxygenase, cytochrome P-450 and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
acts as an electron transfer component of the alkane monoxygenase system
-
-
?
additional information
?
-
-
acts as an electron transfer component of the alkane monoxygenase system
-
-
?
additional information
?
-
NADPH-dependent reducing activity for cytochrome c or nitroblue tetrazolium
-
-
?
additional information
?
-
-
NADPH-dependent reducing activity for cytochrome c or nitroblue tetrazolium
-
-
?
additional information
?
-
-
component of the microsomal electron transport system
-
-
?
additional information
?
-
-
CPR, the obligate electron donor for microsomal P450 enzymes, is essential for the bioactivation of many procarcinogens
-
-
?
additional information
?
-
-
deletion of the NADPH-cytochrome P450 reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity
-
-
?
additional information
?
-
-
major effect of POR is on ellipticine detoxication (formation of 9-hydroxyellipticine by microsomal CYPs), and less on its oxidative activation to 12-hydroxy and 13-hydroxyellipticine
-
-
?
additional information
?
-
-
component of the microsomal electron transport system
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
O-deethylation of 7-ethoxycoumarin
-
-
?
additional information
?
-
-
mixed function oxidase system composed of cytochrome P-450, NADPH-cytochrome c reductase and phospholipids, biotransformation of airborne compounds
-
-
?
additional information
?
-
-
simultaneous catalysis of reduction of cytochrome c and hydroxylation of laurate
-
-
?
additional information
?
-
-
part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase
-
-
?
additional information
?
-
fatty-acid-stimulated electron transfer in wild-type and Ala264 mutant flavocytochromes is linked to substrate hydroxylation
-
-
?
additional information
?
-
-
fatty-acid-stimulated electron transfer in wild-type and Ala264 mutant flavocytochromes is linked to substrate hydroxylation
-
-
?
additional information
?
-
-
hydroxylation of benzo-a-pyrene, testosterone and progesterone
-
-
?
additional information
?
-
-
denitration of glyceryl trinitrate
-
-
?
additional information
?
-
-
O-dealkylation of pentoxyresorufin
-
-
?
additional information
?
-
-
component of the electron transport chain required for activity of the 17,20-lyase in testis microsomes, removal of 2-carbon side chain from 17-position of 21-carbon steroids
-
-
?
additional information
?
-
-
involved in the reduction of testosterone
-
-
?
additional information
?
-
-
as part of the microsomal ethanol-oxidizing system composed of NADPH-cytochrome c reductase, cytochrome P-450, phospholipids
-
-
?
additional information
?
-
-
aniline hydroxylase
-
-
?
additional information
?
-
-
N-demethylation of aminopyrine
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
detoxification of drugs, inactivation of procarcinogens
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
?
additional information
?
-
-
microsomal heme oxygenase system composed of heme oxygenase and NADPH-cytochrome c reductase catalyzes the oxidative degradation of heme to biliverdin, essential role in the physiological heme catabolism
-
-
?
additional information
?
-
-
the enzyme also catalyzes the oxidative deformylation of a model xenobiotic aldehyde, 2-phenylpropionaldehyde, to the n-1 alcohol, 1-phenylethanol in the absence of cytochrome P450
-
-
?
additional information
?
-
-
the C-terminal 23 amino acids of heme oxygenase-1 play an important role in the interaction between heme oxygenase-1 and NADPH cytochrome P450 reductase, enhancing the conversion of hemin to biliverdin
-
-
?
additional information
?
-
the presence of NADPH-cytochrome P450 reductase prevents heme oxygenase-1 from acetylation of lysine residues, Lys149 and Lys153, located in the F-helix. The heme degradation activity of the fully acetylated heme oxygenase-1 in the NADPH/NADPH-cytochrome P450 reductase-supported system is significantly reduced, whereas almost no inactivation is detected in heme oxygenase-1 in the presence of NADPH-cytochrome P450 reductase, which prevents acetylation of Lys149 and Lys153
-
-
?
additional information
?
-
-
cytochrome c is the most popular electron acceptor, several dyes and electron acceptors are also in use: dichlorophenol indophenol, ferricyanide and tetrazoliums
-
-
?
additional information
?
-
-
NADPH-cytochrome P450 reductase interacts with heme oxygenase-1
-
-
?
additional information
?
-
-
2,4,6-trinitrophenol, 2,4-dinitrophenol, 2,6-dinitrotoluene, 1,2-dinitrobenzene, 1,4-dinitrobenzene, 2,4-dinitrobenzoic acid, 3,5-dinitrobenzoic acid, 2-nitrotoluene, 2-nitrobenzonitrile, 4-nitrotoluene and 4-nitrobenzaldehyde are not subject to denitration by the enzyme
-
-
?
additional information
?
-
-
detoxification of drugs, inactivation of procarcinogens
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
?
additional information
?
-
-
as part of the microsomal ethanol-oxidizing system composed of NADPH-cytochrome c reductase, cytochrome P-450, phospholipids
-
-
?
additional information
?
-
-
aniline hydroxylase
-
-
?
additional information
?
-
-
N-demethylation of aminopyrine
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
component of the electron transport chain required for activity of the 17,20-lyase in testis microsomes, removal of 2-carbon side chain from 17-position of 21-carbon steroids
-
-
?
additional information
?
-
-
denitration of glyceryl trinitrate
-
-
?
additional information
?
-
-
involved in the reduction of testosterone
-
-
?
additional information
?
-
-
O-dealkylation of pentoxyresorufin
-
-
?
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
involved in the sterol biosynthesis pathways
-
-
?
additional information
?
-
-
involved in the sterol biosynthesis pathways
-
-
?
additional information
?
-
-
mixed-function oxidase system composed of cytochrome P450, NADPH cytochrome P450 reductase and lipid
-
-
?
additional information
?
-
cytochrome P450 monooxygenase gets reducing equivalents from NADPH cytochrome P450 reductase
-
-
?
additional information
?
-
-
cytochrome P450 monooxygenase gets reducing equivalents from NADPH cytochrome P450 reductase
-
-
?
additional information
?
-
-
omega-hydroxylation of fatty acids together with cytochrome P450
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
microsomal heme oxygenase system composed of heme oxygenase and NADPH-cytochrome c reductase catalyzes the oxidative degradation of heme to biliverdin, essential role in the physiological heme catabolism
-
-
?
additional information
?
-
menadione or adrenaline are not reduced
-
-
?
additional information
?
-
menadione or adrenaline are not reduced
-
-
?
additional information
?
-
menadione or adrenaline are not reduced
-
-
?
additional information
?
-
-
menadione or adrenaline are not reduced
-
-
?
additional information
?
-
menadione or adrenaline ate not reduced
-
-
?
additional information
?
-
menadione or adrenaline ate not reduced
-
-
?
additional information
?
-
menadione or adrenaline ate not reduced
-
-
?
additional information
?
-
-
menadione or adrenaline ate not reduced
-
-
?
additional information
?
-
-
oxidation of N-nitrosodimethylamine, N-nitroso-N-methylaniline, aminopyrine and 1-phenylazo-2-naphtol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone + NADPH
NADP+ + ?
-
i.e. RH1, the enzyme reduces the antitumor drug RH1 to a semiquinone free radical. Following this reduction RH1 undergoes redox cycling under oxic conditions to produce potentially damaging hydroxyl radicals
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
NADPH + H+ + n oxidized hemoprotein
NADP+ + n reduced hemoprotein
paraquat + NADPH
?
-
paraquat is a toxic herbicide
-
-
?
additional information
?
-
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
Coleus scutellarioides
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
NADPH-cytochrome P450 reductase is a unique universal donor of electrons to practically all known microsomal cytochrome P450s and one of the most important components of the monooxygenase system
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
component of the cytochrome P450 dependent monooxygenase system
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
Coleus scutellarioides
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
Corbula caribea
-
component of the mixed function oxygenase system
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism, reduced cytochrome P450 is essential for drug metabolism
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in drug metabolism, NADPH-cytochrome P450 deletion mouse is resistant to acetaminophen concentrations at doses toxic for normal mice
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
component of the cytochrome P450 dependent monooxygenase system
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
transfer of electrons during the CYP catalytic cycle
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
involved in the hydroxylation of progesterone at the 11alpha position
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
involved in activation of cytochrome P450 monooxygenase systems
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
involved in activation of cytochrome P450 monooxygenase systems
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
part of the microsomal electron-transport chains and responsible for the transfer of reducing equivalents between NADPH or NADH and cytochrome P-450
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
component of the hydroxylation of lauric acid
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
during hydroxylation of alkanes
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
part of the microsomal electron-transport chains and responsible for the transfer of reducing equivalents between NADPH or NADH and cytochrome P-450
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
during ecdysone hydroxylation
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
during hydroxylation of fatty acids through the bacterial fusion protein P450BM3
-
-
?
NADPH + ferricytochrome P450
ferrocytochrome P450 + NADP+
-
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
?
NADPH + H+ + n oxidized hemoprotein
NADP+ + n reduced hemoprotein
-
-
-
-
?
NADPH + H+ + n oxidized hemoprotein
NADP+ + n reduced hemoprotein
-
-
-
?
additional information
?
-
-
monooxygenase system only present in cells grown on alkanes
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P450, cytochrome b5 and NADPH cytochrome c P450 reductase
-
-
?
additional information
?
-
-
disruption of redA leads to mutant cells that form yellow mounds that fail to make proper fruiting bodies. The developmental arrest shown by this mutant implicates redA-encoded P450 oxidoreductase in the metabolism of compounds that control cell differentiation
-
-
?
additional information
?
-
-
CYP3A related metabolism in horse is dependent on the expression of the enzyme and also on adequate levels of NADPH P450 reductase and cytochrome b5
-
-
?
additional information
?
-
-
electron transport system composed of cytochrome P-450, cytochrome b5-like hemeproteins, NADPH cytochrome c reductase, and NADH-ferricyanide reductase
-
-
?
additional information
?
-
-
P450 Red does not contribute to the activation of RH1 (i.e. 2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone) in cells with normal P450 Red activity and plays only a minor role in activating this agent in cells with high levels of this enzyme
-
-
?
additional information
?
-
-
CYPOR is involved in reduction of the prodrug PR-104A
-
-
?
additional information
?
-
-
functional assays studying the effects of specific POR mutations on steroidogenesis shows that several POR variants impair CYP17A1, CYP21A2 and CYP19A1 activities to different degrees
-
-
?
additional information
?
-
-
P450R function is essential for cytochrome P450 activity. The enzyme provides the electrons used in P450-mediated reactions using NADPH as a cofactor. P450R-transfected MDA 231 breast cells display increased sensitivity to mitomycin C and 5-fluorouracil as compared to their empty-vector transfected counterparts. NADPH levels are decreased in P450R-overexpressing cells
-
-
?
additional information
?
-
-
the bioreductive agent RH1 can be reduced by the enzyme. RH1 produces DNA strand breaks and crosslinks in isolated DNA after reduction by P450 Red. P450 Red does not play a significant role in activating RH1 in cells with normal P450 Red activity
-
-
?
additional information
?
-
-
the enzyme donates electrons derived from NADPH to a variety of acceptor proteins, including squalene monooxygenase, 7-dehydro-cholesterol reductase, heme oxygenase, cytochrome b5 , and many microsomal cytochromes P450
-
-
?
additional information
?
-
-
binding of cytochrome P450 2B4 to cytochrome b5 and cytochrome P450 reductase, binding site on cytochrome P450 2B4 for its redox partners, complex formation modelling, overview
-
-
?
additional information
?
-
-
monooxygenase system composed of ecdysone 20-monooxygenase, cytochrome P-450 and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
acts as an electron transfer component of the alkane monoxygenase system
-
-
?
additional information
?
-
-
acts as an electron transfer component of the alkane monoxygenase system
-
-
?
additional information
?
-
-
component of the microsomal electron transport system
-
-
?
additional information
?
-
-
CPR, the obligate electron donor for microsomal P450 enzymes, is essential for the bioactivation of many procarcinogens
-
-
?
additional information
?
-
-
deletion of the NADPH-cytochrome P450 reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity
-
-
?
additional information
?
-
-
major effect of POR is on ellipticine detoxication (formation of 9-hydroxyellipticine by microsomal CYPs), and less on its oxidative activation to 12-hydroxy and 13-hydroxyellipticine
-
-
?
additional information
?
-
-
component of the microsomal electron transport system
-
-
?
additional information
?
-
-
mixed function oxidase system composed of cytochrome P-450, NADPH-cytochrome c reductase and phospholipids, biotransformation of airborne compounds
-
-
?
additional information
?
-
-
part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase
-
-
?
additional information
?
-
-
detoxification of drugs, inactivation of procarcinogens
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
?
additional information
?
-
-
microsomal heme oxygenase system composed of heme oxygenase and NADPH-cytochrome c reductase catalyzes the oxidative degradation of heme to biliverdin, essential role in the physiological heme catabolism
-
-
?
additional information
?
-
-
the C-terminal 23 amino acids of heme oxygenase-1 play an important role in the interaction between heme oxygenase-1 and NADPH cytochrome P450 reductase, enhancing the conversion of hemin to biliverdin
-
-
?
additional information
?
-
the presence of NADPH-cytochrome P450 reductase prevents heme oxygenase-1 from acetylation of lysine residues, Lys149 and Lys153, located in the F-helix. The heme degradation activity of the fully acetylated heme oxygenase-1 in the NADPH/NADPH-cytochrome P450 reductase-supported system is significantly reduced, whereas almost no inactivation is detected in heme oxygenase-1 in the presence of NADPH-cytochrome P450 reductase, which prevents acetylation of Lys149 and Lys153
-
-
?
additional information
?
-
-
detoxification of drugs, inactivation of procarcinogens
-
-
?
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
?
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
?
additional information
?
-
-
involved in the sterol biosynthesis pathways
-
-
?
additional information
?
-
-
involved in the sterol biosynthesis pathways
-
-
?
additional information
?
-
-
mixed-function oxidase system composed of cytochrome P450, NADPH cytochrome P450 reductase and lipid
-
-
?
additional information
?
-
cytochrome P450 monooxygenase gets reducing equivalents from NADPH cytochrome P450 reductase
-
-
?
additional information
?
-
-
cytochrome P450 monooxygenase gets reducing equivalents from NADPH cytochrome P450 reductase
-
-
?
additional information
?
-
-
microsomal heme oxygenase system composed of heme oxygenase and NADPH-cytochrome c reductase catalyzes the oxidative degradation of heme to biliverdin, essential role in the physiological heme catabolism
-
-
?
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0.31
4-nitrobenzaldehyde
-
-
0.05
5-cyano-2,3-ditolyl tetrazolium chloride
-
-
0.0019
azidonitrophenyl-gamma-aminobutyryl-NADPH
-
-
0.000001 - 0.0466
cytochrome c
7.2
ethanol
-
microsomal ethanol oxidizing system
0.0072 - 0.1193
ferricyanide
0.00087 - 5
ferricytochrome c
0.055 - 0.077
oxidized 2,6-dichlorophenolindophenol
0.0018 - 0.011
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
0.0078
oxidized cytochrome c
at pH 7.8 and 25°C
-
additional information
additional information
-
1.4
4-Nitroacetophenone
-
-
1.4
4-Nitroacetophenone
-
electron donor NADH, electron acceptor dichlorophenolindophenol
0.000001
cytochrome c
wild type, cosubstrate FAD, Km below
0.00012
cytochrome c
T491V mutant, cosubstrate FAD
0.0008
cytochrome c
G488L mutant, cosubstrate FAD
0.0015
cytochrome c
W677X mutant, cosubstrate NADPH
0.0028
cytochrome c
W677Y mutant, cosubstrate NADPH
0.0041
cytochrome c
R454E mutant, cosubstrate NADPH
0.0056
cytochrome c
S678X mutant, cosubstrate NADPH
0.0058
cytochrome c
Y456S mutant, cosubstrate NADPH
0.0059
cytochrome c
T491V mutant, cosubstrate NADPH
0.006
cytochrome c
-
spleen
0.0062
cytochrome c
wild type, cosubstrate NADPH
0.0063
cytochrome c
C472T mutant, cosubstrate NADPH
0.0077
cytochrome c
G488L mutant, cosubstrate NADPH
0.0078
cytochrome c
Y456S mutant, cosubstrate FAD
0.0095
cytochrome c
-
kidney
0.0131
cytochrome c
-
Y140F/178F double mutant
0.0135
cytochrome c
deletion mutant T236/G237
0.0138
cytochrome c
pH 7.5, 25°C
0.014
cytochrome c
-
Y178F mutant
0.015
cytochrome c
deletion mutant T236/G237/E238/E239
0.0178
cytochrome c
-
native enzyme, liver
0.0185
cytochrome c
-
Y178D mutant
0.0188
cytochrome c
-
Y140F mutant
0.0191
cytochrome c
-
Y140D mutant
0.0211
cytochrome c
-
wild type
0.0251
cytochrome c
R454E mutant, cosubstrate FAD
0.0466
cytochrome c
-
cosubstrate NADPH
0.0072
ferricyanide
pH 7.4, 25°C
0.0276
ferricyanide
pH 7.4, 25°C
0.1193
ferricyanide
at pH 7.4 and 25°C
0.00087
ferricytochrome c
-
at pH 7.5 and 25°C
0.0012
ferricytochrome c
isozyme CPR1, at 25°C, pH 7.4
0.0016
ferricytochrome c
isozyme CPR1, at 25°C, pH 7.4
0.002
ferricytochrome c
-
wild type enzyme, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0024
ferricytochrome c
-
mutant enzyme E115A/E116A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0025
ferricytochrome c
-
mutant enzyme D113A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0034
ferricytochrome c
-
mitochondrial reductase
0.0036
ferricytochrome c
-
mutant enzyme E115A/E116A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.004
ferricytochrome c
-
wild type enzyme, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0043
ferricytochrome c
-
grown on glycerol
0.00455
ferricytochrome c
-
grown on alkanes
0.0052
ferricytochrome c
-
mutant enzyme D113A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.006
ferricytochrome c
-
mutant enzyme E115A/E116A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0078
ferricytochrome c
-
-
0.0085
ferricytochrome c
-
wild type enzyme, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0098
ferricytochrome c
pH 7.7, 30°C
0.01
ferricytochrome c
-
-
0.0105
ferricytochrome c
-
microsomal reductase
0.011
ferricytochrome c
-
full length enzyme, pH 7.8, 25°C
0.011
ferricytochrome c
-
mutant enzyme D113A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0117
ferricytochrome c
-
pH 7.5, 41°C
0.012
ferricytochrome c
-
truncated enzyme, pH 7.8, 25°C
0.01282
ferricytochrome c
-
at pH 8.0 and 50°C
0.0129
ferricytochrome c
pH 7.4, 25°C
0.013
ferricytochrome c
-
mutant enzyme E115A/E116A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0159
ferricytochrome c
-
pH 7.6, 25°C
0.016
ferricytochrome c
-
mutant enzyme E115A/E116A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0167
ferricytochrome c
-
at pH 7.5 and 25°C
0.017
ferricytochrome c
pH 7.7, 30°C
0.018
ferricytochrome c
pH 7.7, 30°C
0.0182
ferricytochrome c
-
determined on the basis of a sequential mechanism
0.0189
ferricytochrome c
-
at pH 8.5 and 23°C
0.019
ferricytochrome c
-
wild type enzyme, pH not specified in the publication, at 25°C
0.02
ferricytochrome c
-
wild type enzyme, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.023
ferricytochrome c
-
wild type enzyme, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0239
ferricytochrome c
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C
0.025
ferricytochrome c
-
mutant enzyme D113A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.026
ferricytochrome c
-
mutant enzyme D113A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0372
ferricytochrome c
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0439
ferricytochrome c
-
at pH 7.5 and 23°C
0.048
ferricytochrome c
-
pH 7.7
0.0514
ferricytochrome c
at pH 7.4 and 25°C
0.057
ferricytochrome c
-
-
0.06289
ferricytochrome c
-
-
0.0732
ferricytochrome c
pH 7.4, 25°C
0.0746
ferricytochrome c
-
at pH 9.5 and 23°C
0.081
ferricytochrome c
isoform CPR1, at pH 7.6 and 25°C
0.0924
ferricytochrome c
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.39
ferricytochrome c
-
mutant enzyme R600W
0.92
ferricytochrome c
-
mutant enzyme P452L
0.99
ferricytochrome c
-
mutant enzyme A503V
1.15
ferricytochrome c
-
mutant enzyme P284T
1.19
ferricytochrome c
-
wild-type enzyme
1.37
ferricytochrome c
-
mutant enzyme V472M
1.61
ferricytochrome c
-
mutant enzyme G213E
1.84
ferricytochrome c
-
mutant enzyme A485T
1.86
ferricytochrome c
-
mutant enzyme E300K
2.07
ferricytochrome c
-
mutant enzyme R406H
2.09
ferricytochrome c
-
mutant enzyme A462T
2.16
ferricytochrome c
-
mutant enzyme delE53
2.25
ferricytochrome c
-
mutant enzyme P284L
2.31
ferricytochrome c
-
mutant enzyme P55L
2.5 - 5
ferricytochrome c
-
mutant enzyme D211L
0.0084
NADH
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0108
NADH
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0133
NADH
-
microsomal reductase
4
NADH
-
wild type enzyme, pH not specified in the publication, at 25°C
4.3
NADH
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C
20
NADH
-
mitochondrial reductase
26.76
NADH
-
at pH 7.5 and 25°C
0.000001
NADPH
wild type, cosubstrate FAD, Km below
0.00012
NADPH
T491V mutant, cosubstrate FAD
0.00014
NADPH
mutant enzyme D634N, at pH 7.5 and 25°C
0.00019
NADPH
mutant enzyme D634A, at pH 7.5 and 25°C
0.00031
NADPH
-
mutant enzyme H322A, at pH 7.5 and 25°C
0.00058
NADPH
-
mutant enzyme H322Q, at pH 7.5 and 25°C
0.0007
NADPH
wild type enzyme, at pH 7.5 and 25°C
0.00071
NADPH
-
wild type enzyme, at pH 7.5 and 25°C
0.00071
NADPH
-
at pH 7.5 and 25°C
0.0008
NADPH
G488L mutant, cosubstrate FAD
0.00102
NADPH
-
at pH 7.5 and 25°C
0.00106
NADPH
mutant enzyme A635G, at pH 7.5 and 25°C
0.00106
NADPH
mutant enzyme R636S, at pH 7.5 and 25°C
0.00122
NADPH
-
at pH 7.5 and 25°C
0.0016
NADPH
mutant enzyme R636A, at pH 7.5 and 25°C
0.0017
NADPH
-
mitochondrial reductase
0.0018
NADPH
mutant enzyme A635G/R636S, at pH 7.5 and 25°C
0.0019
NADPH
-
full length enzyme, pH 7.8, 25°C
0.0022
NADPH
pH 7.4, 25°C
0.0022
NADPH
-
truncated enzyme, pH 7.8, 25°C
0.0027
NADPH
deletion mutant T236/G237/E238/E239
0.003
NADPH
deletion mutant T236/G237
0.0037
NADPH
pH 7.4, 25°C
0.0046
NADPH
isozyme CPR1, at 25°C, pH 7.4
0.00506
NADPH
purified recombinant enzyme, pH 7.8, 25°C
0.005208
NADPH
-
at pH 8.0 and 50°C
0.0055
NADPH
-
microsomal reductase
0.0056
NADPH
isozyme CPR1, at 25°C, pH 7.4
0.00577
NADPH
pH 7.7, 30°C
0.0064
NADPH
-
wild type, cosubstrate cytochrome c
0.00648
NADPH
purified recombinant enzyme, pH 7.8, 25°C
0.0066
NADPH
-
native enzyme, liver, cosubstrate cytochrome c
0.0066
NADPH
-
Y140D mutant, cosubstrate cytochrome c
0.0071
NADPH
-
Y178F mutant, cosubstrate cytochrome c
0.0078
NADPH
-
Y140F mutant, cosubstrate cytochrome c
0.0078
NADPH
Y456S mutant, cosubstrate FAD
0.0085
NADPH
W677X mutant, cosubstrate cytochrome c
0.0086
NADPH
-
at pH 7.5 and 25°C
0.0094
NADPH
-
pH 7.5, 41°C
0.0095
NADPH
-
Y178D mutant, cosubstrate cytochrome c
0.0114
NADPH
-
Y140F/178F double mutant, cosubstrate cytochrome c
0.0116
NADPH
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C
0.0125
NADPH
-
wild type enzyme, pH not specified in the publication, at 25°C
0.0129
NADPH
-
pH 7.6, 25°C
0.0134
NADPH
G488L mutant, cosubstrate cytochrome c
0.0143
NADPH
W677Y mutant, cosubstrate cytochrome c
0.0163
NADPH
wild type, cosubstrate cytochrome c
0.0166
NADPH
R454E mutant, cosubstrate cytochrome c
0.0187
NADPH
at pH 7.4 and 25°C
0.0192
NADPH
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0199
NADPH
S678X mutant, cosubstrate cytochrome c
0.0201
NADPH
T491V mutant, cosubstrate cytochrome c
0.0217
NADPH
C472T mutant, cosubstrate cytochrome c
0.025
NADPH
-
mutant enzyme Y607C
0.0251
NADPH
R454E mutant, cosubstrate FAD
0.029
NADPH
-
grown on alkanes
0.0308
NADPH
-
determined on the basis of a sequential mechanism
0.033
NADPH
-
grown on glycerol
0.0341
NADPH
-
cosubstrate cytochrome c
0.0425
NADPH
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.05
NADPH
Coleus scutellarioides
-
0.05
NADPH
Coleus scutellarioides
recombinant yeast microsomal CPR, pH 7.5, 35°C
0.0511
NADPH
pH 7.7, 30°C
0.0548
NADPH
Y456S mutant, cosubstrate cytochrome c
0.05488
NADPH
pH 7.7, 30°C
0.066
NADPH
-
mutant enzyme P284T
0.084
NADPH
-
mutant enzyme R600W
0.125
NADPH
-
mutant enzyme P452L
0.144
NADPH
-
wild-type enzyme
0.144
NADPH
-
mutant enzyme A485T
0.146
NADPH
-
mutant enzyme P55L
0.151
NADPH
-
mutant enzyme delE53
0.153
NADPH
-
mutant enzyme D211L
0.155
NADPH
-
mutant enzyme A503V
0.157
NADPH
-
mutant enzyme P284L
0.169
NADPH
-
mutant enzyme V472M
0.177
NADPH
-
mutant enzyme R406H
0.196
NADPH
-
mutant enzyme G213E
0.215
NADPH
Coleus scutellarioides
recombinant yeast internal CPR, pH 7.5, 35°C
0.222
NADPH
-
mutant enzyme E300K
0.276
NADPH
-
mutant enzyme A462T
0.055
oxidized 2,6-dichlorophenolindophenol
-
grown on glycerol
0.077
oxidized 2,6-dichlorophenolindophenol
-
grown on alkanes
0.0018
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0021
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0022
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0026
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0026
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0031
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0038
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0039
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0041
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0062
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0063
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0065
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.0087
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme D113A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.01
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
wild type enzyme, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.011
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
-
mutant enzyme E115A/E116A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
additional information
additional information
-
-
-
additional information
additional information
-
cosubstrate NADH, biphasic kinetic
-
additional information
additional information
-
O2-generation
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
kinetic mechanism, overview
-
additional information
additional information
-
kinetic mechanism, overview
-
additional information
additional information
CsCPR displays Michaelis-Menten behavior with respect to both cytochrome c and NADPH
-
additional information
additional information
-
kinetics by stopped-flow spectroscopy
-
additional information
additional information
steady-state kinetics of P450 enzyme reactions supported by Malassezia globosa NPR, overview
-
additional information
additional information
-
steady-state kinetics of P450 enzyme reactions supported by Malassezia globosa NPR, overview
-
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L86F/L219F
-
the mutant upon reconstitution with the Anopheles minimus cytochrome P450 CYP6AA3 and a NADPH-regenerating system, increases CYP6AA3-mediated deltamethrin degradation compared to the wild type enzyme
L86F/L219F/P456A
-
increased stability with significant reduction in aggregation compared to the wild-type enzyme. The triple mutant is purified in high yield with stoichiometries of 0.97 FMN and 0.55 FAD (compared to 0.92 FMN and 1.05 FAD for wild-type enzyme). Deficiency in FAD content is overcome by addition of exogenous FAD to the enzyme. Both wild-type and the triple mutant follow a two-site ping-pong mechanism with similar kinetic constants
P456A
-
mutant enzyme contains 0.28 FMN and 0.5 FAD compared to 0.5 FMN and 1.05 FAD for wild-type enzyme
A115V
-
Vmax/Km for cytochrome c is 63% of wild-type value, Vmax/Km for NADPH is 41% of wild-type value
A457H
-
the POR mutant is associated with total loss of heme oxygenase-1 activity
A462T
-
vmax/Km for ferricytochrome c is 85% of the wild-type value. Vmax/Km for NADPH is 69% of the wild-type value
A485T
-
vmax/Km for ferricytochrome c is 36% of the wild-type value. Vmax/Km for NADPH is 51% of the wild-type value
A635G/R636S
the mutations lead to a modest increase in cytochrome c reduction, which is linked to weaker coenzyme binding and faster interflavin electron transfer
D211L
-
vmax/Km for ferricytochrome c is 27% of the wild-type value. Vmax/Km for NADPH is 59% of the wild-type value
D634A
the variant elicits a modest increase in coenzyme binding affinity coupled with a 36fold reduction in cytochrome c turnover and a 17fold decrease in the pre-steady state rate of flavin reduction
D634N
the variant elicits a modest increase in coenzyme binding affinity coupled with a 10fold reduction in cytochrome c turnover and a 3fold decrease in the pre-steady state rate of flavin reduction
delE53
-
vmax/Km for ferricytochrome c is 57% of the wild-type value. Vmax/Km for NADPH is 93% of the wild-type value
delT236_I242
-
either deletion of a 7 amino acid long segment or its replacement by polyproline repeats (5 and 10 residues) results in a significant increase in 2',5'-ADP enthalpy of binding. This is accompanied by a decrease in the number of thermodynamic microstates available for the ligand-cytochrome P450 reductase complex. The estimated heat capacity change for this interaction changes from -220 cal/mol*K in the wild-type enzyme to -580 cal/mol*K in the deletion mutant. Presteady-state kinetics measurements reveal a 50fold decrease in the microscopic rate for interdomain (FAD/FMN) electron transfer in the deletion mutant. Multiple turnover cytochome c reduction assays indicate that these mutations impair the ability of the FMN-binding domain to shuttle electrons from the FAD-binding domain to the cytochrome partner
delT236_I242ins(Pro)10
-
either deletion of a 7 amino acid long segment or its replacement by polyproline repeats (5 and 10 residues) results in a significant increase in 2',5'-ADP enthalpy of binding. This is accompanied by a decrease in the number of thermodynamic microstates available for the ligand-cytochrome P450 reductase complex
delT236_I242ins(Pro)5
-
either deletion of a 7 amino acid long segment or its replacement by polyproline repeats (5 and 10 residues) results in a significant increase in 2',5'-ADP enthalpy of binding. This is accompanied by a decrease in the number of thermodynamic microstates available for the ligand-cytochrome P450 reductase complex
DELTAD675/DELTAV676
tandem deletion variant, about 16% of wild-type activity
DELTAS678
deletion of Ser678 has no effect on cytochrome c reductase activity or Km values for NADPH or cytochrome c
DELTAV676
repositioning of Trp677 by deletion of Val676 decreases cytochrome c reductase activity, to about 6% of wild-type levels
E300K
-
vmax/Km for ferricytochrome c is 93% of the wild-type value. Vmax/Km for NADPH is 104% of the wild-type value
F646del
-
Vmax/Km for cytochrome c is 36% of wild-type value, Vmax/Km for NADPH is 94% of wild-type value
G213E
-
vmax/Km for ferricytochrome c is 111% of the wild-type value. Vmax/Km for NADPH is 105% of the wild-type value
G240P
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
G539R
-
Vmax/Km for cytochrome c is 9% of wild-type value, Vmax/Km for NADPH is 0.2% of wild-type value
H322Ala
-
the mutation does not affect the rate of NADPH hydride transfer or the FAD redox potentials, but does impede interflavin electron transfer. The mutant elicits a 4fold decrease in cytochrome c reduction and a 1.5fold decrease in ferricyanide reduction. The H322A substitution also leads to a modest increase in NADP(H) binding affinity, evidenced by a 2-3fold reduction in the Km for NADPH and Ki for NADP+
H322Q
-
the mutant shows a 50% decrease in cytochrome c and ferricyanide reduction and a marginal increase in NADP(H) binding affinity compared to the wild type enzyme
H628P
-
mutation results in similar disruption of CYP17A1 and CYP21A2 activities
I245A
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
I245A/R246A
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
I245P
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
I245R/R246I
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
L565P
-
Vmax/Km for cytochrome c is 14% of wild-type value, Vmax/Km for NADPH is 1.4% of wild-type value
M263V
-
Vmax/Km for cytochrome c is 76% of wild-type value, Vmax/Km for NADPH is 57% of wild-type value
P284L
-
vmax/Km for ferricytochrome c is 104% of the wild-type value. Vmax/Km for NADPH is 153% of the wild-type value
P284T
-
vmax/Km for ferricytochrome c is 16% of the wild-type value. Vmax/Km for NADPH is 32% of the wild-type value
P452L
-
vmax/Km for ferricytochrome c is 16% of the wild-type value. Vmax/Km for NADPH is 12% of the wild-type value
P55L
-
vmax/Km for ferricytochrome c is 67% of the wild-type value. Vmax/Km for NADPH is 123% of the wild-type value
Q153R
-
Vmax/Km for cytochrome c is 9% of wild-type value, Vmax/Km for NADPH is 11% of wild-type value
R246A
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
R246P
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
R406H
-
vmax/Km for ferricytochrome c is 62% of the wild-type value. Vmax/Km for NADPH is 78% of the wild-type value
R600W
-
vmax/Km for ferricytochrome c is 18% of the wild-type value. Vmax/Km for NADPH is 7% of the wild-type value
R616X
-
the POR mutant is associated with total loss of heme oxygenase-1 activity
R636A
the mutation leads to a modest increase in cytochrome c reduction, which is linked to weaker coenzyme binding and faster interflavin electron transfer
R636S
the mutation leads to a modest increase in cytochrome c reduction, which is linked to weaker coenzyme binding and faster interflavin electron transfer
S243P
mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations
S244C
-
mutation results in similar disruption of CYP17A1 and CYP21A2 activities
T142A
-
Vmax/Km for cytochrome c is 49% of wild-type value, Vmax/Km for NADPH is 52% of wild-type value
V472M
-
vmax/Km for ferricytochrome c is 23% of the wild-type value. Vmax/Km for NADPH is 24% of the wild-type value
V631I
-
Vmax/Km for cytochrome c is 74% of wild-type value, Vmax/Km for NADPH is 23% of wild-type value
W676H
-
rate of FAD-reduction is modestly affected, enzyme is reduced only to the two-electron level in rapid mixing experiments
W677A
substitution of Trp677 decreases NADPH-dependent cytochrome c reductase activity 25- to 55fold. W677A substitution abolishes the decrease in cytochrome c reductase activity at low pH
W677G
substitution of Trp677 decreases NADPH-dependent cytochrome c reductase activity 25- to 55fold. W677G substitution exhibits only a slight decrease in activity at low pH
W677G/S678X
W677G/S678X substitution exhibits only a slight decrease in activity at low pH
Y607C
-
Vmax/Km for NADPH is 20% of the wild-type value
DELTA1-23
-
truncated enzyme
A264C
no notable decreases in expression of the respective haem domains or flavocytochromes. For A264C haem domain, fatty-acid-induced perturbation of the spinstate equilibrium is observed in some cases, but the extent of high-spin conversion is substantially less than observed for wild-type with arachidonate
A264M
higher dodecanoate affinity than wild-type BM3. For the A264M mutant, a more substantial fatty-acid-induced high-spin conversion of haem iron is observed than for A264C, albeit slightly less than for wild-type with the same fatty acids.
A264Q
no notable decreases in expression of the respective haem domains or flavocytochromes
C136A
site-directed mutagenesis
C228A
site-directed mutagenesis
C363T
site-directed mutagenesis
C445L
site-directed mutagenesis
C566A
site-directed mutagenesis, the mutant shows full catalytic activity and a 2.5fold increased Km for NADPH compared to the wild-type enzyme
D113A
-
the mutation increases kcat approximately 2fold, but does not affect Km at the lowest ionic strength (10 mM), the mutant displays no change in catalytic efficiency compared to the wild type enzyme
E115A/E116A
-
the mutations increase kcat approximately 2fold, but does not affect Km at the lowest ionic strength (10 mM), the mutant displays a slight decrease in catalytic efficiency at higher ionic strengths due to a larger increase in Km than observed for kcat
E238A/E239A
hinge region connecting the FMN domain to the rest of the protein
G237/+AA/E238
hinge region connecting the FMN domain to the rest of the protein
G237/+AAAA/238
hinge region connecting the FMN domain to the rest of the protein
G488L
substitution decreases FAD binding by approximately 80% but does not affect FMN incorporation, 42fold decrease in catalytic activity compared to wild type, substitution does not affect either Km for NADPH or Km for cytochrome c, addition of FAD to the mutant results in partial restoration of catalytic activity
K56Q
-
the full-length mutant enzyme is stable to spontaneopus proteolysis but possesses spectral and catzalytic properties of the wild-type flavoprotein
R454E
substitution decreases both FAD binding and FMN incorporation, suggesting interaction between the two flavin domains and/or the interconnecting region, FAD content ranged from undetectable to approximately 0.1 mol of FAD/mol of enzyme, 338fold decrease in catalytic activity compared to wild type, substitution does not affect either Km for NADPH or Km for cytochrome c, addition of FAD to the mutant resulted in partial restoration of catalytic activity
S457A/C630A/D675N
site-directed mutagenesis, catalytically inactive mutant possessing a structure almost identical to that of the wild-type
S678X
substitution does not affect FAD or FMN incorporation, substitution has no effect on the catalytic activity or kinetic properties
T236A/G237A/E238A/E239A
hinge region connecting the FMN domain to the rest of the protein
T491V
substitution decreases FAD binding by approximately 50% but does not affect FMN incorporation, 2fold decrease in catalytic activity compared to wild type, substitution does not affect either Km for NADPH or Km for cytochrome c, addition of FAD to the mutant results in full restoration of catalytic activity
W677X
substitution does not affect FAD or FMN incorporation, 34fold decrease in catalytic activity compared to wild type, substitution does not alter significantly Km for cytochrome c but decreases Km for NADPH
W677Y
substitution does not affect FAD or FMN incorporation, 2fold decrease in catalytic activity compared to wild type, substitution does not alter significantly Km for cytochrome c but decreases Km for NADPH
Y140D
-
substitution does not eliminate FMN binding but reduces cytochrome c reductase activity, Km value for cytochrome c or NADPH similar to wild type
Y140D/178D
-
substitution abolishes FMN binding and cytochrome c reductase activity
Y140F
-
substitution has no effect on FMN content or catalytic activity, Km value for cytochrome c or NADPH similar to wild type
Y140F/178F
-
substitution has no effect on FMN content or catalytic activity, slightly decreases Km for cytochrome c, NADPH Km value slightly higher than wild type
Y178D
-
substitution abolishes FMN binding and cytochrome c reductase activity, Km value for cytochrome c similar to wild type, NADPH Km value slightly higher than wild type
Y178F
-
substitution has no effect on FMN content or catalytic activity, slightly decreases Km for cytochrome c, NADPH Km value similar to wild type
Y456S
substitution decreases FAD binding but did not affect FMN incorporation, 250fold decrease in catalytic activity compared to wild type, substitution increases Km for cytochrome c, addition of FAD to the mutant results in full restoration of catalytic activity
L219F
-
mutant enzyme contains 0.83 FMN and 0.5 FAD compared to 0.53 FMN and 1.05 FAD for wild-type enzyme
L219F
-
the mutant upon reconstitution with the Anopheles minimus cytochrome P450 CYP6AA3 and a NADPH-regenerating system, increases CYP6AA3-mediated deltamethrin degradation compared to the wild type enzyme
L86F
-
mutant enzyme contains 0.83 FMN and 0.5 FAD compared to 0.92 FMN and 1.05 FAD for wild-type enzyme
L86F
-
the mutant upon reconstitution with the Anopheles minimus cytochrome P450 CYP6AA3 and a NADPH-regenerating system, increases CYP6AA3-mediated deltamethrin degradation compared to the wild type enzyme
A287P
-
preferential inhibition of CYP17A1 over CYP21A2
A287P
-
Vmax/Km for cytochrome c is 9% of wild-type value, Vmax/Km for NADPH is 16% of wild-type value
A287P
-
the POR mutant is associated with 75-80% of normal heme oxygenase-1 activity
A503V
-
Vmax/Km for cytochrome c is 69% of wild-type value, Vmax/Km for NADPH is 86% of wild-type value
A503V
-
vmax/Km for ferricytochrome c is 67% of the wild-type value. Vmax/Km for NADPH is 56% of the wild-type value
A503V
-
the POR mutant is associated with close to wild type activity of heme oxygenase-1
C569Y
-
Vmax/Km for cytochrome c is 6% of wild-type value, Vmax/Km for NADPH is 2% of wild-type value
C569Y
-
the POR mutant is associated with 75-80% of normal heme oxygenase-1 activity
G413S
-
Vmax/Km for cytochrome c is 76% of wild-type value, Vmax/Km for NADPH is identical to wild-type value
G413S
-
the POR mutant is associated with close to wild type activity of heme oxygenase-1
G504R
-
Vmax/Km for cytochrome c is 53% of wild-type value, Vmax/Km for NADPH is 47% of wild-type value
G504R
-
the POR mutant is associated with close to wild type activity of heme oxygenase-1
P228L
-
Vmax/Km for cytochrome c is 75% of wild-type value, Vmax/Km for NADPH is 72% of wild-type value
P228L
-
the POR mutant is associated with close to wild type activity of heme oxygenase-1
R316W
-
Vmax/Km for cytochrome c is 61% of wild-type value, Vmax/Km for NADPH is 77% of wild-type value
R316W
-
the POR mutant is associated with close to wild type activity of heme oxygenase-1
R457H
-
Vmax/Km for cytochrome c is 0.7% of wild-type value
R457H
mutation in the FAD domain
V492E
-
mutation causes Antley-Bixler syndrome due to diminished binding of the FAD cofactor. Activity is restored by the addition of FAD
V492E
-
Vmax/Km for cytochrome c is 0.3% of wild-type value
V492E
mutation in the FAD domain
V492E
-
the POR mutant is associated with total loss of heme oxygenase-1 activity
V608F
-
Vmax/Km for cytochrome c is 8% of wild-type value, Vmax/Km for NADPH is 3% of wild-type value
V608F
-
the POR mutant is associated with 75-80% of normal heme oxygenase-1 activity
Y181D
-
mutation results in similar disruption of CYP17A1 and CYP21A2 activities
Y181D
-
the POR mutant is associated with total loss of heme oxygenase-1 activity
Y459H
-
mutation causes Antley-Bixler syndrome due to diminished binding of the FAD cofactor. Activity is restored by the addition of FAD
Y459H
-
Vmax/Km for cytochrome c is 0.4% of wild-type value
Y459H
-
the POR mutant is associated with total loss of heme oxygenase-1 activity
C472T
site-directed mutagenesis
C472T
substitution does not affect FAD or FMN incorporation, substitution has no effect on activity, Km for NADPH or Km for cytochrome c
additional information
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DELTA55AnCYPOR has an approximately 0.5fold increased FAD content compared to the wild type enzyme
additional information
-
chimeric protein: yeast FMN (residues 44-211) and human connecting/FAD (residues 232-677) domain
additional information
-
deletion of 11 amino acids of the membrane anchor yields a cytosolic protein that does not bind to the endoplasmic reticulum, whereas lengthening the membrane anchor by 5 amino acids causes the protein to be transported to the plasma membrane of COS cells
additional information
-
knock-down CYPOR in multiple osteoblast cell lines using RNAi technology decreasing the expression of Connexin 43, known to play a critical role in bone formation, modeling, and remodeling. Knock-down of CYPOR also decreases Gap Junction Intercellular Communication (GJIC) and hemichannel activity
additional information
replacement of all seven cysteine residues, no gross effect is observed on FMN and FAD binding and electron transfer from NADPH. Cytochrome c reduction is decreased to 2% of wild-type. Introduction of Cys residues S9C, S32C, S55C, T668C to the Cys-less mutant shows substantial conformational changes upon membrane reconstitution of mutant, while liposome insertion has little effect on the T668C
additional information
specific residues of the hinge segment are important in the control of the conformational equilibrium of CPR. Mutations in residues G240, S243, I245 and R246 of the hinge segment, are capable of reducing cytochrome c yet with different efficiency and their maximal rates of cytochrome c reduction are shifted to lower salt concentration. Residue R246 seems to play a key role in a salt bridge network present at the interface of the hinge and the connecting domain
additional information
the deletion of more than 29 residues from the N-terminus of CYPOR decreases cytochrome P450 activity concomitant with alterations in electrophoretic mobility and an increased resistance to protease digestion. The altered kinetic properties of these mutants are consistent with electron transfer through random collisions rather than via formation of a stable CYPOR-P450 complex
additional information
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comparison of enzyme gene expression in enterocytes isolated from the small intestine of intestinal epithelium-specific Por knock-out mice, i.e. IE-Cpr-null mice, and that observed in wild-type littermates, overview. Cholesterol biosynthetic activity is greatly reduced in the enterocytes of the IE-Cpr-null mice, as evidenced by the accumulation of the lanosterol metabolite, 24-dihydrolanosterol. Levels of the cholesterol precursor farnesyl diphosphate and its derivative geranylgeranyl pyrophosphate are also increased in the enterocytes of the IE-Cpr-null mice. Expression of STAT1 (signal transducer and activator of transcription 1), a downstream target of geranylgeranyl pyrophosphate signaling, is enhanced
additional information
-
knock-down CYPOR in multiple osteoblast cell lines using RNAi technology decreasing the expression of Connexin 43, known to play a critical role in bone formation, modeling, and remodeling. Knock-down of CYPOR also decreases Gap Junction Intercellular Communication (GJIC) and hemichannel activity
additional information
mutations at residue 264 in the haem (P450) domain of the enzyme lead to novel amino acid sixth (distal) co-ordination ligands to the haem iron
additional information
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mutations at residue 264 in the haem (P450) domain of the enzyme lead to novel amino acid sixth (distal) co-ordination ligands to the haem iron
additional information
the position of the amino acid 264 side chain (even in enzymes or subpopulations thereof where the residue does not ligate the haem iron) probably interferes with catalytically productive substrate docking
additional information
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the position of the amino acid 264 side chain (even in enzymes or subpopulations thereof where the residue does not ligate the haem iron) probably interferes with catalytically productive substrate docking
additional information
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FMN-depleted enzyme is prepared by dialyzing the mutant enzyme Y140A/Y178A, against 2 M KBr. FMN-depleted enzyme can support the conversion of verdoheme to the ferric biliverdin-iron chelate, indicating that electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN
additional information
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The removal of the N-terminal hydrophobic sequence of NADPH-cytochrome P450 reductase results in loss of the ability of the flavoprotein to interact and transfer electrons to cytochrome P450. Truncated forms of the flavoprotein (residue 46-676 of the mutant (Q56Q) or 57-676 of the wild-type NADPH-cytochrome P450 reductase) are unable to transfer electrons to cytochrome P450c17 or P4503A4
additional information
deletion mutants in the hinge region (connecting the FMN domain to the rest of the protein): deletion of T236 and G237 or deletion of T236, G237, E238 and E239, also in combination with deletion of the first 56 residues of the N-terminus (resulting in a soluble protein)
additional information
generation of a truncated -56 mutant form W677X of the rat 147CC514, with Trp677 and Ser678 truncated, the mutant exhibits decreased NADP+ binding and alterations in the conformation of the NADP+-binding site
additional information
chimeric protein: yeast FMN (residues 44-211) and human connecting/FAD (residues 232-677) domain
additional information
Saccharomyces cerevisiae /Homo sapiens
chimeric protein: yeast FMN domain (residues 44-211) and human FAD domain (residues 232-677)
additional information
truncation f the N-terminal putative membrane anchor leads to increased activity in reducing cytochrome c as compared to the wild-type enzyme, overview
additional information
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truncation f the N-terminal putative membrane anchor leads to increased activity in reducing cytochrome c as compared to the wild-type enzyme, overview
additional information
-
truncation f the N-terminal putative membrane anchor leads to increased activity in reducing cytochrome c as compared to the wild-type enzyme, overview
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