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Enzyme Nomenclature
Information on EC 1.6.2.4 - NADPH-hemoprotein reductase
Word Map on EC 1.6.2.4
- 1.6.2.4
- hepatic
-
monooxygenase
- heme
- fmn
-
xenobiotics
- flavoproteins
- phenobarbital
- testosterone
-
benzoapyrene
- cyp3a4
- semiquinone
- benzphetamine
-
one-electron
- aniline
-
nadh-cytochrome
-
bioreductive
- dt-diaphorase
- 7-ethoxycoumarin
- aminopyrine
-
drug-metabolizing
- cyp2e1
- 3-methylcholanthrene
-
phenobarbital-induced
-
o-deethylation
- n-demethylase
-
p-450-dependent
- androstenedione
- 21-hydroxylase
-
mixed-function
- beta-naphthoflavone
- metyrapone
- ethylmorphine
- cumene
-
phenobarbital-treated
- 7-ethoxyresorufin
-
p450-mediated
- 7,8-benzoflavone
-
p450-catalyzed
-
omega-hydroxylation
-
nitroreduction
-
p-nitroanisole
-
17alpha-hydroxylase
-
o-dealkylation
-
n-nitrosodimethylamine
- cyp17a1
- biotechnology
- chlorzoxazone
-
6beta-hydroxylation
-
2-amino-3-methylimidazo4,5-fquinoline
- medicine
- bufuralol
- cyp21a2
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.6.2.4
-
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RECOMMENDED NAME
GeneOntology No.
NADPH-hemoprotein reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
-
-
-
-
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
at high ionic strength nonclassical two-site ping pong mechanism, at low ionic strength a sequential bisubstrate mechanism
-
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
catalytic cycle and the rate-limiting step, which is at or after the introduction of the second electron from the reductase to the heme iron
-
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
catalytic cycle and the rate-limiting step, which is at or after the introduction of the second electron from the reductase to the heme iron
-
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
kinetic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NADPH:hemoprotein oxidoreductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases (e.g. EC 1.14.14.1, unspecific monooxygenase) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. It also reduces cytochrome b5 and cytochrome c. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
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CAS REGISTRY NUMBER
COMMENTARY
9023-03-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Corbula caribea
significant activity only in organisms isolated from oil seep site, very low activity in organisms from control site
-
-
e.g. maize, potato, avocado, bramble, tulip, leek, Vicia faba, sunflower, bramble, Gingko biloba
-
-
Sprague-Dawley strain
-
-
-
288545, 288550, 288555, 288559, 288573, 288575, 288576, 288579, 288582, 288591, 288592, 288603, 288609
-
-
-
288589, 288614, 288617, 288618, 657897, 657914, 658621, 658948, 659978, 671348, 671680, 672881, 672891, 673808, 675071, 676960, 684718, 685027, 685178, 685942, 686398, 686709, 686851, 686913, 687959, 688993, 689794, 690133, 697592, 699733, 711112, 711152, 711717, 712406, 712656, 713542, 713594, 724112, 724127, 724179, 726266
-
-
a transgenic mouse model, with the NADPH-P450 reductase (Cpr) gene deleted in a lung-specific and doxycycline-inducible fashion (lung-Cpr-null)
-
-
-
288550, 288552, 288573, 288575, 288587, 288590, 288595, 288602, 288619, 438257, 672278, 676967, 686350, 686851, 689883, 696115, 696311, 696907, 700369, 711106, 711305, 711313, 713542, 724127, 724313
-
-
Sprague-Dawley strain
-
-
Saccharomyces cerevisiae /Homo sapiens chimeric protein
Uniprot
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme is a member of the diflavin oxidoreductase family. They are multi-domain enzymes containing distinct FAD and FMN domains connected by a flexible hinge. The protein has evolved by fusing two ancestral genes that encode proteins related to a FMN-containing flavodoxin and a FAD-containing ferredoxin-NADP+ oxidoreductase
evolution
-
the enzyme is a member of the diflavin oxidoreductase family. They are multi-domain enzymes containing distinct FAD and FMN domains connected by a flexible hinge. The protein has evolved by fusing two ancestral genes that encode proteins related to a FMN-containing flavodoxin and a FAD-containing ferredoxin-NADP+ oxidoreductase
evolution
chicken POR shares high homology with other vertebrates PORs and possesses the conserved binding domains of FAD, FMN, and NADPH
evolution
-
Spodoptera littoralis P450s belong to four clades defined by their conservation with vertebrate P450s and their cellular localization
evolution
grouping of dual Cytochrome P450 reductases, CPRs, is in accordance with class I and class II of eudicotyledon CPRs, overview; grouping of dual Cytochrome P450 reductases, CPRs, is in accordance with class I and class II of eudicotyledon CPRs, overview
malfunction
-
mutations in POR may reduce heme oxygenase-1 activity, potentially influencing heme catabolism in individuals carrying mutant POR alleles
malfunction
-
human patients with severe forms of CYPOR mutation show bone defects such as cranio- and humeroradial synostoses and long bone fractures, known as Antley-Bixler-like syndrome, ABS
metabolism
human P450 1A2 and 2A6 are able to successfully catalyze the O-deethylation of 7-ethoxyresorufin and the 7-hydroxylation of coumarin, respectively, with the support of the purified enzyme NPR. Purified NPR is an orthologous reductase protein that supports cytochrome P450 enzymes in Malassezia globosa
metabolism
involvement of the enzyme in the withanolide biosynthesic pathway, overview; involvement of the enzyme in the withanolide biosynthesic pathway, overview
physiological function
the recombinant enzymes supports the activity of CYP73A25, a cinnamate 4-hydroxylase of cotton; the recombinant enzymes supports the activity of CYP73A25, a cinnamate 4-hydroxylase of cotton
physiological function
-
regulation of gap junction function by CYPOR, Cx43 may play an important role(s) in CYPOR-mediated bone defects seen in patients
physiological function
-
regulation of gap junction function by CYPOR, Cx43 may play an important role(s) in CYPOR-mediated bone defects
physiological function
NADPH-cytochrome P450 reductase is one of the most important components of the cytochrome P450 enzyme system. It catalyzes electron transfer from NADPH to all known P450s, thus plays central roles not only in the metabolism of exogenous xenobiotics but also in the regulation of endogenous hormones in insects
physiological function
-
regulation of the CPR gene by odorants within insect antennae
physiological function
CYPOR is an essential electron donor to microsomal P450s, therefore it is critical to the function of the large number of physiologic processes regulated by P450
physiological function
-
NADPH-cytochrome P450 reductase is essential for the functioning of microsomal cytochrome P450 monooxygenases and heme oxygenases. Potential biological functions of cytochrome P450 reductase-dependent enzymes in small intestine in expression of major histocompatibility complex class II genes
physiological function
-
the enzyme is capable of activating molecular oxygen on its own merit, generating diffusible reduced oxygen species. It deplete peroxide via diffusible radical mediated process, thereby leading to the formation of water (but without significant evolution of oxygen). CPR mediated processes are bound to be energetically wasteful and potentially hazardous owing to the unavoidable nature of the CPR to generate and deplete diffusible reduced oxygen species. Molecular mechanisms of oxygen activation and peroxide depletion by CPR, overview
physiological function
cytochrome P450 reductase is the most imperative redox partner of multiple P450s involved in primary and secondary metabolite biosynthesis; cytochrome P450 reductase is the most imperative redox partner of multiple P450s involved in primary and secondary metabolite biosynthesis
additional information
-
interaction analysis of membrane-located enzyme CPR with cytochrome P450 CYP1A2, overview
additional information
-
CPR is a diflavin protein containing the flavin cofactors FAD, accepting hydride ions from NADPH, and FMN, accepting single electrons from FAD and reducing the heme center of the P450 monooxygenase domain
additional information
CPR is a diflavin protein containing the flavin cofactors FAD, accepting hydride ions from NADPH, and FMN, accepting single electrons from FAD and reducing the heme center of the P450 monooxygenase domain
additional information
-
cytochrome P450 reductase is a membrane-bound diflavin protein, which transfers two electrons sequentially from NADPH through FAD to the FMN cofactor, which is the ultimate donor of electrons to cytochrome P450 and other acceptor proteins
additional information
-
FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 oxygenase domain, electron transfer mechanism, overview. The two flavin domains undergo large domain movements during catalysis, domain-domain interactions, structure-activity analysis, overview
additional information
-
FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 or NOS oxygenase domain, electron transfer mechanism, overview. The two flavin domains undergo large domain movements during catalysis, domain-domain interactions, structure-activity analysis, overview
additional information
-
role of P450 hydrophobic residues in complex formation with CPR and uncovered novel roles for the surface-exposed residues V267 and L270 of CYP2B4 in mediating CYP2B4-CPR interactions, interaction analysis of wild-type and genetically engineered variants of cytochrome c CYP2B4, i.e. V267C, L270C, L420C, R133C, Y484C, H226C or E60C., overview
additional information
-
the antennae of insects are a key site for P450-mediated metabolism of a large range of exogenous and endogenous molecules
additional information
the electron transfer pathway in CYPOR begins with the obligate two electron donor, NADPH, which transfers a hydride ion to FAD, which in turn donates electrons to the FMN cofactor. The FMN hydroquinone then transfers electrons, one at a time, to its redox partners. Comparison of the structures without and with NADP+ shows movement of the Gly631-Asn635 loop. In the NADP+-free structure, the loop adopts a conformation that sterically hinders NADP(H) binding. The structure with NADP+ shows movement of the Gly631-Asn635 loop to a position that permits NADP(H) binding. Comparison of mutant and wild-type structures, overview. The Gly631-Asn635 loop movement controls NADPH binding and NADP+ release, this loop movement in turn facilitates the flavin domain movement, allowing electron transfer from FMN to the CYPOR redox partners
additional information
-
CPR is a diflavin protein containing the flavin cofactors FAD, accepting hydride ions from NADPH, and FMN, accepting single electrons from FAD and reducing the heme center of the P450 monooxygenase domain
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 5-cyano-2,3-di-p-tolyltetrazolium chloride
NADP+ + (5-cyano-2,3-di-p-tolyltetrazolium chloride) formazan
-
-
formazan is fluorescent
-
?
NADPH + H+ + 2 oxidized cytochrome P450 2B4
NADP+ + 2 reduced cytochrome P450 2B4
-
-
-
-
?
NADPH + H+ + dichlorophenolindophenol
NADP+ + reduced 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 + hexadecanal
NADP+ + hexadecanol
-
brain, hexadecanal replaceable by p-nitroacetophenone, or p-pyridinecarboxaldehyde, benzalacetone or p-nitrobenzaldehyde
-
?
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+
-
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+
-
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+
-
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+
-
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+
-
-
-
-
?
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+
-
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: 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+
-
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+
-
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+
-
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+
-
-
-
?
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+
-
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+
-
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+
-
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 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+
-
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+
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+
-
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+
-
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+
-
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+
-
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+
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 oxidized cytochrome c + NADPH + H+
2 reduced cytochrome c + NADP+
-
-
-
?
ferricytochrome c + dithionite
ferrocytochrome c + ?
-
very low rate of internal electron transfer
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
during hydroxylation of fatty acids through the bacterial fusion protein P450BM3
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + 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 + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
component of the hydroxylation of lauric acid
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
during hydroxylation of alkanes
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + 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 + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
-
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
during ecdysone hydroxylation
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
-
-
-
-
?
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+ + 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 + 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
mixed function oxidase system composed of cytochrome P-450, NADPH-cytochrome c reductase and phospholipids, biotransformation of airborne compounds
-
-
-
additional information
?
-
-
hydroxylation of benzo-a-pyrene, testosterone and progesterone
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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 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.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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 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+
-
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+
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+
-
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+
-
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+
-
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+
-
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+
Q8X1W0
involved in activation of cytochrome P450 monooxygenase systems
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
Q8X1W0
involved in activation of cytochrome P450 monooxygenase systems
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
-
-
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
during hydroxylation of fatty acids through the bacterial fusion protein P450BM3
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + 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 + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
component of the hydroxylation of lauric acid
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
during hydroxylation of alkanes
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + 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 + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
-
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
-
during ecdysone hydroxylation
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
H2ER12
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
D6P3J1, I1E3I6
-
-
-
?
additional information
?
-
-
part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase
-
-
-
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
?
-
-
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
?
-
P00388
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
?
-
A5Y0M3
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
azido nitrophenyl-gamma-aminobutyryl-NADPH
-
in the absence of photoirradiation equally efficient as NADPH
FAD
; the highest increase of 34% is measured after addition of 0.01 mM FAD
FAD
-
the enzyme contains 0.22 mol of FAD per mol of protein, when supplemented with exogenous flavin cofactors, the activity of purified CYPOR-mediated cytochrome c reduction is increased
FAD
one mole isozyme CPR2 contains 0.91 mol of FAD; one mol isozyme CPR1 contains 0.87 mol of FAD
FAD
-
-
685178, 686913, 697616, 701157, 711112, 711152, 711717, 712406, 712656, 713019, 713542, 724112, 724127
FAD
-
-
288546, 288577, 288585, 288605, 288616, 288619, 288620, 695874, 698882, 701158, 711106, 711305, 711313, 713019, 713542, 724127, 725422
FMN
-
not implicated in plant NADPH-ferricyanide reductase; ratio FAD : FMN 1 : 1
FMN
-
riboflavin-deficient microsomes: 40-66% of that of the control microsomes
FMN
second FMN binding site is detected at the interface of the connecting and FMN binding domains. The two FMN binding sites have different accessibilities to the bulk solvent and different amino acid environments, suggesting stabilization of different electronic structures of the reduced flavin. Since only one FMN cofactor is required for function, a hypothetical mechanism of electron transfer is discussed that proposes shuttling of a single FMN between these two sites coupled with the transition between two semiquinone forms, neutral and anionic
FMN
-
binding affinity for FMN is in the submicromolar range, 30times higher than that for FAD
FMN
-
the enzyme contains 0.11 mol of FMN per mol of protein, when supplemented with exogenous flavin cofactors, the activity of purified CYPOR-mediated cytochrome c reduction is increased
FMN
one mole isozyme CPR2 contains 0.86 mol of FMN; one mol isozyme CPR1 contains 0.83 mol of FMN
FMN
-
-
685178, 686913, 697616, 701157, 711112, 711152, 711717, 712406, 712656, 713019, 713542, 724112, 724127
FMN
-
-
288546, 288616, 288619, 288620, 695874, 698882, 701158, 711106, 711305, 711313, 713019, 713542, 724127, 725422
NADPH
-
-
288618, 657897, 657914, 658621, 658948, 659978, 672891, 686851, 686913, 689794, 711112, 711152, 711717, 712406, 712656, 713019, 713542, 713594, 724112, 724127
NADPH
-
-
288549, 288550, 288552, 288554, 288565, 288580, 288585, 288616, 288620, 438257, 671712, 672278, 674672, 676967, 711106, 711305, 711313, 713019, 713542, 724127, 724313
additional information
-
NADH dependent activity on paraquat ist thought to be due to the presence of cytochrome b5 reductase
-
additional information
-
CPR is a diflavin protein containing the flavin cofactors FAD, accepting hydride ions from NADPH, and FMN, accepting single electrons from FAD and reducing the heme center of the P450 monooxygenase domain
-
additional information
CPR is a diflavin protein containing the flavin cofactors FAD, accepting hydride ions from NADPH, and FMN, accepting single electrons from FAD and reducing the heme center of the P450 monooxygenase domain
-
additional information
-
cytochrome P450 reductase is a membrane-bound diflavin protein, which transfers two electrons sequentially from NADPH through FAD to the FMN cofactor, which is the ultimate donor of electrons to cytochrome P450 and other acceptor proteins
-
additional information
-
FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 oxygenase domain, electron transfer mechanism, structure, and redox potentials of the individual redox couples of FAD and FMN of CYPOR, overview. The FAD and FMN domains are connected by a flexible hinge region. The amino acids of the connecting domain are interspersed with the FNR-like domain. The connecting domain, composed mainly of alpha-helices, is tightly bound to the FNR-like domain, and together they form the FAD domain
-
additional information
-
FAD accepts a hydride ion from NADPH, and reduced FAD donates electrons to FMN, which in turn transfers electrons to the heme center of cytochrome P450 or NOS oxygenase domain. The FAD and FMN domains are connected by a flexible hinge region, which spans 12 residues from Gly232 to Arg243. The amino acids of the connecting domain are interspersed with the FNR-like domain, (residues 244-266 and 326-450 in rat CYPOR numbering). The connecting domain, composed mainly of alpha-helices, is tightly bound to the FNR-like domain, and together they form the FAD domain, electron transfer mechanism, structure, and redox potentials of the individual redox couples of FAD and FMN of CYPOR, overview
-
additional information
the ribityl-nicotinamide moiety of NADP+ rotates, and the nicotinamide ring is stacked on the re-side of the flavin ring poised to transfer hydride ion to the N5 atom of FAD. the AMP-PPi portion of NADP+ binds to the enzyme in the same manner as that observed in the structures of wild-type and W677X, the nicotinamide moiety adopts a very different conformation the AMP-PPi portion of NADP+ binds to the enzyme in the same manner as that observed in the structures of wild-type and W677X, the nicotinamide moiety adopts a very different conformation
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
isozyme CPR1 increases to about 2old in the presence of 0.1 M KCl, then decreases at higher concentrations of KCl; isozyme CPR2 increases to about 2old in the presence of 0.1 M KCl, then decreases at higher concentrations of KCl
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
formation of superoxide anion, in the presence of menadione
4-phenylimidazole
inhibitory azole ligand that co-ordinates the haem iron in the sixth (axial) position
AlCl3
-
noncompetitive inhibitor, inhibitory effects of Al3+ and Tl3+ on purified cytochrome P450 reductase are partially recovered by 1 mM EDTA
Cd2+
-
0.05 mM, 66% inhibition. IC50: 0.024 mM, noncompetitive inhibition; 0.05 mM, 66% inhibition, noncompetitive
Cr3+
-
0.05 mM,65% inhibition. IC50: 0.033 mM, noncompetitive inhibition; 0.05 mM, 65% inhibition, noncompetitive
diphenylene iodonium sulfate
-
time-dependent and concentration-dependent inhibition of cDNA-expressed liver enzyme as well as aortic and hepatic microsomal enzyme activity
Hg2+
-
0.05 mM, complete inhibition. IC50: 0.00007 mM, noncompetitive inhibition; 0.05 mM, complete inhibition, noncompetitive
N-ethylmaleimide
-
reduction of cytochrome c and formation of superoxide anion
Ni2+
-
0.05 mM, 37% inhibition. IC50: 0.143 mM, noncompetitive inhibition; 0.05 mM, 37% inhibition, noncompetitive
p-hydroxymercuribenzoate
-
presence of mercaptoethanol or NADPH provides slight protection against inhibition
TlCl3
-
noncompetitive inhibitor, inhibitory effects of Al3+ and Tl3+ on purified cytochrome P450 reductase are partially recovered by 1 mM EDTA
diphenyleneiodonium
about 60% inhibition at 0.02 mM and more than 90% inhibition at 0.06 mM; about 60% inhibition at 0.02 mM and more than 90% inhibition at 0.06 mM
diphenyleneiodonium
0.03 mM, 62% inhibition; 0.03 mM, 64% inhibition; 0.03 mM, 76% inhibition
HgCl2
-
cells grown on alkane or glycerol, presence of NADPH provides protection against inhibition
HgCl2
-
incubation with NADPH provides protection against inhibition
p-chloromercuribenzoate
-
cells grown on alkane or glycerol, presence of NADPH provides protection against inhibition
p-chloromercuribenzoate
-
incubation with NADPH provides protection against inhibition
additional information
-
increasing ionic strength, grown on alkane or glycerol
-
additional information
-
the herbal medicines Epimedii herba, Glycyrrhizae radix and Leonuri herba inhibit one or more NADPH-CYP reductase. Epimedii herba extract is the most potent inhibitor, IC50: 0.1859 mg/ml
-
additional information
-
at low molar ratios of cytochrome b5 to cytochrome P450 reductase, the more rapid catalysis results in enhanced substrate metabolism. In contrast, at high molar ratios of cytochome b5 to cytochrome P450 reductase, cytochrome b5 inhibits activity by binding to the proximal surface of cytochrome P450 and preventing the reductase from reducing ferric cytochrome P450 to the ferrous protein, thereby aborting the catalytic reaction cycle
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
increases internal electron transfer in dithionite reduced enzyme
laurate
-
plus carbon monoxide, greater stimulation compared to laurate alone or carbon monoxide alone, decrease of stimulation in the presence of NADPH; stimulation
potassium phosphate
-
activity slightly higher than with sodium chloride or sodium sulfate
spinach ferredoxin
-
stimulation of the NADPH-reduction of cytochrome c-550 and horse cytochrome c
-
additional information
-
increasing ionic strength, increase in activity
-
additional information
-
activity is upregulated upon exposure of the cells to melanoides from roasted malt
-
additional information
-
in contrast to the inhibitory effects of 2-chloroethyl ethyl sulfide on redox cycling b cytochrome P450 reductase, spontaneous hydrogen peroxide production by the enzyme is stimulated by 2-chloroethyl ethyl sulfide. This response is concentration-dependent in the range of 0.1-10 mM, reaching a maximum at 0.3 mM
-
additional information
-
at low molar ratios of cytochrome b5 to cytochrome P450 reductase, the more rapid catalysis results in enhanced substrate metabolism. In contrast, at high molar ratios of cytochome b5 to cytochrome P450 reductase, cytochrome b5 inhibits activity by binding to the proximal surface of cytochrome P450 and preventing the reductase from reducing ferric cytochrome P450 to the ferrous protein, thereby aborting the catalytic reaction cycle. Cytochrome b5 stimulates catalysis by causing a conformational change in the active site, which allows the active oxidizing oxyferryl species of cytochrome P450 to be formed more rapidly than in the presence of reductase
-
additional information
-
in contrast to the inhibitory effects of 2-chloroethyl ethyl sulfide on redox cycling b cytochrome P450 reductase, spontaneous hydrogen peroxide production by the enzyme is stimulated by 2-chloroethyl ethyl sulfide. This response is concentration-dependent in the range of 0.1-10 mM, reaching a maximum at 0.3 mM
-
additional information
-
storage of the enzyme at -75°C for 4 months results in a slight activation of the enzyme activity
-
additional information
-
in contrast to the inhibitory effects of 2-chloroethyl ethyl sulfide on redox cycling b cytochrome P450 reductase, spontaneous hydrogen peroxide production by the enzyme is stimulated by 2-chloroethyl ethyl sulfide. This response is concentration-dependent in the range of 0.1-10 mM, reaching a maximum at 0.3 mM
-
additional information
-
addition of trypsin significantly increases activity in detergent free buffer, no effect in the presence of detergent
-
additional information
-
increasing ionic strength, increase in activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0372
cytochrome c
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0924
cytochrome c
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.002
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
0.0036
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
0.0052
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
0.0085
ferricytochrome c
-
wild type enzyme, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.011
ferricytochrome c
-
mutant enzyme D113A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.013
ferricytochrome c
-
mutant enzyme E115A/E116A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.016
ferricytochrome c
-
mutant enzyme E115A/E116A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
0.019
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
0.0084
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)
4.3
NADH
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C
0.0066
NADPH
-
native enzyme, liver, cosubstrate cytochrome c; Y140D 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
0.0192
NADPH
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
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
; recombinant yeast microsomal CPR, pH 7.5, 35°C
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; 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
1.4
p-nitroacetophenone
-
electron donor NADH, electron acceptor dichlorophenolindophenol
additional information
additional information
-
cosubstrate NADH, biphasic kinetic
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics by stopped-flow spectroscopy
-
additional information
additional information
CsCPR displays Michaelis-Menten behavior with respect to both cytochrome c and NADPH
-
additional information
additional information
kinetic mechanism, overview
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
-
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
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.67
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
16.67
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
20
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
23.3
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
25
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C; mutant enzyme E115A/E116A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C; mutant enzyme E115A/E116A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
33.33
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
35
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
36.7
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C; mutant enzyme E115A/E116A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
55
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
58.3
ferricytochrome c
Rattus norvegicus
-
mutant enzyme E115A/E116A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C; mutant enzyme E115A/E116A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
65
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
5.83
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
8.5
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
10.5
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
11.67
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
13
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
13.83
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
18.3
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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; 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
20
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
25
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
28.3
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
30
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
38.3
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
40
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
56.67
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1500
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
1700
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
2200
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
2300
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
2500
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
3300
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
3700
ferricytochrome c
Rattus norvegicus
-
mutant enzyme E115A/E116A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C; wild type enzyme, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
4500
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C; mutant enzyme E115A/E116A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
6000
ferricytochrome c
Rattus norvegicus
-
mutant enzyme E115A/E116A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
7000
ferricytochrome c
Rattus norvegicus
-
mutant enzyme E115A/E116A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
8300
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
10000
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
10500
ferricytochrome c
Rattus norvegicus
-
mutant enzyme E115A/E116A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C
313
2700
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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; 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
2385
2800
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
2385
3000
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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; 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
2385
4700
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
2385
4800
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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; 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
2385
5000
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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; 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
2385
5300
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
2385
5800
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
2385
6500
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
2385
6800
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
2385
7200
oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
Rattus norvegicus
-
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
2385
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0711
2'-AMP
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.1319
2'-AMP
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0115
NADP+
-
wild type enzyme, pH not specified in the publication, at 25°C
0.0322
NADP+
-
pH 7.7, 25°C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0459
NADP+
-
pH 7.7, 25°C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00007
Hg2+
Liza saliens
-
0.05 mM, complete inhibition. IC50: 0.00007 mM, noncompetitive inhibition; pH 7.7, 24°C
0.143
Ni2+
Liza saliens
-
0.05 mM, 37% inhibition. IC50: 0.143 mM, noncompetitive inhibition; pH 7.7, 24°C
0.38
2-chloroethyl ethyl sulfide
Homo sapiens
-
using ferricytochrome c as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37°C
1.9
2-chloroethyl ethyl sulfide
Mus musculus
-
using ferricytochrome c as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37°C
2.9
2-chloroethyl ethyl sulfide
Rattus norvegicus
-
in 10 mM phosphate buffer (pH 7.4), at 37°C
3.3
2-chloroethyl ethyl sulfide
Mus musculus
-
using oxidized 2,6-dichlorophenolindophenol as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37°C
8.6
2-chloroethyl ethyl sulfide
Homo sapiens
-
using oxidized 2,6-dichlorophenolindophenol as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0085
-
whole homogenate, prepared from 6 day-organisms, centrifugation for 165 min
0.0095
-
post-mitochondrial supernatant, prepared from 6 day-organisms, centrifugation for 165 min
0.0097
-
post-mitochondrial supernatant, prepared from 1 day-organisms, centrifugation for 6 h
0.0116
-
whole homogenate, prepared from 1 day-organisms, centrifugation for 165 min
0.0133
-
fraction precipitated with 40-50% ammonium sulfate, 3-methylcholantrene treated-animals
0.0135
-
whole homogenate, prepared from 1 day-organisms, centrifugation for 6 h
0.0144
-
post-mitochondrial supernatant, prepared from 1 day-organisms, centrifugation for 165 min
0.02
0.021
-
riboflavin-deficient animals, feeding period 7 weeks, electron acceptor: cytochrome c
0.036
0.0438
-
after cell breakage through filter screen and centrifugation for 30 min
0.066
-
riboflavin-deficient animals, feeding period 6 weeks, electron acceptor: cytochrome c
0.075
-
riboflavin deficient animals, feeding period 7 weeks, electron acceptor: ferricyanide
0.097
-
riboflavin-deficient-animals, feeding period 6 weeks, electron acceptor: ferricyanide
0.124 - 0.138
-
fraction precipitated with 40-50% ammonium sulfate, 3-methylcholantrene-treated animals
0.157
-
control animals, feeding period 6 weeks, electron acceptor: ferricyanide
0.165
-
control animals, feeding period 6 weeks, electron acceptor: cytochrome c
0.245
-
purification by ion exchange chromatography and gel filtration, electron acceptor: dichlorophenolindophenol
0.258 - 0.276
-
fraction precipitated with 40-50% ammonium sulfate, phenobarbital-treated animals
0.361
-
coexpression of 17alpha-2D6 + pJR7, supplementation of cultures with delta-aminolevulinic acid
0.414
-
coexpression of 17alpha-2D6 + pJR7, without supplementation of cultures with delta-aminolevulinic acid
0.517
-
coexpression of ompA-2D6 + pJR7, supplementation of cultures with delta-aminolevulinic acid
0.601
-
coexpression of ompA-2D6 + pJR7, without supplementation of cultures with delta-aminolevulinic acid
1.12
-
purification by ion exchange chromatography and gel filtration, electron acceptor: ferricyanide
1.696
-
recombinant enzyme coexpressed with CYP3A4 in Spodoptera frugiperda cell lines
2.15
isozyme CPR2, using ferricyanide as cosubstrate, at 25°C, pH 7.4
3.17
isozyme CPR2, using ferricytochrome c as cosubstrate, at 25°C, pH 7.4
3.3
isozyme CPR2, for NADPH with cytochrome c as cosubstrate, at 25°C, pH 7.4
3.47
isozyme CPR1, using ferricyanide as cosubstrate, at 25°C, pH 7.4
3.904
-
recombinant enzyme coexpressed with CYP3A4 in Trichoplusia ni cell lines
4.69
isozyme CPR1, using ferricytochrome c as cosubstrate, at 25°C, pH 7.4
4.78
isozyme CPR1, for NADPH with cytochrome c as cosubstrate, at 25°C, pH 7.4
9.32
isozyme CPR1, using dichlorophenolindophenol as cosubstrate, at 25°C, pH 7.4
9.84
isozyme CPR2, using dichlorophenolindophenol as cosubstrate, at 25°C, pH 7.4
12.5
-
grown on alkane, electron acceptor: neotetrazolium chloride, purified enzyme
17.14
-
purification by affinity chromatography on 2',5'-ADP-Sepharose 4B
26
36
40.5
50
-
grown on alkane, electron acceptor: dichlorophenolindophenol, purified enzyme
51.5
-
bacterially expressed reductase protein, electron acceptor: cytochrome c
62.5
63.8
-
purification by n-octylamino-Sepharose 4B and 2',5'-ADP column chromatography
102
-
bacterially expressed reductase protein, electron acceptor: ferricyanide; Y140D mutant, electron acceptor: ferricyanide
additional information
62.5
-
purification by affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate
additional information
-
physical incorporation of NADPH-cytochrome P450 reductase and cytochrome P450 into phospholipid vesicles using glycocholate and Bio-Beads. The efficiency of incorporation of reductase and CYP2B4 is examined in reconstituted systems prepared by the detergent-dialysis method as a function of the detergent used
additional information
-
The substitution mutants (E238A/E239A and T236A/G237A/E238A/E239A) exhibit wild-type activity with cytochrome c. The 2- and 4-alanine addition mutants exhibit about 50% increase in activity compared with the wild-type enzyme. The two and four amino acid deletion mutants reduce cytochrome c 6.4- and 214-fold slower than wild type, respectively.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.7
7.8 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
less than 50% of maximal activity above and below, grown on alkane or glycerol
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
it is the relaxation to the thermodynamic equilibrium position between various two-electron reduced enzyme species, which is affected by both the pH value and the solvent and which decelerates with increasing pH
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
deletion of the NADPH-cytochrome P450 reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity
-
cement gland, lens placode, ear vesicle, mesencephalon, rhombencephalon, lymphatic vessel and heart anlage at stage 29
additional information
overexpression of TcCPR-B in Trypanosoma cruzi epimastigotes increases its resistance to the typical chemotherapeutic agents Nifurtimox and Benznidazole
-
hepatic cytochrome P450 reductase-null mice reveal a second microsomal reductase for squalene monooxygenase
-
liver POR plays an important role regulating gene expression and lipid metabolism locally. The hepatic deficiency of this enzyme reverberates throughout the biological system and produces a coordinated response to the low levels of circulating cholesterol and bile
-
; 3-methylcholantrene-treated animals; phenobarbital-treated animals
-
-
phenobarbital-treated animals
-
-
288550, 288571, 288575, 288577, 288580, 288585, 288587, 288590, 288602, 288616, 288619, 288620, 438257, 671712, 674672, 684900, 686851, 713542
-
phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals
-
-
; phenobarbital-treated animals; phenobarbital-treated animals; riboflavin-deficient animals
-
-
the numbers of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-induced lung tumors are reduced in the lung-Cpr-null mice but are increased in the liver-Cpr-null mice, relative to wild-type control mice
additional information
tissue- and developmental stage-dependent expression analysis of CsCPR mRNA by real-time quantitative PCR. The enzyme is exxpressed in the digestive, metabolic, and olfactory organs of the larvae and adults, overview
additional information
-
CPR activity in 28-day-old male offspring in only the LM76 group (low protein diet based on the modified version of the AIN76A purified diet) but not in the L93 group (low protein diet based on the AIN93G purified diet) is significantly greater than its purified control. CPR activity in 28-day-old male offspring of the M76 group is lower than that in the NP group (nonpurified diet). CPR activities in 65- and 150-day-old male offspring in all five groups are similar. CPR activities in 28-day-old female offspring of the LPD groups are similar to those of their respective purified control groups. However, CPR activities in 28-day-old female offspring in both the purified control groups are lower than that in the NP group. These differences disappeare by day 65, and the lack of differences persisted on day 150. Gender differences (activity in males greater than that in females) are present in all five groups on day 150 but not on days 28 and 65 (the 28-day-old NP group being an exception)
additional information
-
P450 enzyme expression patterns in adult and larval tissues, overview
additional information
presence in every Trypanosoma cruzi developmental stage; presence in every Trypanosoma cruzi developmental stage
additional information
presence in every Trypanosoma cruzi developmental stage; presence in every Trypanosoma cruzi developmental stage
additional information
presence in every Trypanosoma cruzi developmental stage; presence in every Trypanosoma cruzi developmental stage
additional information
-
presence in every Trypanosoma cruzi developmental stage; presence in every Trypanosoma cruzi developmental stage
additional information
higher expression level of WsCPR2 in comparison to WsCPR1; higher expression level of WsCPR2 in comparison to WsCPR1
additional information
higher expression level of WsCPR2 in comparison to WsCPR1; higher expression level of WsCPR2 in comparison to WsCPR1
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
heterologously expressed native and truncated protein
-
heterologously expressed native and truncated protein
-
-
68% of the enzyme resides in detergent-resistant lipid microdomains of the endoplasmic reticulum. The unique lipid components of these domains enhance CYP1A2 substrate metabolism through greater efficiency in CPR/CYP1A2 binding, lipid composition analysis, overview. Lipid composition of purified lipid vesicles affects CYP1A2 substrate metabolism and CPR-CYP1A2 binding
bound, the N-terminal membrane anchor is functionally dispensable
-
cytochrome b5 is a membrane-bound protein that is inserted into the membrane via an alpha-helix at its carboxy terminus. A random-coil linker of 15 amino acids connects the acidic soluble cytosolic heme domain to the membrane anchor
-
membrane-bound protein associated with the cytoplasmic side of the endoplasmic reticulum
-
membrane-bound protein associated with the cytoplasmic side of the endoplasmic reticulum
the enzyme contains membrane anchor regions; the enzyme contains membrane anchor regions
-
-
-
-
-
-
288546, 288549, 288550, 288552, 288554, 288560, 288565, 288571, 288573, 288575, 288577, 288578, 288580, 288585, 288602, 288605, 288606, 288607, 288612, 671712, 686851, 698882, 713542, 724127, 725422
-
outer membrane of vitamin D3-deficient mitochondrion
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000 - 68000
70000
73000
-
NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY), gel filtration
75000
76000
77000
77600
x * 76000, recombinant N-terminally truncated and His6-tagged protein, SDS-PAGE, x * 77600, about, sequence calculation
78000 - 79000
78000
79000
81000
82000 - 85000
82000
85000
additional information
65000 - 68000
-
sedimentation equilibrium centrifugation, values depending on pH
76000
x * 76000, recombinant N-terminally truncated and His6-tagged protein, SDS-PAGE, x * 77600, about, sequence calculation
78000
-
SDS-PAGE, band is accompanied by two smaller, proteolytic forms of the enzyme formed during solubilization or purification
78000
-
x * 78000 (hydrophobic domain (6000 Da) + soluble catalytic domain (72000 Da))
additional information
-
a weak band at the level of the Jerusalem artichoke reductase
additional information
-
differences in MW partially due to method of solubilization
additional information
-
differences in MW partially due to method of solubilization
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
x * 76000, recombinant N-terminally truncated and His6-tagged protein, SDS-PAGE, x * 77600, about, sequence calculation
?
-
x * 78000 (hydrophobic domain (6000 Da) + soluble catalytic domain (72000 Da))
?
x * 68600, calculated from sequence; x * 71300, calculated from sequence; x * 78400, calculated from sequence
dimer
-
2 * 34300-40000, SDS-PAGE, sedimentation equilibrium centrifugation after treatment with guanidine-HCl
monomer
-
1 * 68000, trypsin-solubilized, SDS-PAGE; 1 * 75000, Triton-solubilized, SDS-PAGE
additional information
self-sufficient fatty acid hydroxylase formed by fusion of soluble NADPHcytochrome P450 reductase and P450 domains
additional information
-
differences in subunit weight partially due to method of solubilization
additional information
-
differences in subunit weight partially due to method of solubilization
additional information
-
domain-domain interactions, structure-activity analysis and structure comparisons, overview
additional information
-
N-terminal amino acid sequence is 27% homologous to that of the Spirulina ferredoxin-NADP reductase
additional information
-
N-terminal amino acid sequence is 27% homologous to that of the Spirulina ferredoxin-NADP reductase
-
additional information
-
domain-domain interactions, structure-activity analysis and structure comparisons, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop technique, 4°C, A264Q crystals are obtained with a mother liquor of 100 mM cacodylic acid (pH 6.0), 160 mM MgCl2 and 16% PEG 3350. A264M crystals are obtained with mother liquor of 100 mM cacodylic acid (pH 6.0), 140 mM MgCl2 and 18% PEG 3350. A264C crystals are obtained under the same conditions, but with 100 mM MgCl2. Crystals are flash-frozen in liquid nitrogen using 10% PEG 200 as cryoprotectant. Crystal structures of the mutant haem domains demonstrate axial ligation of P450 haem iron by methionine and glutamine ligands trans to the cysteine thiolate, creating novel haem iron ligand sets in the A264M/Q variants
purified mutant CYPOR with an engineered disulfide bond between the FAD and FMN domains, with or without complexed NADP+, hanging drop vapour diffusion method, mixing of 0.002 ml of 15 mg/ml protein solution with 0.002 ml of reservoir solution containing 100 mM HEPES, pH 7.2, 150 mM MgCl2, and 17% PEG 335, purified protein is treated with 2 and 20 times molar excess of FMN and NADP+, respectively, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
crystal structure of truncated yeast NADPH-cytochrome P450 reductase, which is functionally active toward its physiological substrate cytochrome P450
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
85% loss of activity within 1 h without added glycerol, 54% loss of activity within 1 h in the presence of 20% glycerol
additional information
additional information
-
FAD and NADPH: protection against thermal inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ability to support benzphetamine N-demethylation activity decreased by about 30% after 1 week of storage at -20°C
-
FAD, FMN necessary for stabilization during purification
the activity of the CPR-CYP3A4 enzyme complex in Nanodiscs gradually decreases over time
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris/HCl, pH 7.25, 1 mM EDTA, 50% glycerol, enzyme stored for less than 1 month prior to use
-
-20°C, several weeks
-70°C, 0.15 mM potassium phosphate buffer, pH 7, 1 mM mercaptoethanol, 1 mM EDTA, 1 micromol FMN, 1 micromol FAD, 0.3% Mulgofen BC-720, 30% glycerol, several months
-
-78°C, 30 mM potassium phosphate buffer, pH 7.7, 0.1 mM EDTA, 20% glycerol, 0.4 mM PMSF
-
-80°C, 10 mM potassium phosphate, pH 7.4, 0.02% Emulgen 911, 0.002 mM flavinmononucleotide
-
4°C or room temperature, at both low and high ionic strength, in the presence or absence of NADP, FAD-depleted enzyme
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2',5'-ADP agarose affinity column chromatography and DEAE resin column chromatography
-
2,5-ADP Sepharose affinitycolumn chromatography and DEAE anion exchange column chromatography
-
chromatography on 2',5'-ADP agarose
column chromatography on 2',5'-ADP-Sepharose, phospholipid composition relatively enriched in L-alpha-1,2-diacyl-sn-glycero-3-phosphoserine and L-alpha-1,2-diacyl-sn-glycero-3-phosphoinositol
-
column chromatography on DEAE-cellulose and affinity chromatography on cytochrome-c-Sepharose 4B
-
column chromatography on phenyl-sepharose CL-4B, DEAE cellulose, hydroxylapatite and Sephadex G-150
-
column chromatography on Sephadex G-100 and DEAE-cellulose
DEAE-cellulose followed by sequential chromatography on Sephadex G-150, DEAE-cellulose and hydroxylapatite
-
expressed in Escherichia coli, column chromatography on 2',5'-ADP-agarose
-
extraction of native enzyme from liver microsomes by Brij 98 solubilization and isolation of detergent-resistant membranes by sucrose gradient centrifugation
-
homogeneity, chromatographic methods (DEAE-Sepharose, Q-Sepharose and hydroxyapatite resins)
liver microsomes, column chromatography on Sephadex G-150 and hydroxylapatatite
-
Ni-NTA column chromatography and Superdex G25 gel filtration, the purified enzyme readily loses its flavin cofactors
-
Ni-NTA resin column chromatography; Ni-NTA resin column chromatography
purified 120fold by a combination of ion exchange chromatography and gel filtration and 745fold by affinity chromatography on 2',5'-ADP-Sepharose 4B
-
recombinant N-terminally truncated and His6-tagged enzyme, lacking the putative membrane anchor, from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration to over 98% purity
recombinant N-terminally truncated and His6-tagged protein from Escherichia coli Rosetta (DE3) cells to over 90% purity
recombinant NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY) and recombinant mutant enzyme L86F/L219F/P456ADELTA55AnCY
-
recombinant truncated mutant from Escherichia coli strain C41(DE3) by aanion exchange and 2',5'-ADP-Sepharose
sequential chromatography on DE 52 cellulose and 2',5'-ADP Sepharose
-
single-step procedure involving affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate or two-column procedure involving chromatography on n-octylamino-Sepharose 4B followed by chromatography on 2',5'-ADP
-
solubilization with 0.2% Triton X-100, gel filtration on Sephacryl S-300 and affinity chromatography on 2',5'-ADP agarose
-
solubilization with lipase, column chromatography on Sephadex G-100 superfine, DEAE-cellulose and Sephadex G-200 superfine
-
solubilization with sodium cholate followed by column chromatography on phenyl-Sepharose CL-4B and DEAE-cellulose
-
trypsin digestion followed by Sephadex filtration and column chromatography on DEAE-cellulose
-
using column chromatography on adenosine 2',5'-biphosphate-Sepharose, followed by high-performance anion-exchange chromatography
-
using column chromatography on DEAE-Sepharose CL 6B and affinity chromatography on a 2',5'-ADP Sepharose 4B column
-
WsCPR1, recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography, cleavage of the tag by thrombin, and elimination of thrombin by benzymedene beads; WsCPR2, recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography, cleavage of the tag by thrombin, and elimination of thrombin by benzymedene beads
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Escherichia coli strain TOP10 and coexpressed with CYP98A14 in Saccharomyces cerevisiae strain INV Sc1
coexpressed together with a form of cytochrome P450 in Salmonella typhimurium TA1538
-
coexpression with CYP3A4 in Spodoptera frugiperda and Trichoplusia ni cell lines
-
coexpression with two differently modified CYP2D6 cDNAs in Escherichia coli, 17alpha-2D6 + pJR7 and ompA-2D6 + pJR7
-
DNA and amino acid sequence determination and analysis, sequence comparisons, the enzyme shows highly conserved exon/intron organization structure, functional expression in Escherichia coli membranes
expressed in Bacillus subtilis DB104 under the transcriptional control of an IPTG-inducible fusion promoter of PgroE and Ptac. The expressed rCPR is released into the culture medium after sporulation by autolysis of the host cell. It is associated with and displayed on the spore surfaces
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression of CPR2 using the modified pYeDP60 vector produces high amounts of active protein, expression in Saccharomyces cerevisiae strain W303
-
expression of missense variant proteins lacking 27 N-terminal residues in Escherichia coli
-
functional expression of mammalian NADPH-cytochrome P450 oxidoreductase on the cell surface of Escherichia coli
-
gene 147CC514, expression of wild-type, truncated mutant, and point mutations in Escherichia coli strain C41(DE3)
gene cpr, DNA and amino acid sequence determination and analysis, expression of the N-terminally truncated and His6-tagged enzyme, lacking the putative membrane anchor, in Escherichia coli strain BL21 (DE3)
gene CsCPR, real-time quantitative PCR expression analysis and phylogenetic tree, heterologous expression of N-terminally truncated and His6-tagged protein in Escherichia coli Rosetta (DE3) cells
gene encoding CPr, DNA and amino acid sequence determination and analysis, expression pattern and phylogenetic analysis
-
NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY) is expressed in Escherichia coli loses FMN, leading to an unstable protein and subsequent aggregation. The triple mutant L86F/L219F/P456FDELTA55AnCY exhibits increased stability with significant reduction in aggregation compared to the wild-type enzyme
-
native and truncated form expressed in Escherichia coli BL21(DE3)pLysS as His tag fusion protein
-
the complete CPR cDNA is expressed as 6*His-tagged fusion protein in both membrane and cytosolic fractions in Escherichia coli. Both fractions contain NADPH-cytochrome c reducing activity. The membrane-bound form containing N-terminal membrane anchor is subjected to purification
to analyze the molecular interaction among CYP3A4, NADPH-cytochrome P450 oxidoreductase, and b5, several fused enzyme genes are constructed and expressed in Saccharomyces cerevisiae. The recombinant fused enzymes CYP3A4-truncated(t)-P450 reductase-t-b5 (3RB) and CYP3A4-t-b5-t-P450 reductase (3BR) in yeast microsomes shows a higher specific activity in 6beta-hydroxylation of testosterone than does the reconstitution premixes of CYP3A4, P450 reductase, and b5. The purified fused enzymes exhibit lower Km values and substantially increased Vmax values in 6beta-hydroxylation of testosterone and oxidation of nifedipine. The fused enzymes shows significantly higher activities in cytochrome c reduction than the reconstitution premixes. Although the affinity of 3RB toward cytochrome c is twice as high as that of 3BR, 3BR and 3RB show nearly the same affinity toward NADPH/NADH. In addition, the heme of the CYP3A4 moiety of 3RB is reduced preferentially and more rapidly than that of 3BR, whereas the heme of the b5 moiety of 3BR is selectively reduced compared with that of 3RB
-
truncated form lacking the membrane anchoring domain expresed in Escherichia coli BL21(DE3)pLysS
-
variants of Depressaria pastinacella CYP6AB3v2 are co-expressed with P450 reductase from Musca domestica in Sf9 cells. Allelic variation in the Depressaria pastinacella CYP6AB3 protein enhances metabolism of plant allelochemicals by altering a proximal surface residue and potential interactions with cytochrome P450 reductase
-
WsCPR1, phylogenetic analysis and quantitative real-time PCR expression analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3); WsCPR2, phylogenetic analysis and quantitative real-time PCR expression analysis, expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
exposure of males to a plant odorant down-regulates the transcript level of CPR
-
expression of isozyme CPR2, but not CPR1, is inducible by mechanical wounding and elicitation. Isozyme CPR1 is expressed at a relatively constant level throughout the developmental stages investigated (0-40 days post anthesis), with a slight up-regulation at 15 days post anthesis; isozyme CPR2 shows a dramatic increase of transcript abundance around 15-20 days post anthesis
WsCPR1 is uninducible while WsCPR2 transcript level increase in a time-dependent manner after elicitor treatments, e.g. by methyljasmonate or salicylic acid; WsCPR1 is uninducible while WsCPR2 transcript level increase in a time-dependent manner after elicitor treatments, e.g. by methyljasmonate or salicylic acid
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L219F
L86F
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
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
A115V
-
Vmax/Km for cytochrome c is 63% of wild-type value, Vmax/Km for NADPH is 41% of wild-type value
A287P
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
A503V
C569Y
D211L
-
vmax/Km for ferricytochrome c is 27% of the wild-type value. Vmax/Km for NADPH is 59% of the wild-type value
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
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
G413S
G504R
G539R
-
Vmax/Km for cytochrome c is 9% of wild-type value, Vmax/Km for NADPH is 0.2% of wild-type value
H628P
-
mutation results in similar disruption of CYP17A1 and CYP21A2 activities
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
P228L
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
R316W
R406H
-
vmax/Km for ferricytochrome c is 62% of the wild-type value. Vmax/Km for NADPH is 78% of the wild-type value
R457H
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
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
V492E
V608F
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
Y181D
Y459H
C472T
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
additional information
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
-
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
V492E
-
mutation causes Antley-Bixler syndrome due to diminished binding of the FAD cofactor. Activity is restored by the addition of FAD
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
-
the POR mutant is associated with total loss of heme oxygenase-1 activity
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
-
DELTA55AnCYPOR has an approximately 0.5fold increased FAD content compared to the wild type enzyme
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; 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
-
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
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
-
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
-
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
-
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
-
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
-
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
-
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
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native or truncated protein reconstituts ergosterol biosynthesis when added to a cell-free system, as well as reconstitution of activity with purified Saccharomyces cerevisiae CYP61, sterol 22-desaturase, Candida albicans and human CYP51
-
oxidation of the reduced P450BM3 by cytochrome c, ferricyanide or 2,6-dichlorophenolindophenol rapidly restores electron transfer and hydroxylase activity
-
reconstitution of metabolism of xenobiotics by plant CYPs, reconstituted electron transport chain consisting of partially purified CYP fraction, phospholipid and isolated tulip NADPH : CYP reductase
-
riboflavin-deficient microsomes, reconstitution of activity with FAD, FMN and riboflavin
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
the enzyme is displayed on the cell surface of Escherichia coli, creating a whole-cell biocatalyst for oxidoreduction of various substrates
medicine
additional information
-
the CPR activity in different recombinant enzyme preparations is crucial for in vitro CYP3A5-mediated clearance of midazolam. The level of CPR affects both the affinity/binding of midazolam to the CYP enzyme and the velocity of the metabolic reaction
medicine
-
medical research, expression systems allows examinations on the activation of promutagenic drugs
medicine
-
presence of quercetin and (-)-epigallocatechin gallate in human diet may increase P-450 reductase activity during doxorubicin therapy (antitumour drug) with subsequent increased risk of toxicity
medicine
-
triple mutant L86F/L219F/P456A or a double mutant L86F/L219F enzyme will serve as a good model of mosquito CYPOR in future structural studies and in the development of new antimalarial agents
medicine
-
the POR genotype contributes to breast cancer risk among African American women
medicine
-
nitrofurantoin-induced redox cycling and subsequent generation of reactive oxygen intermediates are not sufficient to mediate cytotoxicity. Cytochrome P450 reductase is not a determinant of sensitivity to redox-active chemotherapeutic agents
medicine
-
manifesting heterozygosity is a possible feature of P450 oxidoreductase deficiency
LINKS TO OTHER DATABASES (specific for EC-Number 1.6.2.4)
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