Information on EC 1.6.2.4 - NADPH-hemoprotein reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.6.2.4
-
RECOMMENDED NAME
GeneOntology No.
NADPH-hemoprotein reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
show the reaction diagram
-
-
-
-
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
kinetic mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NADPH:hemoprotein oxidoreductase
A flavoprotein (FMN, FAD) containing both FMN and FAD. 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. The enzyme catalyses the reduction of the heme-thiolate-dependent monooxygenases, such as EC 1.14.14.1, unspecific monooxygenase and reduction of EC 1.14.99.3, heme oxygenase (biliverdin-producing). It is part of the microsomal hydroxylating system. It also reduces cytochrome b5 and cytochrome c.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldehyde reductase (NADPH-dependent)
-
-
-
-
CPR
-
-
-
-
CPR
Candida apicola ATCC 96134
-
-
CYPOR
-
-
cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent)
-
-
-
-
cytochrome P450 NADPH reductase
-
-
cytochrome P450 oxidoreductase
-
-
cytochrome P450 oxidoreductase
-
cytochrome P450 oxidoreductase
-
-
cytochrome P450 oxidoreductase
-
-
cytochrome P450 reductase
-
-
cytochrome P450 reductase
-
cytochrome P450 reductase
-
-
cytochrome P450 reductase
-
-
cytochrome P450 reductase
-
-
cytochrome P450 reductase
-
-
cytochrome P450 reductase
-
-
cytochrome P450 reductase
-
-
cytochrome P450-diflavin reductase
-
cytochrome P450-diflavin reductase
Candida apicola ATCC 96134
-
-
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase
-
-
-
-
EC 1.6.99.2
-
-
related
-
FAD-cytochrome c reductase
-
-
-
-
ferrihemprotein P450 reductase
-
-
-
-
flavocytochrome P450 BM3
-
NAD(P)H cytochrome P450 reductase
-
-
NADP-cytochrome c reductase
-
-
-
-
NADP-cytochrome P-450 reductase
-
-
NADP-cytochrome reductase
-
-
-
-
NADPH cytochrome P450 reductase
-
-
NADPH cytochrome P450 reductase
-
-
NADPH cytochrome P450 reductase
-
-
NADPH cytochrome P450 reductase
-
-
NADPH cytochrome P450 reductase
-
-
NADPH cytochrome P450 reductase
-
-
NADPH cytochrome P450 reductase
-
NADPH dependent cytochrome P450 reductase
-
-
NADPH P450 oxidoreductase
-
-
NADPH P450 oxidoreductase
-
NADPH P450 oxidoreductase
-
NADPH P450 reductase
-
-
NADPH P450 reductase
-
-
NADPH-CPR
-
-
NADPH-CYP reductase
-
-
NADPH-CYP reductase
-
-
NADPH-cytochrome c oxidoreductase
-
-
-
-
NADPH-cytochrome c reductase
-
-
-
-
NADPH-cytochrome p-450 reductase
-
-
-
-
NADPH-cytochrome P450 (CYP) oxidoreductase
-
-
-
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 oxidoreductase
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 oxidoreductase
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 oxidoreductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
NADPH-cytochrome P450 reductase
-
NADPH-cytochrome P450 reductase
Corbula caribea
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
-
-
NADPH-cytochrome P450 reductase
Saccharomyces cerevisiae /Homo sapiens
-
-
NADPH-cytochrome P450 reductase
-
NADPH-cytochrome P450 reductase
Trametes versicolor IFO 30340
-
-
NADPH-cytochrome P450 reductase
-
NADPH-cytochrome P450 reductase
-
NADPH-dependent cytochrome c reductase
-
-
-
-
NADPH-dependent cytochrome P450 reductase
-
-
NADPH-dependent P450 reductase
-
-
NADPH-ferricytochrome c oxidoreductase
-
-
-
-
NADPH-ferrihemoprotein reductase
-
-
NADPH-ferrihemoprotein reductase
-
-
NADPH-ferrihemoprotein reductase
Corbula caribea
-
-
NADPH-ferrihemoprotein reductase
-
-
NADPH-ferrihemoprotein reductase
-
-
NADPH-ferrihemoprotein reductase
-
-
NADPH-ferrihemoprotein reductase
-
-
NADPH-ferrihemoprotein reductase
-
-
NADPH-ferrihemoprotein reductase
-
NADPH-ferrihemoprotein reductase
Trametes versicolor IFO 30340
-
-
NADPH-P450 reductase
-
-
NADPH-P450 reductase
-
NADPH-P450 reductase
-
-
NADPH: cytochrome P450 oxidoreductase
-
-
NADPH: cytochrome P450 reductase
-
NADPH:CYP oxidoreductase
-
NADPH:cytochrome P450 oxidoreductase
-
-
NADPH:cytochrome P450 reductase
-
-
NADPH:cytochrome P450 reductase
-
NADPH:ferrihemoprotein oxidoreductase
-
-
NADPH:ferrihemoprotein oxidoreductase
-
-
NADPH:ferrihemoprotein oxidoreductase
Corbula caribea
-
-
NADPH:ferrihemoprotein oxidoreductase
-
-
NADPH:ferrihemoprotein oxidoreductase
-
-
NADPH:ferrihemoprotein oxidoreductase
-
-
NADPH:ferrihemoprotein oxidoreductase
-
-
NADPH:ferrihemoprotein oxidoreductase
-
-
NADPH:ferrihemoprotein oxidoreductase
-
NADPH:ferrihemoprotein oxidoreductase
Trametes versicolor IFO 30340
-
-
neotetrazolin reductase
Corbula caribea
-
-
P-450 reductase
-
-
P450 BM3
bifunctional P-450/NADPH-P450 reductase, EC1.14.14.1/EC1.6.2.4
P450 oxidoreductase
-
-
P450 oxidoreductase
-
P450 oxidoreductase
-
-
P450 oxidoreductase
-
P450 Red
-
-
P450 reductase
-
-
P450 reductase
-
-
P450 reductase
-
-
P450R
-
-
-
-
P450R
-
-
P450REd
-
-
reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase
-
-
-
-
reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
SbCPR2
-
-
TPNH-cytochrome c reductase
-
-
-
-
TPNH2 cytochrome c reductase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-03-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression in Escherichia coli
SwissProt
Manually annotated by BRENDA team
gene cpr
UniProt
Manually annotated by BRENDA team
Candida apicola ATCC 96134
gene cpr
UniProt
Manually annotated by BRENDA team
grown on alkanes or glycerol
-
-
Manually annotated by BRENDA team
gene CsCPR
UniProt
Manually annotated by BRENDA team
Corbula caribea
significant activity only in organisms isolated from oil seep site, very low activity in organisms from control site
-
-
Manually annotated by BRENDA team
axenic mutant, strain Ax-2
-
-
Manually annotated by BRENDA team
e.g. maize, potato, avocado, bramble, tulip, leek, Vicia faba, sunflower, bramble, Gingko biloba
-
-
Manually annotated by BRENDA team
cultivars CCRI1 2 and CCRI20
UniProt
Manually annotated by BRENDA team
cv. Ogosta
-
-
Manually annotated by BRENDA team
L. var. Blanc commun., Jerusalem artichoke
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae /Homo sapiens chimeric protein
-
-
Manually annotated by BRENDA team
a transgenic mouse model, with the NADPH-P450 reductase (Cpr) gene deleted in a lung-specific and doxycycline-inducible fashion (lung-Cpr-null)
-
-
Manually annotated by BRENDA team
NMRI/Kisslegg strain
-
-
Manually annotated by BRENDA team
normal mouse and NADPH-cytochrome P450 deletion mutant
-
-
Manually annotated by BRENDA team
Mus musculus NMRI/Kisslegg
NMRI/Kisslegg strain
-
-
Manually annotated by BRENDA team
L. cv Dobrujanski 7
-
-
Manually annotated by BRENDA team
albino animals
-
-
Manually annotated by BRENDA team
gene 147CC514
UniProt
Manually annotated by BRENDA team
recombinant
UniProt
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley strain
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar strain
-
-
Manually annotated by BRENDA team
grown anaerobically
-
-
Manually annotated by BRENDA team
grown anaerobically, wild type strain
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae /Homo sapiens chimeric protein
Uniprot
Manually annotated by BRENDA team
Saccharomyces cerevisiae /Homo sapiens
chimeric protein
Uniprot
Manually annotated by BRENDA team
Saccharomyces cerevisiae JL20
JL20 strain
-
-
Manually annotated by BRENDA team
southern armyworm
-
-
Manually annotated by BRENDA team
strain IFO 30340
SwissProt
Manually annotated by BRENDA team
Trametes versicolor IFO 30340
strain IFO 30340
SwissProt
Manually annotated by BRENDA team
WsCPR1; WsCPR1
UniProt
Manually annotated by BRENDA team
WsCPR2; WsCPR2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
microsomal P450 systems, overview
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
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
metabolism
involvement of the enzyme in the withanolide biosynthesic pathway, overview; involvement of the enzyme in the withanolide biosynthesic pathway, overview
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
-
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
Candida apicola ATCC 96134
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
-
3-fold lower activity than with NADPH
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
-
low rate of internal electron transfer
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
-
lower binding affinity for NADH compared to NADPH
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Corbula caribea
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: duroquinone
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome b5
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: neotetrazolium chloride
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: benzoquinone, additional electron acceptor: vitamin K3
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: nitroblue tetrazolium salt
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: nitroblue tetrazolium salt
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: benzylviologen
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: benzylviologen
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: menadione
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: formylated cytochrome c
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron donor: azidonitrophenyl-gamma-aminobutyryl-NADPH
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
NADH less than 5% of NADPH activity
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
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+
show the reaction diagram
-
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+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
additional electron acceptor: ferricyanide, additional electron acceptor: neotetrazolium chloride, additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
additional electron acceptor: ferricyanide, additional electron acceptor: cytochrome b5, additional electron acceptor: 2,6-dichlorophenolindophenol
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Lodderomyces elongisporus EH15D
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Trametes versicolor IFO 30340
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Wistar
-
additional electron acceptor: neotetrazolium chloride, additional electron acceptor: benzoquinone, additional electron acceptor: vitamin K3, additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Wistar
-
additional electron acceptor: ferricyanide
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Rattus norvegicus Wistar
-
additional electron acceptor: cytochrome P450
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Mus musculus NMRI/Kisslegg
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
Mus musculus NMRI/Kisslegg
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
component of the cytochrome P450 dependent monooxygenase system
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
Corbula caribea
-
component of the mixed function oxygenase system
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
involved in activation of cytochrome P450 monooxygenase systems
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
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+
show the reaction diagram
-
involved in drug metabolism, reduced cytochrome P450 is essential for drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in the hydroxylation of progesterone at the 11alpha position
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
transfer of electrons during the CYP catalytic cycle
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
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+
show the reaction diagram
Trametes versicolor IFO 30340
involved in activation of cytochrome P450 monooxygenase systems
-
?
2 oxidized cytochrome c + NADPH + H+
2 reduced cytochrome c + NADP+
show the reaction diagram
-
-
-
?
2 oxidized cytochrome c + NADPH + H+
2 reduced cytochrome c + NADP+
show the reaction diagram
-
-
?
2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone + NADPH
NADP+ + ?
show the reaction diagram
-
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
-
?
benzphetamine
?
show the reaction diagram
-
demethylation in the presence of added lipid
-
-
?
cocaine
?
show the reaction diagram
-
demethylation in the presence of added lipid
-
-
?
ferricytochrome c + dithionite
ferrocytochrome c + ?
show the reaction diagram
-
-
-
?
NADPH + 5-cyano-2,3-di-p-tolyltetrazolium chloride
NADP+ + (5-cyano-2,3-di-p-tolyltetrazolium chloride) formazan
show the reaction diagram
-
-
formazan is fluorescent
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
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+
show the reaction diagram
-
during ecdysone hydroxylation
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
component of the hydroxylation of lauric acid
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
during hydroxylation of alkanes
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
during hydroxylation of fatty acids through the bacterial fusion protein P450BM3
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
show the reaction diagram
-
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
show the reaction diagram
-
-
?
NADPH + H+ + 2 oxidized cytochrome c
NADP+ + 2 reduced cytochrome c
show the reaction diagram
-
-
?
NADPH + H+ + 2 oxidized cytochrome P450 2B4
NADP+ + 2 reduced cytochrome P450 2B4
show the reaction diagram
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
Candida apicola, Candida apicola ATCC 96134
-
-
?
NADPH + H+ + dichlorophenolindophenol
NADP+ + reduced dichlorophenolindophenol
show the reaction diagram
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
?
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
show the reaction diagram
-
-
-
?
NADPH + H+ + oxidized cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
show the reaction diagram
-
-
-
?
NADPH + hexadecanal
NADP+ + hexadecanol
show the reaction diagram
-
brain, hexadecanal replaceable by p-nitroacetophenone, or p-pyridinecarboxaldehyde, benzalacetone or p-nitrobenzaldehyde
-
?
NADPH + mitoxanthrone
NADP+ + ?
show the reaction diagram
-
-
-
?
NADPH + O2
NADP+ + O2-
show the reaction diagram
-
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-
show the reaction diagram
-
slow reaction, presence of menadione, or duroquinone, or vitamin K3 essential
superoxide anion
?
NADPH + octanal
NADP+ + octanol
show the reaction diagram
-
-
-
?
paraquat + NADPH
?
show the reaction diagram
-
paraquat is a toxic herbicide
-
-
?
ferricytochrome c + dithionite
ferrocytochrome c + ?
show the reaction diagram
-
very low rate of internal electron transfer
-
?
additional information
?
-
no activity with NADH
-
-
-
additional information
?
-
-
hydroxylation of benzo-a-pyrene, testosterone and progesterone
-
-
?
additional information
?
-
-
hydroxylation of coumarate
-
-
?
additional information
?
-
-
coexpressed with CYP3A4 in insect cell lines, testosterone 6-beta-hydroxylase activity
-
-
?
additional information
?
-
-
denitration of glyceryl trinitrate
-
-
?
additional information
?
-
-
O-dealkylation of pentoxyresorufin
-
-
?
additional information
?
-
-
omega-hydroxylation of fatty acids together with cytochrome P450
-
-
?
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
?
-
-
coexpressed with two differently modified CYP2D6 cDNAs in Escherichia coli, functional recombinant monooxygenase, bufuralol and metoprolol metabolism
-
-
?
additional information
?
-
-
as part of the microsomal ethanol-oxidizing system composed of NADPH-cytochrome c reductase, cytochrome P-450, phospholipids
-
-
?
additional information
?
-
-
oxidation of N-nitrosodimethylamine, N-nitroso-N-methylaniline, aminopyrine and 1-phenylazo-2-naphtol
-
-
?
additional information
?
-
-
aniline hydroxylase, N-demethylation of aminopyrine
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine
-
-
?
additional information
?
-
-
N-demethylation of benzphetamine, O-deethylation of 7-ethoxycoumarin
-
-
?
additional information
?
-
-
hydroxylation of ecdysone
-
-
?
additional information
?
-
-
simultaneous catalysis of reduction of cytochrome c and hydroxylation of laurate
-
-
?
additional information
?
-
-
monooxygenase system only present in cells grown on alkanes
-
-
-
additional information
?
-
-
monooxygenase system composed of cytochrome P450, cytochrome b5 and NADPH cytochrome c P450 reductase
-
-
-
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
-
additional information
?
-
-
part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase
-
-
-
additional information
?
-
-
involved in the sterol biosynthesis pathways
-
-
-
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
?
-
-
mixed-function oxidase system composed of cytochrome P450, NADPH cytochrome P450 reductase and lipid
-
-
-
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, monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
-
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
-
additional information
?
-
-
electron transport system composed of cytochrome P-450, cytochrome b5-like hemeproteins, NADPH cytochrome c reductase, and NADH-ferricyanide 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
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
CPR, the obligate electron donor for microsomal P450 enzymes, is essential for the bioactivation of many procarcinogens
-
-
-
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
?
-
-
CYPOR is involved in reduction of the prodrug PR-104A
-
-
-
additional information
?
-
cytochrome P450 monooxygenase gets reducing equivalents from NADPH cytochrome P450 reductase
-
-
-
additional information
?
-
-
deletion of the NADPH-cytochrome P450 reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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 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
?
-
menadione or adrenaline are not reduced
-
-
-
additional information
?
-
menadione or adrenaline ate not reduced
-
-
-
additional information
?
-
fatty-acid-stimulated electron transfer in wild-type and Ala264 mutant flavocytochromes is linked to substrate hydroxylation
-
-
-
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
?
-
-
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
?
-
NADPH-dependent reducing activity for cytochrome c or nitroblue tetrazolium
-
-
-
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
detoxification of drugs, inactivation of procarcinogens, monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
-
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
as part of the microsomal ethanol-oxidizing system composed of NADPH-cytochrome c reductase, cytochrome P-450, phospholipids, aniline hydroxylase, N-demethylation of aminopyrine, N-demethylation of benzphetamine
-
-
?
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
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
?
-
Rattus norvegicus Sprague-Dawley
-
denitration of glyceryl trinitrate
-
-
?
additional information
?
-
Lodderomyces elongisporus EH15D
-
acts as an electron transfer component of the alkane monoxygenase system
-
-
-
additional information
?
-
Saccharomyces cerevisiae JL20
-
involved in the sterol biosynthesis pathways
-
-
-
additional information
?
-
Rattus norvegicus Wistar
-
involved in the reduction of testosterone
-
-
?
additional information
?
-
Rattus norvegicus Wistar
-
O-dealkylation of pentoxyresorufin
-
-
?
additional information
?
-
Mus musculus NMRI/Kisslegg
-
component of the microsomal electron transport system
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
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 P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
component of the cytochrome P450 dependent monooxygenase system
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
Corbula caribea
-
component of the mixed function oxygenase system
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
Q8X1W0
involved in activation of cytochrome P450 monooxygenase systems
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
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+
show the reaction diagram
-
involved in drug metabolism, reduced cytochrome P450 is essential for drug metabolism
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
involved in the hydroxylation of progesterone at the 11alpha position
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
transfer of electrons during the CYP catalytic cycle
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
Trametes versicolor IFO 30340
Q8X1W0
involved in activation of cytochrome P450 monooxygenase systems
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
-
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
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+
show the reaction diagram
-
during ecdysone hydroxylation
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
component of the hydroxylation of lauric acid
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
during hydroxylation of alkanes
-
?
NADPH + cytochrome P-450
reduced cytochrome P-450 + NADP+
show the reaction diagram
-
during hydroxylation of fatty acids through the bacterial fusion protein P450BM3
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
P00388
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
F1P2T2
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
R4UB73
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
A8PYK0
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
D6P3J1, I1E3I6
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
Candida apicola, Candida apicola ATCC 96134
H2ER12
-
-
?
paraquat + NADPH
?
show the reaction diagram
-
paraquat is a toxic herbicide
-
-
?
2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone + NADPH
NADP+ + ?
show the reaction diagram
-
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
-
?
additional information
?
-
-
monooxygenase system only present in cells grown on alkanes
-
-
-
additional information
?
-
-
monooxygenase system composed of cytochrome P450, cytochrome b5 and NADPH cytochrome c P450 reductase
-
-
-
additional information
?
-
-
microsomal electron transport system composed of cytochrome b5, cytochrome P450, NADH-cytochrome b5 reductase and NADPH-cytochrome c reductase
-
-
-
additional information
?
-
-
part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase
-
-
-
additional information
?
-
-
involved in the sterol biosynthesis pathways
-
-
-
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
?
-
-
mixed-function oxidase system composed of cytochrome P450, NADPH cytochrome P450 reductase and lipid
-
-
-
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, monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
-
additional information
?
-
-
monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
-
additional information
?
-
-
electron transport system composed of cytochrome P-450, cytochrome b5-like hemeproteins, NADPH cytochrome c reductase, and NADH-ferricyanide 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
-
-
-
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
?
-
-
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
?
-
-
CPR, the obligate electron donor for microsomal P450 enzymes, is essential for the bioactivation of many procarcinogens
-
-
-
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
?
-
-
CYPOR is involved in reduction of the prodrug PR-104A
-
-
-
additional information
?
-
A5Y0M3
cytochrome P450 monooxygenase gets reducing equivalents from NADPH cytochrome P450 reductase
-
-
-
additional information
?
-
-
deletion of the NADPH-cytochrome P450 reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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 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
?
-
-
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
?
-
Rattus norvegicus Sprague-Dawley
-
detoxification of drugs, inactivation of procarcinogens, monooxygenase system composed of cytochrome P-450, NADPH-cytochrome c reductase, phospholipids
-
-
-
additional information
?
-
Lodderomyces elongisporus EH15D
-
acts as an electron transfer component of the alkane monoxygenase system
-
-
-
additional information
?
-
Saccharomyces cerevisiae JL20
-
involved in the sterol biosynthesis pathways
-
-
-
additional information
?
-
Mus musculus NMRI/Kisslegg
-
component of the microsomal electron transport system
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
azido nitrophenyl-gamma-aminobutyryl-NADPH
-
in the absence of photoirradiation equally efficient as NADPH
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
1 mol per subunit
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
1 mol per subunit
FAD
-
ratio FAD : FMN 1 : 1; tightly bound
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
1 mol per subunit
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
ratio FAD : FMN 1 : 1; tightly bound
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
ratio FAD : FMN 1 : 1
FAD
-
loosely bound
FAD
together with FMN
FAD
-
together with FMN
FAD
-
together with FMN, two binding sites
FAD
-
together with FMN
FAD
-
together with FMN
FAD
Corbula caribea
-
together with FMN
FAD
-
together with FMN
FAD
-
together with FMN
FAD
-
together with FMN
FAD
-
wild-type enzyme contains 1.05 FAD
FAD
Saccharomyces cerevisiae /Homo sapiens
-
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
-
a diflavoenzyme
FMN
-
1 mol per mol of enzyme; ratio FAD : FMN 1 : 1
FMN
-
0.87 nmol per mg protein
FMN
-
ratio FAD : FMN 1 : 1
FMN
-
not implicated in plant NADPH-ferricyanide reductase; ratio FAD : FMN 1 : 1
FMN
-
1 mol per mol of enzyme; ratio FAD : FMN 1 : 1; tightly bound
FMN
-
ratio FAD : FMN 1 : 1
FMN
-
ratio FAD : FMN 1 : 1
FMN
-
loosely bound; ratio FAD : FMN 1 : 1
FMN
-
ratio FAD : FMN 1 : 1
FMN
-
ratio FAD : FMN 1 : 1
FMN
-
ratio FAD : FMN 1 : 1
FMN
-
loosely bound
FMN
-
riboflavin-deficient microsomes: 40-66% of that of the control microsomes
FMN
together with FAD
FMN
-
together with FAD
FMN
-
together with FAD
FMN
-
together with FAD
FMN
Corbula caribea
-
together with FAD
FMN
-
together with FAD
FMN
-
together with FAD
FMN
-
together with FAD
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
-
wild-type enzyme contains 0.92 FMN
FMN
Saccharomyces cerevisiae /Homo sapiens
-
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
NADH
-
less effective than NADPH
NADH
-
low affinity
NADH
-
less effective than NADPH
NADH
-
activity not detected
NADPH
-
NADH less than 5% of NADPH activity
NADPH
-
higher activity towards NADPH than towards NADH
NADPH
-
-
NADPH
-
not replaceable by NADH
NADPH
Corbula caribea
-
-
NADPH
-
-
NADPH
nicotinamide binding is regulated by the Asp632 loop
NADPH
-
preferred over NADH
FMN
-
a diflavoenzyme
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
-
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
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
investigation of the haem-domain
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
-
stimulation by increasing ionic strength
additional information
-
stimulation by increasing ionic strength
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
competitive with NADPH
2'-AMP
-
competitive inhibition
2'-AMP
-
-
2'-AMP
-
dead-end inhibitor
2,6-dichlorophenolindophenol
-
formation of superoxide anion, in the presence of menadione
2-chloroethyl ethyl sulfide
-
potent inhibitor
3-((3-cholamidopropyl)dimethylammonio)propanesulfonic acid
-
-
3-Aminonicotinamide adenine dinucleotide phosphate
-
-
-
4-phenylimidazole
inhibitory azole ligand that co-ordinates the haem iron in the sixth (axial) position
5,5'-dithiobis(2-nitrobenzoate)
-
in absence of FAD or NADPH
6-Propyl-2-thiouracil
-
-
AlCl3
-
noncompetitive inhibitor, inhibitory effects of Al3+ and Tl3+ on purified cytochrome P450 reductase are partially recovered by 1 mM EDTA
alpha-lipoic acid
-
-
Cd2+
-
0.05 mM, 66% inhibition. IC50: 0.024 mM, noncompetitive inhibition; 0.05 mM, 66% inhibition, noncompetitive
cetyltrimethyl ammonium bromide
-
-
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
diphenyleneiodonium
0.03 mM, 62% inhibition; 0.03 mM, 64% inhibition; 0.03 mM, 76% inhibition
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
EDTA
-
reduction of cytochrome c and formation of superoxide anion
Hg2+
-
0.05 mM, complete inhibition. IC50: 0.00007 mM, noncompetitive inhibition; 0.05 mM, complete inhibition, noncompetitive
HgCl2
-
cells grown on alkane or glycerol, presence of NADPH provides protection against inhibition
HgCl2
-
incubation with NADPH provides protection against inhibition
Lubrol WX
-
-
-
N-ethylmaleimide
-
reduction of cytochrome c and formation of superoxide anion
NAD+
-
cosubstrate NADH
NADP+
-
-
NADP+
-
cosubstrate NADPH
NADP+
-
non-competitive inhibition
NADP+
-
competitive inhibition
NADP+
-
competitive inhibition
NADP+
-
competitive inhibition
NADP+
-
product inhibitor
NADP+
-
competitive inhibition
Ni2+
-
0.05 mM, 37% inhibition. IC50: 0.143 mM, noncompetitive inhibition; 0.05 mM, 37% inhibition, noncompetitive
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
cells grown on alkane or glycerol, presence of NADPH provides protection against inhibition
p-chloromercuribenzoate
-
incubation with NADPH provides protection against inhibition
p-hydroxymercuribenzoate
-
presence of mercaptoethanol or NADPH provides slight protection against inhibition
quercetin
-
reduction of cytochrome c and formation of superoxide anion
quercetin
-
IC50: 0.00088 mg/ml
steapsin
-
brain
-
TlCl3
-
noncompetitive inhibitor, inhibitory effects of Al3+ and Tl3+ on purified cytochrome P450 reductase are partially recovered by 1 mM EDTA
Triton N-101
-
-
-
additional information
-
high ionic strength
-
additional information
-
increasing ionic strength, grown on alkane or glycerol
-
additional information
-
-
-
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
-
no inhibition by 0.05 mM Zn2+
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
increases internal electron transfer in dithionite reduced enzyme
2'-AMP
-
increases internal electron transfer in dithionite reduced enzyme
CO
-
stimulation
hexadecanol
-
stimulation
lanosterol
-
activation
laurate
-
plus carbon monoxide, greater stimulation compared to laurate alone or carbon monoxide alone, decrease of stimulation in the presence of NADPH; stimulation
nagarse
-
activation
-
Nonionic detergent
-
activation
-
palmitate
-
stimulation
Phenobarbital
-
stimulation
potassium phosphate
-
activity slightly higher than with sodium chloride or sodium sulfate
sodium cholate/Lubrol PX
-
increases activity
spinach ferredoxin
-
stimulation of the NADPH-reduction of cytochrome c-550 and horse cytochrome c
-
Tetradecanol
-
stimulation
menadione
-
slight stimulation
additional information
-
low ionic strength, slight stimulation
-
additional information
-
increasing ionic strength, increase in activity
-
additional information
-
increasing ionic strength, increase in activity
-
additional information
-
storage of the enzyme at -75C for 4 months results in a slight activation of the enzyme activity
-
additional information
-
activity is upregulated upon exposure of the cells to melanoides from roasted malt
-
additional information
-
addition of trypsin significantly increases activity in detergent free buffer, no effect in the presence of detergent
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.055
2,6-dichlorophenolindophenol
-
grown on glycerol
0.077
2,6-dichlorophenolindophenol
-
grown on alkanes
0.05
5-cyano-2,3-ditolyl tetrazolium chloride
-
-
0.0019
azidonitrophenyl-gamma-aminobutyryl-NADPH
-
-
-
2.5
Benzalacetone
-
-
0.000001
cytochrome c
-
wild type, cosubstrate FAD, Km below
0.00012
cytochrome c
-
T491V mutant, cosubstrate FAD
0.0008
cytochrome c
-
G488L mutant, cosubstrate FAD
0.0015
cytochrome c
-
W677X mutant, cosubstrate NADPH
0.0028
cytochrome c
-
W677Y mutant, cosubstrate NADPH
0.0034
cytochrome c
-
mitochondrial reductase
0.0034
cytochrome c
-
-
0.0041
cytochrome c
-
R454E mutant, cosubstrate NADPH
0.0043
cytochrome c
-
grown on glycerol
0.00455
cytochrome c
-
grown on alkanes
0.0056
cytochrome c
-
S678X mutant, cosubstrate NADPH
0.0058
cytochrome c
-
Y456S mutant, cosubstrate NADPH
0.0059
cytochrome c
-
T491V mutant, cosubstrate NADPH
0.006
cytochrome c
-
spleen
0.0062
cytochrome c
-
wild type, cosubstrate NADPH
0.0063
cytochrome c
-
C472T mutant, cosubstrate NADPH
0.0077
cytochrome c
-
G488L mutant, cosubstrate NADPH
0.0078
cytochrome c
-
-
0.0078
cytochrome c
-
Y456S mutant, cosubstrate FAD
0.0082
cytochrome c
-
-
0.0095
cytochrome c
-
kidney
0.01
cytochrome c
-
-
0.0105
cytochrome c
-
microsomal reductase
0.013
cytochrome c
-
-
0.013
cytochrome c
-
-
0.0131
cytochrome c
-
-
0.0131
cytochrome c
-
Y140F/178F double mutant
0.0135
cytochrome c
-
deletion mutant T236/G237
0.0138
cytochrome c
pH 7.5, 25C
0.014
cytochrome c
-
Y178F mutant
0.015
cytochrome c
-
deletion mutant T236/G237/E238/E239
0.0178
cytochrome c
-
native enzyme, liver
0.0182
cytochrome c
-
determined on the basis of a sequential mechanism
0.0185
cytochrome c
-
Y178D mutant
0.0188
cytochrome c
-
Y140F mutant
0.0191
cytochrome c
-
Y140D mutant
0.0211
cytochrome c
-
wild type
0.024
cytochrome c
-
-
0.0251
cytochrome c
-
R454E mutant, cosubstrate FAD
0.0372
cytochrome c
-
pH 7.7, 25C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0466
cytochrome c
-
cosubstrate NADPH
0.057
cytochrome c
-
-
0.06289
cytochrome c
-
-
0.0924
cytochrome c
-
pH 7.7, 25C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
7.2
ethanol
-
microsomal ethanol oxidizing system
0.0012
ferricytochrome c
isozyme CPR1, at 25C, pH 7.4
0.0016
ferricytochrome c
isozyme CPR1, at 25C, pH 7.4
0.002
ferricytochrome c
-
wild type enzyme, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.0024
ferricytochrome c
-
mutant enzyme E115A/E116A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.0025
ferricytochrome c
-
mutant enzyme D113A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.0036
ferricytochrome c
-
mutant enzyme E115A/E116A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.004
ferricytochrome c
-
wild type enzyme, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.0052
ferricytochrome c
-
mutant enzyme D113A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.006
ferricytochrome c
-
mutant enzyme E115A/E116A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.0085
ferricytochrome c
-
wild type enzyme, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.0098
ferricytochrome c
pH 7.7, 30C
0.011
ferricytochrome c
-
full length enzyme, pH 7.8, 25C
0.011
ferricytochrome c
-
mutant enzyme D113A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.012
ferricytochrome c
-
truncated enzyme, pH 7.8, 25C
0.013
ferricytochrome c
-
mutant enzyme E115A/E116A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.016
ferricytochrome c
-
mutant enzyme E115A/E116A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.017
ferricytochrome c
pH 7.7, 30C
0.018
ferricytochrome c
pH 7.7, 30C
0.019
ferricytochrome c
-
wild type enzyme, pH not specified in the publication, at 25C
0.02
ferricytochrome c
-
wild type enzyme, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.023
ferricytochrome c
-
wild type enzyme, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.0239
ferricytochrome c
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25C
0.025
ferricytochrome c
-
mutant enzyme D113A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.026
ferricytochrome c
-
mutant enzyme D113A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.048
ferricytochrome c
-
pH 7.7
0.39
ferricytochrome c
-
mutant enzyme R600W
0.92
ferricytochrome c
-
mutant enzyme P452L
0.99
ferricytochrome c
-
mutant enzyme A503V
1.15
ferricytochrome c
-
mutant enzyme P284T
1.19
ferricytochrome c
-
wild-type enzyme
1.37
ferricytochrome c
-
mutant enzyme V472M
1.61
ferricytochrome c
-
mutant enzyme G213E
1.84
ferricytochrome c
-
mutant enzyme A485T
1.86
ferricytochrome c
-
mutant enzyme E300K
2.07
ferricytochrome c
-
mutant enzyme R406H
2.09
ferricytochrome c
-
mutant enzyme A462T
2.16
ferricytochrome c
-
mutant enzyme delE53
2.25
ferricytochrome c
-
mutant enzyme P284L
2.31
ferricytochrome c
-
mutant enzyme P55L
2.5 - 5
ferricytochrome c
-
mutant enzyme D211L
0.03
hexadecanal
-
-
0.0084
NADH
-
pH 7.7, 25C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0108
NADH
-
pH 7.7, 25C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0133
NADH
-
microsomal reductase
0.23
NADH
-
-
4
NADH
-
wild type enzyme, pH not specified in the publication, at 25C
4.3
NADH
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25C
20
NADH
-
mitochondrial reductase
24
NADH
-
-
40
NADH
-
kidney
50
NADH
-
spleen
0.000001
NADPH
-
wild type, cosubstrate FAD, Km below
0.00012
NADPH
-
T491V mutant, cosubstrate FAD
0.0008
NADPH
-
G488L mutant, cosubstrate FAD
0.001 - 0.003
NADPH
-
-
0.001
NADPH
-
-
0.0017
NADPH
-
mitochondrial reductase
0.00189
NADPH
-
-
0.0019
NADPH
-
full length enzyme, pH 7.8, 25C
0.0022
NADPH
-
truncated enzyme, pH 7.8, 25C
0.0027
NADPH
-
deletion mutant T236/G237/E238/E239
0.003
NADPH
-
deletion mutant T236/G237
0.00303
NADPH
-
-
0.0033
NADPH
-
kidney
0.0036
NADPH
-
-
0.0046
NADPH
-
-
0.0046
NADPH
isozyme CPR1, at 25C, pH 7.4
0.0047
NADPH
-
spleen
0.00506
NADPH
purified recombinant enzyme, pH 7.8, 25C
0.0055
NADPH
-
microsomal reductase
0.0056
NADPH
isozyme CPR1, at 25C, pH 7.4
0.0057
NADPH
-
-
0.00577
NADPH
pH 7.7, 30C
0.0062
NADPH
-
-
0.0063
NADPH
-
-
0.0064
NADPH
-
wild type, cosubstrate cytochrome c
0.00648
NADPH
purified recombinant enzyme, pH 7.8, 25C
0.0066
NADPH
-
native enzyme, liver, cosubstrate cytochrome c; Y140D mutant, cosubstrate cytochrome c
0.0071
NADPH
-
Y178F mutant, cosubstrate cytochrome c
0.0078
NADPH
-
Y140F mutant, cosubstrate cytochrome c
0.0078
NADPH
-
Y456S mutant, cosubstrate FAD
0.0085
NADPH
-
W677X mutant, cosubstrate cytochrome c
0.0095
NADPH
-
Y178D mutant, cosubstrate cytochrome c
0.0114
NADPH
-
Y140F/178F double mutant, cosubstrate cytochrome c
0.0116
NADPH
-
mutant enzyme L86F/L219F, pH not specified in the publication, at 25C
0.0125
NADPH
-
wild type enzyme, pH not specified in the publication, at 25C
0.0134
NADPH
-
G488L mutant, cosubstrate cytochrome c
0.0143
NADPH
-
W677Y mutant, cosubstrate cytochrome c
0.0163
NADPH
-
wild type, cosubstrate cytochrome c
0.0166
NADPH
-
R454E mutant, cosubstrate cytochrome c
0.0192
NADPH
-
pH 7.7, 25C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0199
NADPH
-
S678X mutant, cosubstrate cytochrome c
0.02
NADPH
-
-
0.0201
NADPH
-
T491V mutant, cosubstrate cytochrome c
0.0217
NADPH
-
C472T mutant, cosubstrate cytochrome c
0.022
NADPH
-
-
0.025
NADPH
-
-
0.025
NADPH
-
mutant enzyme Y607C
0.0251
NADPH
-
R454E mutant, cosubstrate FAD
0.029
NADPH
-
grown on alkanes
0.0308
NADPH
-
determined on the basis of a sequential mechanism
0.0324
NADPH
-
-
0.033
NADPH
-
grown on glycerol
0.0341
NADPH
-
cosubstrate cytochrome c
0.0425
NADPH
-
pH 7.7, 25C, 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, 35C
0.0511
NADPH
pH 7.7, 30C
0.0548
NADPH
-
Y456S mutant, cosubstrate cytochrome c
0.05488
NADPH
pH 7.7, 30C
0.066
NADPH
-
mutant enzyme P284T
0.084
NADPH
-
mutant enzyme R600W
0.125
NADPH
-
mutant enzyme P452L
0.144
NADPH
-
mutant enzyme A485T; wild-type enzyme
0.146
NADPH
-
mutant enzyme P55L
0.151
NADPH
-
mutant enzyme delE53
0.153
NADPH
-
mutant enzyme D211L
0.155
NADPH
-
mutant enzyme A503V
0.157
NADPH
-
mutant enzyme P284L
0.169
NADPH
-
mutant enzyme V472M
0.177
NADPH
-
mutant enzyme R406H
0.196
NADPH
-
mutant enzyme G213E
0.215
NADPH
recombinant yeast internal CPR, pH 7.5, 35C
0.222
NADPH
-
mutant enzyme E300K
0.276
NADPH
-
mutant enzyme A462T
0.21
octanal
-
-
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 25C
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 25C
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 25C
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 25C; 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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
1.4
p-nitroacetophenone
-
electron donor NADH, electron acceptor dichlorophenolindophenol
1.4
p-nitroacetophenone
-
-
0.31
p-nitrobenzaldehyde
-
-
0.0053
menadione
-
-
additional information
additional information
-
cosubstrate NADH, biphasic kinetic
-
additional information
additional information
-
-
-
additional information
additional information
-
O2-generation
-
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
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.63
2,6-dichlorophenolindophenol
Trypanosoma cruzi
-
-
42
5-cyano-2,3-ditolyl tetrazolium chloride
Rattus norvegicus
-
-
15
cytochrome c
Trypanosoma cruzi
-
-
20.5
cytochrome c
Sus scrofa
-
-
20.8 - 22.5
cytochrome c
Rattus norvegicus, Sus scrofa
-
-
21.3
cytochrome c
Rattus norvegicus
-
aortic microsomal enzyme
21.9
cytochrome c
Rattus norvegicus
-
purified enzyme
31.92
cytochrome c
Candida apicola
H2ER12
pH 7.5, 25C
50
cytochrome c
Rattus norvegicus
-
-
53.3
cytochrome c
Bacillus megaterium
-
-
102
cytochrome c
Candida tropicalis
-
grown on alkanes
417
cytochrome c
Bacillus megaterium
-
in the presence of laurate and carbon monoxide
64.5
ferricyanide
Trypanosoma cruzi
-
-
0.43
ferricytochrome c
Homo sapiens
-
mutant enzyme Y459H
0.47
ferricytochrome c
Homo sapiens
-
mutant enzyme V492E
0.5
ferricytochrome c
Homo sapiens
-
mutant enzyme R457H
1.5
ferricytochrome c
Homo sapiens
-
mutant enzyme Q153R
1.73
ferricytochrome c
Homo sapiens
-
mutant enzyme C569Y
1.87
ferricytochrome c
Homo sapiens
-
mutant enzyme L565P; mutant enzyme V608F
2.6
ferricytochrome c
Homo sapiens
-
mutant enzyme A287P
2.7
ferricytochrome c
Homo sapiens
-
mutant enzyme G539R
3.6
ferricytochrome c
Homo sapiens
-
mutant enzyme T142A
3.97
ferricytochrome c
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
4.6
ferricytochrome c
Homo sapiens
-
mutant enzyme G413S
4.9
ferricytochrome c
Homo sapiens
-
mutant enzyme P228L
5.2
ferricytochrome c
Homo sapiens
-
mutant enzyme G504R
5.4
ferricytochrome c
Homo sapiens
-
mutant enzyme R316W
5.47
ferricytochrome c
Homo sapiens
-
mutant enzyme V631I
5.73
ferricytochrome c
Homo sapiens
-
mutant enzyme A503V
5.8
ferricytochrome c
Homo sapiens
-
mutant enzyme A115V
6.4
ferricytochrome c
Homo sapiens
-
mutant enzyme F646del
6.47
ferricytochrome c
Homo sapiens
-
wild-type enzyme
6.7
ferricytochrome c
Homo sapiens
-
mutant enzyme M263V
10.1
ferricytochrome c
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
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 25C
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 25C
19
ferricytochrome c
Phanerochaete chrysosporium
-
full length enzyme, pH 7.8, 25C
20
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
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 25C
25
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C; mutant enzyme E115A/E116A, using 30 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C; mutant enzyme E115A/E116A, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
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 25C
35
ferricytochrome c
Rattus norvegicus
-
wild type enzyme, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
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 25C; mutant enzyme E115A/E116A, using 110 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
42
ferricytochrome c
Phanerochaete chrysosporium
-
truncated enzyme, pH 7.8, 25C
55
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
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 25C; mutant enzyme E115A/E116A, using 310 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
65
ferricytochrome c
Rattus norvegicus
-
mutant enzyme D113A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
0.67
NADPH
Homo sapiens
-
mutant enzyme G539R
0.87
NADPH
Homo sapiens
-
mutant enzyme C569Y
1.7
NADPH
Homo sapiens
-
mutant enzyme L565P
2.3
NADPH
Homo sapiens
-
mutant enzyme V608F; mutant enzyme V631I
2.5
NADPH
Homo sapiens
-
mutant enzyme A287P
2.6
NADPH
Homo sapiens
-
mutant enzyme A115V
2.97
NADPH
Homo sapiens
-
mutant enzyme T142A
3.1
NADPH
Homo sapiens
-
mutant enzyme Q153R
3.63
NADPH
Homo sapiens
-
mutant enzyme G504R
3.8
NADPH
Homo sapiens
-
mutant enzyme P228L
3.86
NADPH
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
3.97
NADPH
Homo sapiens
-
mutant enzyme A503V
4.3
NADPH
Homo sapiens
-
mutant enzyme F646del
4.4
NADPH
Homo sapiens
-
mutant enzyme G413S
4.87
NADPH
Homo sapiens
-
wild-type enzyme
4.9
NADPH
Homo sapiens
-
mutant enzyme M263V; mutant enzyme R316W
10.2
NADPH
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C; 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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
1.45
menadione
Trypanosoma cruzi
-
-
additional information
additional information
Nitrobacter winogradskyi
-
-
-
additional information
additional information
Rattus norvegicus, Sus scrofa
-
-
-
additional information
additional information
Rattus norvegicus
-
-
-
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
313
3321
ferricytochrome c
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
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 25C; wild type enzyme, using 60 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
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 25C; mutant enzyme E115A/E116A, using 210 mM ferricytochrome c as substrate, in 20 mM HEPES buffer (pH 7.5), at 25C
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 25C
313
6305
ferricytochrome c
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
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 25C
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 25C
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 25C
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 25C
313
838
NADPH
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
5
1825
NADPH
Gossypium hirsutum
C0LLU4, C0LLU5
isozyme CPR1, at 25C, pH 7.4
5
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 25C; 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 25C
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 25C
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 25C; 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 25C
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 25C
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 25C; 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 25C
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 25C; 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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
2385
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0054
2',5'-ADP
-
pH 7.0, 25C
0.0711
2'-AMP
-
pH 7.7, 25C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.1319
2'-AMP
-
pH 7.7, 25C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.18
2'-AMP
-
pH 7.0, 25C
0.0089
AlCl3
-
-
0.0728
Cd2+
-
pH 7.7, 24C
0.073
Cd2+
-
-
0.0178
Cr3+
-
pH 7.7, 24C
0.018
Cr3+
-
-
0.000048
Hg2+
-
; pH 7.7, 24C
0.0115
NADP+
-
wild type enzyme, pH not specified in the publication, at 25C
0.0322
NADP+
-
pH 7.7, 25C, NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.0459
NADP+
-
pH 7.7, 25C, triple mutant L86F/L219F/P456A of NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY)
0.329
Ni2+
-
; pH 7.7, 24C
0.0056
TlCl3
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
2-chloroethyl ethyl sulfide
Homo sapiens
-
using ferricytochrome c as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37C
1.9
2-chloroethyl ethyl sulfide
Mus musculus
-
using ferricytochrome c as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37C
2.9
2-chloroethyl ethyl sulfide
Rattus norvegicus
-
in 10 mM phosphate buffer (pH 7.4), at 37C
3.3
2-chloroethyl ethyl sulfide
Mus musculus
-
using oxidized 2,6-dichlorophenolindophenol as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37C
8.6
2-chloroethyl ethyl sulfide
Homo sapiens
-
using oxidized 2,6-dichlorophenolindophenol as cosubstrate, in 10 mM phosphate buffer (pH 7.4), at 37C
0.034
AlCl3
Liza saliens
-
-
0.14
alpha-lipoic acid
Homo sapiens
-
-
0.024
Cd2+
Liza saliens
-
0.05 mM, 66% inhibition. IC50: 0.024 mM, noncompetitive inhibition
0.033
Cd2+
Liza saliens
-
pH 7.7, 24C
0.024
Cr3+
Liza saliens
-
pH 7.7, 24C
0.033
Cr3+
Liza saliens
-
0.05 mM,65% inhibition. IC50: 0.033 mM, noncompetitive inhibition
0.00007
Hg2+
Liza saliens
-
0.05 mM, complete inhibition. IC50: 0.00007 mM, noncompetitive inhibition; pH 7.7, 24C
0.143
Ni2+
Liza saliens
-
0.05 mM, 37% inhibition. IC50: 0.143 mM, noncompetitive inhibition; pH 7.7, 24C
0.0118
Tannic acid
Rattus norvegicus
-
-
0.0174
Tannic acid
Homo sapiens
-
-
0.003
TlCl3
Liza saliens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.002
-
outer membrane of mitochondria
0.00271
-
microsomes
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
0.0104
-
aortic microsomal preparation
0.01087
-
after cell breakage with glass beads and for 30 min
0.0116
-
whole homogenate, prepared from 1 day-organisms, centrifugation for 165 min
0.0128
-
endogenous enzyme
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
0.0173
-
endogenous enzyme
0.0196
-
mitochondria
0.02
-
midgut and hindgut
0.02
-
brain
0.02
-
microsomes
0.02 - 0.12
-
flower buds, open flowers exhibits a similar value
0.0204
-
inner membrane plus matrix
0.021
-
riboflavin-deficient animals, feeding period 7 weeks, electron acceptor: cytochrome c
0.0223
-
spheroplasts
0.0224
-
inner membrane
0.0233
-
-
0.025
-
electron donor: NADH, electron acceptor: dichlorophenolindophenol
0.029
-
malpighian tubules
0.03
-
electron donor: NADPH, electron acceptor: cytochrome b5
0.033
-
endoplasmic reticulum
0.034
-
beta-naphthoflavone-treated animals
0.036
-
mitochondrial fraction
0.036
-
control microsomes
0.04
-
microsomes, 3-methylcholantrene treated-animals
0.0438
-
after cell breakage through filter screen and centrifugation for 30 min
0.048
-
microsomes, control animals
0.05
-
cholate and Lubrol Px
0.055
-
electron donor: NADH, electron acceptor: cytochrome c
0.059
-
no detergent
0.06572
-
purified microsomal ethanol-oxidizing system fraction
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
0.0775
-
purified enzyme
0.079
-
females
0.0857
-
outer membrane
0.08572
-
microsomes
0.087
-
microsomes
0.097
-
riboflavin-deficient-animals, feeding period 6 weeks, electron acceptor: ferricyanide
0.1 - 0.3
-
grown on glycerol, microsomal fraction
0.105
-
microsomes, phenobarbital-treated animals
0.119
-
105000 x g pellet, microsomes
0.124 - 0.138
-
fraction precipitated with 40-50% ammonium sulfate, 3-methylcholantrene-treated animals
0.144
-
fraction precipitated with 40-50% ammonium sulfate, control animals
0.157
-
control animals, feeding period 6 weeks, electron acceptor: ferricyanide
0.165
-
control animals, feeding period 6 weeks, electron acceptor: cytochrome c
0.17
-
R454E mutant, electron acceptor: cytochrome c
0.171
-
nuclear envelope
0.189
-
electron acceptor: formylated cytochrome c
0.211
-
brain, electron acceptor: hexadecanal
0.225 - 0.38
-
endogenous enzyme
0.23
-
Y456S mutant, 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
0.28
-
Y140D/178D double mutant, electron acceptor: cytochrome c
0.3 - 0.7
-
-
0.333
-
microsomes
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
0.44
-
Y178D mutant, electron acceptor: cytochrome c
0.517
-
coexpression of ompA-2D6 + pJR7, supplementation of cultures with delta-aminolevulinic acid
0.58
-
peroxidation of microsomes for 18 min
0.601
-
coexpression of ompA-2D6 + pJR7, without supplementation of cultures with delta-aminolevulinic acid
0.676
-
purified enzyme, liver
0.7
-
under carbon limitation
0.72
-
control microsomes
0.75 - 1.1
-
grown on alkane, microsomal fraction
0.788
-
mitochondria
0.928
-
electron acceptor: cytochrome c
1
-
under oxygen limitation
1.12
-
purification by ion exchange chromatography and gel filtration, electron acceptor: ferricyanide
1.2
-
soybean oil or malt extract as carbon source, high aeration
1.35
-
G488L mutant, electron acceptor: cytochrome c
1.429
-
purification by ion exchange chromatography and gel filtration
1.696
-
recombinant enzyme coexpressed with CYP3A4 in Spodoptera frugiperda cell lines
1.7
-
W677X mutant, electron acceptor: cytochrome c
2.15
isozyme CPR2, using ferricyanide as cosubstrate, at 25C, pH 7.4
2.6
-
glucose as carbon source, low aeration
3.17
isozyme CPR2, using ferricytochrome c as cosubstrate, at 25C, pH 7.4
3.27
-
purified full length enzyme, pH 7.8, 25C
3.3
isozyme CPR2, for NADPH with cytochrome c as cosubstrate, at 25C, pH 7.4
3.47
isozyme CPR1, using ferricyanide as cosubstrate, at 25C, 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 25C, pH 7.4
4.78
isozyme CPR1, for NADPH with cytochrome c as cosubstrate, at 25C, pH 7.4
5.5
-
preparative polyacrylamide disc gel electrophoresis
5.7
-
soybean oil as carbon source, low aeration
5.9
-
brain, electron acceptor: p-nitrobenzaldehyde
6.83
purified recombinant enzyme, pH 7.8, 25C
7.56
purified recombinant enzyme, pH 7.8, 25C
8.64
-
electron acceptor: dichlorophenolindophenol
9.32
isozyme CPR1, using dichlorophenolindophenol as cosubstrate, at 25C, pH 7.4
9.84
isozyme CPR2, using dichlorophenolindophenol as cosubstrate, at 25C, pH 7.4
10.5
-
glycerol as carbon source, low aeration
11
-
Y140D mutant, electron acceptor: cytochrome c
12.5
-
grown on alkane, electron acceptor: neotetrazolium chloride, purified enzyme
13.1
-
endoplasmic reticulum
14.5
-
purified enzyme with cytochrome c as substrate, pH 7.7
14.76
-
purified truncated enzyme, pH 7.8, 25C
15.2
-
polymorphonuclear leukocytes
16.5
-
cDNA-expressed liver enzyme
17.1
-
liver
17.14
-
purification by affinity chromatography on 2',5'-ADP-Sepharose 4B
17.9
-
electron donor: NADPH, electron acceptor: dichlorophenolindophenol
18.1
-
mitochondria
18.4
-
electron acceptor: 2,6-dichlorophenolindophenol
18.5
-
grown on alkane, electron acceptor: ferricyanide, purified enzyme
19
-
electron acceptor: neotetrazolium chloride
22
-
in the presence of 0.005 mM FMN
24.3
-
purified truncated protein
26
-
electron acceptor: ferricyanide
26.1
-
-
28
-
electron acceptor: menadione
29
-
grown on alkane, electron acceptor: menadione, purified enzyme
32.7
-
T491V mutant, electron acceptor: cytochrome c
36
-
purified truncated protein
36
-
W677Y mutant, electron acceptor: cytochrome c
37.6
-
purified enzyme
40.5
-
electron donor: NADPH, electron acceptor: ferricyanide
40.7
-
Golgi apparatus
41.1
-
plasma membrane
41.2
-
electron donor: NADPH, electron acceptor: cytochrome c
42
-
electron acceptor: dichlorophenolindophenol
46
-
Y140F/178F double mutant, electron acceptor: cytochrome c
47.4
-
Y178F mutant, electron acceptor: cytochrome c
48.1
-
Y178D mutant, electron acceptor: ferricyanide
50
-
grown on alkane, electron acceptor: dichlorophenolindophenol, purified enzyme
51
-
Y140D/178D double mutant, electron acceptor: ferricyanide
51.5
-
bacterially expressed reductase protein, electron acceptor: cytochrome c
52.9
-
electron acceptor: ferricyanide
53.3
-
electron acceptor: cytochrome c
55.2
-
Y140F mutant, electron acceptor: cytochrome c
57.4
-
wild type, electron acceptor: cytochrome c
60
-
purified enzyme, microsomes
60 - 120
-
purified enzyme
62.5
-
purification by affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate
62.5
-
S678X mutant, electron acceptor: cytochrome c
63.8
-
purification by n-octylamino-Sepharose 4B and 2',5'-ADP column chromatography
65.4
-
C472T mutant, electron acceptor: cytochrome c
70
-
grown on alkane, electron acceptor: cytochrome c, purified enzyme
94.2
-
Y140F/178F double mutant, electron acceptor: ferricyanide
94.8
-
Y140F mutant, electron acceptor: ferricyanide
98.3
-
electron acceptor: ferricyanide
102
-
bacterially expressed reductase protein, electron acceptor: ferricyanide; Y140D mutant, electron acceptor: ferricyanide
113
-
Y178F mutant, electron acceptor: ferricyanide
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9 - 7.5
-
microsomal ethanol-oxidizing system
7 - 7.4
-
O2- generation
7.1 - 7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4 - 7.7
assay at
7.4 - 7.8
-
-
7.7
assay at
7.8
assay at; assay at
7.8 - 8
-
-
7.8 - 8
-
grown on alkane or glycerol
8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
less than 50% of maximal activity above and below, grown on alkane or glycerol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
assay at; assay at
29 - 37
-
assay at
30
-
assay at
30 - 37
assay at
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
sequence calculation
6
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
deletion of the NADPH-cytochrome P450 reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity
Manually annotated by BRENDA team
-
cement gland, lens placode, ear vesicle, mesencephalon, rhombencephalon, lymphatic vessel and heart anlage at stage 29
Manually annotated by BRENDA team
overexpression of TcCPR-B in Trypanosoma cruzi epimastigotes increases its resistance to the typical chemotherapeutic agents Nifurtimox and Benznidazole
Manually annotated by BRENDA team
-
buds and nascent, open flowers
Manually annotated by BRENDA team
Corbula caribea
-
-
Manually annotated by BRENDA team
-
alpha-lipoic acid decreases enzyme activity in lung and heart
Manually annotated by BRENDA team
Corbula caribea
-
-
Manually annotated by BRENDA team
-
NaCl application results in a significant increase in the activity
Manually annotated by BRENDA team
-
polymorphonuclear
Manually annotated by BRENDA team
-
phenobarbital-treated animals
Manually annotated by BRENDA team
-
3-methylcholantrene-treated animals; phenobarbital-treated animals
Manually annotated by BRENDA team
-
riboflavin-deficient animals
Manually annotated by BRENDA team
-
hepatic cytochrome P450 reductase-null mice reveal a second microsomal reductase for squalene monooxygenase
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus NMRI/Kisslegg
-
; 3-methylcholantrene-treated animals; phenobarbital-treated animals
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals; phenobarbital-treated animals
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
; phenobarbital-treated animals; phenobarbital-treated animals; riboflavin-deficient animals
-
Manually annotated by BRENDA team
-
alpha-lipoic acid decreases enzyme activity in lung and heart
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
,of larvae of both sexes
Manually annotated by BRENDA team
-
of larvae, induction of larvae with pentamethylbenzene
Manually annotated by BRENDA team
-
olfactory and respiratory mucosa
Manually annotated by BRENDA team
-
primary from mouse calvariae
Manually annotated by BRENDA team
-
Vicia faba, leek, sunflower
Manually annotated by BRENDA team
-
beta-naphtoflavone-treated animals
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
beta-naphtoflavone-treated animals
-
Manually annotated by BRENDA team
-
transfected with the human P450 Red gene
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
type II lung epithelial cell
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
additional information
presence in every Trypanosoma cruzi developmental stage; presence in every Trypanosoma cruzi developmental stage
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
P450 enzyme expression patterns in adult and larval tissues, overview
Manually annotated by BRENDA team
additional information
higher expression level of WsCPR2 in comparison to WsCPR1; higher expression level of WsCPR2 in comparison to WsCPR1
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Rattus norvegicus Sprague-Dawley
-
;
-
Manually annotated by BRENDA team
-
heterologously expressed native and truncated protein
Manually annotated by BRENDA team
Saccharomyces cerevisiae JL20
-
heterologously expressed native and truncated protein
-
Manually annotated by BRENDA team
Corbula caribea
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
colocalization with cytochromes P450
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
membrane-bound protein associated with the cytoplasmic side of the endoplasmic reticulum
Manually annotated by BRENDA team
bound, the N-terminal membrane anchor is functionally dispensable
Manually annotated by BRENDA team
the enzyme contains membrane anchor regions; the enzyme contains membrane anchor regions
Manually annotated by BRENDA team
Trametes versicolor IFO 30340
-
-
-
Manually annotated by BRENDA team
-
0.03 to 0.1% of aortic microsomal protein
-
Manually annotated by BRENDA team
-
heterologously expressed native and truncated protein
-
Manually annotated by BRENDA team
Aspergillus ochraceus NRRL 405, Aspergillus ochraceus TS, Lodderomyces elongisporus EH15D
-
-
-
-
Manually annotated by BRENDA team
Mus musculus NMRI/Kisslegg
-
;
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
0.03 to 0.1% of aortic microsomal protein
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae JL20
-
heterologously expressed native and truncated protein
-
-
Manually annotated by BRENDA team
-
outer membrane of vitamin D3-deficient mitochondrion
Manually annotated by BRENDA team
-
outer membrane of mitochondria
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000 - 68000
-
sedimentation equilibrium centrifugation, values depending on pH
288567
65000 - 68000
-
gel filtration, sedimentation equilibrium centrifugation
288570
65000 - 68000
-
gel filtration, kidney
288576, 288579
65000 - 68000
-
gel filtration, liver
288583
70000
-
gel filtration
288551
70000
-
testis, gel filtration
288555
70000
-
gel filtration
288572
73000
-
NADPH-cytochrome c oxidoreductase lacking the first 55 amino acid residues (DELTA55AnCY), gel filtration
684727
75000
-
truncated protein
288618
76000
-
SDS-PAGE
659104
77140
isozyme CPR1, calculated from amino acid sequence
713235
78000
-
-
288618
78000
-
SDS-PAGE, band is accompanied by two smaller, proteolytic forms of the enzyme formed during solubilization or purification
659807
78000
-
SDS-PAGE
698882
78000
-
SDS-PAGE
711102
78000
-
SDS-PAGE
711305
78000
-
-
711313
78000
-
SDS-PAGE
711717
78000 - 79000
-
sedimentation equilibrium centrifugation
288583
78000 - 79000
-
liver
288590
78300
calculated from amino acid sequence
700774
78590
isozyme CPR2, calculated from amino acid sequence
713235
79300
-
theoretical mass, truncated enzyme
657728
80700
calculated from the deduced amino acid sequence
657619
81000
SDS-PAGE
657619
81600
-
theoretical mass, full length enzyme
657728
82000
-
-
701157
82000
-
-
701158
82000 - 85000
-
SDS-PAGE followed by Western blotting
288550
82000 - 85000
-
-
288550
82000 - 85000
-
calculation from FAD content
288572
82000 - 85000
-
-
288588
82000 - 85000
-
-
288589
83000
-
His-tagged enzyme, SDS-PAGE
711027
84000
-
Western blot analysis of fresh microsomal extracts
288621
85900
-
SDS-PAGE, truncated enzyme
657728
88200
-
SDS-PAGE, full length enzyme
657728
100000
-
gel filtration
288556
400000
-
polymorphonuclear leukocytes, gel filtration
288545
additional information
-
-
288550
additional information
-
a weak band at the level of the Jerusalem artichoke reductase
288550
additional information
-
differences in MW partially due to method of solubilization
288553
additional information
-
differences in MW partially due to method of solubilization
288564
additional information
-
-
288568
additional information
-
liver microsomes, gel filtration
288582
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 79000, SDS-PAGE
?
-
x * 77000, SDS-PAGE
?
-
x * 85000, SDS-PAGE
?
-
x * 76000, SDS-PAGE
?
-
x * 82000, SDS-PAGE
?
-
x * 76000, SDS-PAGE
?
-
x * 70000, SDS-PAGE
?
-
x * 75000-76000, SDS-PAGE
?
-
x * 72000-87000, SDS-PAGE
?
-
x * 62000
?
-
wild type, x * 80000, SDS-PAGE
?
x * 77300, calculated from sequence
?
x * 68600, calculated from sequence; x * 71300, calculated from sequence; x * 78400, calculated from sequence
?
-
x * 78000 (hydrophobic domain (6000 Da) + soluble catalytic domain (72000 Da))
?
x * 77000, x * 79000, x * 81000, SDS-PAGE
?
x * 78300, calculated
?
x * 76068, sequence calculation
?
x * 76000, recombinant N-terminally truncated and His6-tagged protein, SDS-PAGE, x * 77600, about, sequence calculation
?
x * 80740, SDS-PAGE
?
Candida apicola ATCC 96134
-
x * 76068, sequence calculation
-
?
Lodderomyces elongisporus EH15D
-
x * 79000, SDS-PAGE
-
?
Mus musculus NMRI/Kisslegg
-
x * 62000
-
?
Rattus norvegicus Sprague-Dawley
-
; x * 75000-76000, SDS-PAGE; x * 85000, SDS-PAGE
-
?
Rattus norvegicus Wistar
-
x * 75000-76000, SDS-PAGE
-
dimer
-
2 * 36000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 34300-40000, SDS-PAGE, sedimentation equilibrium centrifugation after treatment with guanidine-HCl
monomer
-
1 * 67000, SDS-PAGE, trypsin- or lipase-solubilized
monomer
-
1 * 72000, SDS-PAGE
monomer
-
1 * 68000, trypsin-solubilized, SDS-PAGE; 1 * 75000, Triton-solubilized, SDS-PAGE
additional information
-
N-terminal amino acid sequence is 27% homologous to that of the Spirulina ferredoxin-NADP reductase
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
self-sufficient fatty acid hydroxylase formed by fusion of soluble NADPHcytochrome P450 reductase and P450 domains
additional information
-
domain-domain interactions, structure-activity analysis and structure comparisons, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
79000 Da and 81000 Da isoforms
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop technique, 4C, 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
deletion mutants
-
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
-
Saccharomyces cerevisiae /Homo sapiens
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-90
-
inactivation
288556
2 - 4
-
1 day, inactivation
288556
20
-
1 day, from 5% to 10% loss of activity
288556
25 - 30
-
diluted solutions: gradual loss of activity
288585
36
-
inactivation above
288565
37
-
85% loss of activity within 1 h without added glycerol, 54% loss of activity within 1 h in the presence of 20% glycerol
659104
40
-
50% activity
288565
50
-
40% activity remaining after 3 min
288578
60
-
brain, inactivation
288554
100
-
10 min, inhibition of O2-formation
288558
additional information
-
FAD and NADPH: protection against thermal inactivation
288567
additional information
-
stable in a frozen state at least for one month
288582
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% glycerol stabilizes enzyme
-
FAD, FMN necessary for stabilization during purification
-
FAD-domains tends to form aggregates and precipitates upon storage at -20C
-
ability to support benzphetamine N-demethylation activity decreased by about 30% after 1 week of storage at -20C
-
stable to multiple freeze-thaw cycles, FAD-depleted enzyme
-
the activity of the CPR-CYP3A4 enzyme complex in Nanodiscs gradually decreases over time
-
FAD, FMN necessary for stabilization during purification
-