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Information on EC 1.6.2.4 - NADPH-hemoprotein reductase and Organism(s) Gallus gallus and UniProt Accession F1P2T2

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EC Tree
     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.2 With a heme protein as acceptor
                1.6.2.4 NADPH-hemoprotein reductase
IUBMB Comments
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases (e.g. EC 1.14.14.1, unspecific monooxygenase) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. It also reduces cytochrome b5 and cytochrome c. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
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Gallus gallus
UNIPROT: F1P2T2
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The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadph-cytochrome p-450 reductase, cytochrome p450 reductase, p450 reductase, p-450 reductase, nadph-p450 reductase, p450 bm3, p450 oxidoreductase, nadph cytochrome p450 reductase, cytochrome p450 oxidoreductase, cypor, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADPH-cytochrome P450 oxidoreductase
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aldehyde reductase (NADPH-dependent)
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-
-
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CPR
-
-
-
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cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent)
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-
-
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dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase
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-
-
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FAD-cytochrome c reductase
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-
-
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ferrihemprotein P450 reductase
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-
-
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NADP-cytochrome c reductase
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-
-
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NADP-cytochrome reductase
-
-
-
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NADPH-cytochrome c oxidoreductase
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-
-
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NADPH-cytochrome c reductase
-
-
-
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NADPH-cytochrome p-450 reductase
-
-
-
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NADPH-cytochrome P450 (CYP) oxidoreductase
-
-
-
-
NADPH-dependent cytochrome c reductase
-
-
-
-
NADPH-ferricytochrome c oxidoreductase
-
-
-
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P450R
-
-
-
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reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase
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-
-
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reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
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TPNH-cytochrome c reductase
-
-
-
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TPNH2 cytochrome c reductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
show the reaction diagram
kinetic mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
NADPH:hemoprotein oxidoreductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases (e.g. EC 1.14.14.1, unspecific monooxygenase) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. It also reduces cytochrome b5 and cytochrome c. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-03-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
?
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
?
ferricytochrome c + NADH + H+
ferrocytochrome c + NAD+
show the reaction diagram
-
-
-
-
r
ferricytochrome c + NADPH + H+
ferrocytochrome c + NADP+
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034 - 0.0105
ferricytochrome c
0.0133 - 20
NADH
0.0017 - 0.0055
NADPH
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.788
-
mitochondria
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
assay at
7.8 - 8
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
outer membrane of vitamin D3-deficient mitochondrion
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
chicken POR shares high homology with other vertebrates PORs and possesses the conserved binding domains of FAD, FMN, and NADPH
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F1P2T2_CHICK
676
1
76969
TrEMBL
other Location (Reliability: 3)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mitochondria
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, the enzyme shows highly conserved exon/intron organization structure, functional expression in Escherichia coli membranes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kulkoski, J.A.; Weber, J.L.; Ghazarian, J.G.
NADPH-cytochrome c reductase in outer membrane of kidney mitochondria. Purification and properties
Arch. Biochem. Biophys.
192
539-547
1979
Gallus gallus
Manually annotated by BRENDA team
Zhou, X.; Li, M.; Sheng, C.; Qiu, X.
NADPH-cytochrome P450 oxidoreductase from the chicken (Gallus gallus): sequence characterization, functional expression and kinetic study
Comp. Biochem. Physiol. C
153
53-59
2011
Gallus gallus (F1P2T2), Gallus gallus
Manually annotated by BRENDA team