Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.6.2.4 - NADPH-hemoprotein reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SB48

for references in articles please use BRENDA:EC1.6.2.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9SB48
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
aldehyde reductase (NADPH-dependent)
-
-
-
-
cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent)
-
-
-
-
cytochrome P450 reductase
-
-
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase
-
-
-
-
FAD-cytochrome c reductase
-
-
-
-
ferrihemprotein P450 reductase
-
-
-
-
NADP-cytochrome c reductase
-
-
-
-
NADP-cytochrome 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 reductase 2
-
-
NADPH-dependent cytochrome c reductase
-
-
-
-
NADPH-ferricytochrome c oxidoreductase
-
-
-
-
P450R
-
-
-
-
reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase
-
-
-
-
reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
TPNH-cytochrome c reductase
-
-
-
-
TPNH2 cytochrome c reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
-
?
NADPH + H+ + ferricyanide
NADP+ + ferrocyanide
show the reaction diagram
-
-
-
-
?
NADPH + H+ + ferricytochrome c
NADP+ + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
NADPH + H+ + ferrocytochrome b5
NADP+ + ferricytochrome b5
show the reaction diagram
-
-
-
-
?
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
2 ferricytochrome c + NADPH
2 ferrocytochrome c + NADP+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricytochrome P450 + NADPH
2 ferrocytochrome P450 + NADP+ + H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00102
NADPH
-
at pH 7.5 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
146
ferricyanide
-
at pH 7.5 and 25°C
2 - 3.7
ferricytochrome c
-
at pH 7.5 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00056
2',5'-ADP
-
at pH 7.5 and 25°C
0.00102
NADP+
-
at pH 7.5 and 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
CPR is membrane-bound
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NCPR1_ARATH
692
1
76766
Swiss-Prot
other Location (Reliability: 4)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 21% (w/v) polyethylene glycol monomethyl ether 2000 and 0.1 M MES, pH 6.5
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
canadine-producing Saccharomyces cerevisiae strain harbors expression cassettes for seven heterologous enzymes: Papaper somniferum norcoclaurine 6-O-methyltransferase (Ps6OMT), Papaver somniferum 3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase 2 (Ps4'OMT), Papapver somniferum coclaurine N-methyltransferase (PsCNMT), Papaver somniferum berberine bridge enzyme (PsBBE), Thalictrum flavum scoulerine 9-O-methyltransferase (TfS9OMT), Thalictrum flavum canadine synthase (TfCAS), and Arabidopsis thaliana cytochrome P450 reductase 1 (CPR). The expression cassettes for the methyltransferases Ps6OMT, PsCNMT, and Ps4'OMT and the cytochrome P450 reductase CPR were chromosomally integrated, TfS9OMT and TfCAS are expressed from a high-copy plasmid, and PsBBE is expressed from a second high-copy plasmid
expressed in Escherichia coli BL21 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
a Saccharomyces cerevisiae strain is engineered to express seven heterologous enzymes (Papaper somniferum norcoclaurine 6-O-methyltransferase (Ps6OMT), Papaver somniferum 3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase 2 (Ps4'OMT), Papapver somniferum coclaurine N-methyltransferase (PsCNMT), Papaver somniferum berberine bridge enzyme (PsBBE), Thalictrum flavum scoulerine 9-O-methyltransferase (TfS9OMT), Thalictrum flavum canadine synthase (TfCAS), and Arabidopsis thaliana cytochrome P450 reductase 1 (CPR)), resulting in protoberberine alkaloid production from a simple benzylisoquinoline alkaloid precursor. A number of strategies are implemented to improve flux through the pathway, including enzyme variant screening, genetic copy number variation, and culture optimization. This leads to an over 70-fold increase in canadine titer up to 1.8 mg/l. Increased canadine titers enable extension of the pathway to produce berberine, a major constituent of several traditional medicines in a microbial host. This strain is viable at pilot scale
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jensen, K.; Moller, B.L.
Plant NADPH-cytochrome P450 oxidoreductases
Phytochemistry
71
132-141
2010
Ammi majus, Arabidopsis thaliana, Capsicum annuum, Ricinus communis, Catharanthus roseus, Centaurium erythraea, Chlamydomonas reinhardtii, Coleus scutellarioides, Eschscholzia californica, Glycine max, Gossypium hirsutum, Helianthus tuberosus, Hypericum androsaemum, Lotus japonicus, Ophiorrhiza pumila, Oryza sativa, Papaver somniferum, Petroselinum crispum, Vigna radiata, Physcomitrium patens, Pisum sativum, Pseudotsuga menziesii, Sorghum bicolor, Taxus cuspidata, Triticum aestivum, Vicia sativa, Vitis vinifera, Zea mays, Artemisia annua, Populus trichocarpa x Populus deltoides, Stevia rebaudiana, Taxus chinensis, Selaginella moellendorffii
Manually annotated by BRENDA team
Whitelaw, D.A.; Tonkin, R.; Meints, C.E.; Wolthers, K.R.
Kinetic analysis of electron flux in cytochrome P450 reductases reveals differences in rate-determining steps in plant and mammalian enzymes
Arch. Biochem. Biophys.
584
107-115
2015
Arabidopsis thaliana, Homo sapiens, Artemisia annua
Manually annotated by BRENDA team
Niu, G.; Zhao, S.; Wang, L.; Dong, W.; Liu, L.; He, Y.
Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function
FEBS J.
284
754-765
2017
Arabidopsis thaliana
Manually annotated by BRENDA team
Galanie, S.; Smolke, C.
Optimization of yeast-based production of medicinal protoberberine alkaloids
Microb. Cell Fact.
14
144
2015
Arabidopsis thaliana (Q9SB48)
Manually annotated by BRENDA team