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Information on EC 1.6.2.2 - cytochrome-b5 reductase and Organism(s) Homo sapiens and UniProt Accession Q7L1T6
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1.6.2.2 cytochrome-b5 reductaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.6.2.2
- erythrocyte
- methemoglobinemia
-
nadph-cytochrome
- hereditary
- reductases
-
cyanosis
- fad
- ferricyanide
- flavoproteins
-
desaturation
- dt-diaphorase
- aniline
-
amidoxime
-
methb
-
hemolysate
-
bioreductive
- n-demethylase
- aminopyrine
-
marc
-
n-hydroxylated
-
mixed-function
-
nadh-binding
- methaemoglobin
- medicine
-
oxyhemoglobin
- diagnostics
- analysis
- industry
- drug development
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadh-cytochrome b5 reductase, cytochrome b5 reductase, methemoglobin reductase, cyb5r3, ncb5or, nadh cytochrome b5 reductase, nadh:cytochrome b5 reductase, cyb5r2, cytochrome-b5 reductase, cyb5r, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
B5R
CyB5R
cytochrome b5 reductase
dihydronicotinamide adenine dinucleotide-cytochrome b5 reductase
-
-
-
-
NADH-cytochrome b5 reductase
NADH-cytochrome-b5 reductase
-
-
-
-
NADH-ferricytochrome b5 oxidoreductase
-
-
-
-
P34/P32
-
-
-
-
P35
-
-
-
-
reduced nicotinamide adeninedinucleotide-cytochrome b5 reductase
-
-
-
-
reductase, cytochrome b5
-
-
-
-
B5R
-
-
-
-
cytochrome b5 reductase
-
-
-
-
NADH-cytochrome b5 reductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
NADH:ferricytochrome-b5 oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9032-25-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt + NADH
?
-
-
-
?
ferricytochrome b5 + 4-(5-(4-[amino(hydroxyamino)methyl]phenyl)-2-furyl)-N'-hydroxybenzenecarboximidamide
ferrocytochrome b5 + ?
-
metabolite of DB289, an antimicrobial prodrug of furamidine
-
-
?
ferricytochrome b5 + 4-(5-(4-[amino(hydroxyamino)methyl]phenyl)-2-furyl)-N'-methoxybenzenecarboximidamide
ferrocytochrome b5 + ?
-
metabolite of DB289, an antimicrobial prodrug of furamidine
-
-
?
ferricytochrome b5 + N-hydroxy-2-amino-1-methyl-6-phenylimidazol[4,5-b]pyridine
ferrocytochrome b5 + ?
-
arylhydroxylamine carcinogen found in grilled meat
-
-
?
ferricytochrome b5 + N-hydroxy-4-aminobiphenyl
ferrocytochrome b5 + ?
-
arylhydroxylamine carcinogen found in cigarette smoke
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
sulfamethoxazole hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
poor electron acceptors: methylene blue, ferricytochrome c, O2, oxidized glutathione, methemoglobin
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
artificial electron acceptor in the presence of menadione: cytochrome c
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
additional electron donors: deamino-NADH, 3-acetylpyridine-NADH
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
artificial acceptors: p-benzoquinone, 5-hydroxy-1,4-naphthoquinone, nitroblue-tetrazolium
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
additional acceptor: methemoglobin-ferrocyanide complex
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in metabolism of endogenous compounds such as steroids, drugs, carcinogens, environmental pollutants
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
enzyme participates in methemoglobin reduction in erythrocytes, in other tissues it plays a role in elongation and desaturation of fatty acids, P-450 mediated drug metabolism and cholesterol biosynthesis as part of the microsomal electron transfer system
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
soluble form of erythrocytes: reduction of methemoglobin
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
soluble form of erythrocytes: reduction of methemoglobin
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, enzyme in presence of cytochrome b5 supports activity of CYP2E1
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, participates in the regeneration of vitamin E and of ascorbate, maintains antioxidant levels and is therefore involved in the protection of membrane lipids from peroxidation, considered as a constitutive housekeeping enzyme
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
recessive congenital methaemoglobinaemia, is caused by NADH-cytochrome b5 reductase deficiency. Two distinct clinical forms, types I and II, are recognized, both characterized by cyanosis from birth. In type II, the cyanosis is accompanied by neurological impairment and reduced life expectancy
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
the electrostatic interactions between the lysyl residues (K42, K126, K163, and K164) in the enzyme and the carboxyl groups (E47, E48, E52, E60, and D64) of cytochrome b5 keep the proteins tightly complexed and are suitable for electron transfer, reaction mechanism, overview
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
potassium ferricyanide, cytochrome b5, or NADH-2,6-dichlorophenol-indophenol can act as electron acceptors
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sulfamethoxazole hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in metabolism of endogenous compounds such as steroids, drugs, carcinogens, environmental pollutants
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
enzyme participates in methemoglobin reduction in erythrocytes, in other tissues it plays a role in elongation and desaturation of fatty acids, P-450 mediated drug metabolism and cholesterol biosynthesis as part of the microsomal electron transfer system
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
soluble form of erythrocytes: reduction of methemoglobin
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
soluble form of erythrocytes: reduction of methemoglobin
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, enzyme in presence of cytochrome b5 supports activity of CYP2E1
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, participates in the regeneration of vitamin E and of ascorbate, maintains antioxidant levels and is therefore involved in the protection of membrane lipids from peroxidation, considered as a constitutive housekeeping enzyme
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
recessive congenital methaemoglobinaemia, is caused by NADH-cytochrome b5 reductase deficiency. Two distinct clinical forms, types I and II, are recognized, both characterized by cyanosis from birth. In type II, the cyanosis is accompanied by neurological impairment and reduced life expectancy
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
the electrostatic interactions between the lysyl residues (K42, K126, K163, and K164) in the enzyme and the carboxyl groups (E47, E48, E52, E60, and D64) of cytochrome b5 keep the proteins tightly complexed and are suitable for electron transfer, reaction mechanism, overview
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
cytochrome b5 reductase is composed of one FAD and one NADH binding domain linked by a hinge region
FAD
-
flavoprotein, the FAD domain has a large cleft in which the FAD prosthetic group is located. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains
FAD
the FAD group of cytochrome b5 reductase increases its solvent exposition upon complex formation with cytochrome b5 promoting an efficient electron transfer between the proteins
NADH
-
-
392811, 394195, 394196, 394199, 394200, 394203, 394210, 394213, 394216, 394222, 394225, 394234, 394235, 657460, 657648, 659107, 659784, 672826, 713187
NADH
-
preferred electron donor for CyB5R, a D239T mutation will change this preference to one for NADPH. The NADH domain provides a suitable position for the NADH coenzyme. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5Z)-5-[(9H-fluoren-3-yl)methylidene]-1-(4-methylphenyl)-2-sulfanylidenedihydropyrimidine-4,6(1H,5H)-dione
about 80% inhibition at 0.5 mM
(5Z)-5-{[4-bromo-5-(morpholin-4-yl)furan-2-yl]methylidene}-1-(4-methylphenyl)-2-sulfanylidenedihydropyrimidine-4,6(1H,5H)-dione
about 5% inhibition at 0.5 mM
1-(2-fluorophenyl)-5-[(1-methyl-2,3-dihydro-1H-indol-3-yl)methyl]-2-sulfanylidenedihydropyrimidine-4,6(1H,5H)-dione
about 75% inhibition at 0.5 mM
2-methyl-6-[(phenylsulfanyl)methyl]-2,5-dihydropyrimidin-4(3H)-one
about 5% inhibition at 0.5 mM
4-({[(2S)-2,3-dihydro-1,3-benzoxazol-2-yl]sulfanyl}methyl)tetrahydropyrimidine-2,5-dione
about 45% inhibition at 0.5 mM
5-(prop-2-en-1-yl)-6-propyl-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 75% inhibition at 0.5 mM
6-(pentyloxy)-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 25% inhibition at 0.05 mM
6-([[(2R)-2,3-dihydro-1,3-benzoxazol-2-yl]sulfanyl]methyl)-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
complete inhibition at 0.05 mM
6-benzyl-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 3% inhibition at 0.5 mM
6-pentyl-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 25% inhibition at 0.5 mM
6-[(phenylsulfanyl)methyl]-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
complete inhibition at 0.05 mM
6-[(phenylsulfanyl)methyl]pyrimidine-2,4(1H,3H)-dione
about 50% inhibition at 0.5 mM
6-{[(2,6-dichlorophenyl)sulfanyl]methyl}-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
complete inhibition at 0.05 mM
6-{[(4-bromophenyl)sulfanyl]methyl}-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 10% inhibition at 0.05 mM
6-{[(4-methylphenyl)sulfanyl]methyl}-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 85% inhibition at 0.05 mM
6-{[(propan-2-yl)sulfanyl]methyl}-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 18% inhibition at 0.05 mM
benzyl alcohol
-
100 mM, 52% inhibition, reversible, may be due to changes in membrane fluidity
K+ high ionic strength
-
reduction of cytochrome b5 or dichlorphenolindophenol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
ferricytochrome b5
-
enzyme from liver microsome membrane, solubilized with Triton X-100
0.045
ferricytochrome b5
-
enzyme from liver microsome membrane, cathepsin D solubilized
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00914
6-([[(2R)-2,3-dihydro-1,3-benzoxazol-2-yl]sulfanyl]methyl)-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
Homo sapiens
at pH 7.5 and 37°C
0.0108
6-[(phenylsulfanyl)methyl]-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
Homo sapiens
at pH 7.5 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
0.00017 mmol ferricyanide reduced/min/10000000 cells, activity in neutrophils
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Cytb5r enzyme activity is drastically reduced in all patients with recessive hereditary methemoglobinemia. Eight different mutations are detected among the twelve mutated alleles identified
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the microsomal isozyme consists of one hydrophobic membrane-anchoring domain and a larger hydrophilic flavin catalytic domain
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
CyB5R is a member of the NAD(P)H-ferredoxin reductase (FNR) enzyme superfamily, phylogenetic analysis
malfunction
metabolism
physiological function
additional information
-
the soluble CyB5R diffraction map reveals two distinct domains: the N-terminal FAD binding domain (from I34 to R143), which contains a binding site for the FAD prosthetic group, and the NADH domain (residues K173 to F301). These domains are separated by a large interdomain cleft (G144-V172) known as a hinge region. The three anti-parallel beta-sheets in the hinge region keep the two lobes in close proximity with the correct conformational orientation. This orientation appears to be critical for electron transfer from NADH to FAD. The FAD domain consists of six anti-parallel beta-sheets and one alpha-helix with the order 5beta/1alpha/1beta. The NADH domain forms a alpha/beta/aalpha structure consisting of five beta-strands and four alpha-helices
malfunction
-
congenital methemoglobinemia due to deficiency of NADH-cytochrome b5 reductase is an autosomal recessive disorder characterized by life long cyanosis
malfunction
-
autosomal cytochrome b5 reductase gene deficiency manifests with the accumulation of oxidized Fe+3 and recessive congenital methemoglobinemia in humans. Diseases related to CyB5R dysfunctions, overviews
malfunction
-
autosomal cytochrome b5 reductase gene deficiency manifests with the accumulation of oxidized Fe3+ and recessive congenital methemoglobinemia in humans
malfunction
-
recessive congenital methaemoglobinaemia is caused by a deficiency of NADH-cytochrome b5 reductase
malfunction
the cytochrome b5/cytochrome b5 reductase system is a viable reductant for cytoglobin in vivo
metabolism
-
2e- transfer from NADH to the enzyme CyB5R, to FAD, followed by reduction of 2 CyB5 and electron transfer to desaturase, CyP450 or methemoglobin
metabolism
an increase of cytochrome b5 reductase flavin autofluorescence is observed in the presence of cytochrome b5. A dissociation constant value between proteins of 0.5 microM and a 1:1 stoichiometry for the complex formation are calculated. A 30 mV negative shift of cytochrome b5 reductase redox potential in presence of cytochrome b5 is observed
metabolism
-
cytochrome b5 reductase mediates redox cycling of a variety of quinones generating superoxide anion, hydrogen peroxide, and, in the presence of transition metals, hydroxyl radicals. Redox cycling activity is oxygen-dependent and preferentially utilizes NADH as a cosubstrate. Quinone redox cycling inhibits reduction of cytochrome b5 by cytochrome b5 reductase under aerobic conditions
physiological function
-
cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. It takes part in many oxidation and reduction reactions, such as the reduction of methemoglobin to hemoglobin
physiological function
-
enzyme overexpression makes cells more resistant to H2O2 (oxidative stress), 2-deoxyglucose (metabolic stress), rotenone and antimycin A (energetic stress), and lactacystin (proteotoxic stress), but does not protect cells against H2O2 and serum withdrawal. Overexpression of the enzyme induces higher mitochondrial functions such as ATP production rate, oxygen consumption rate, and activities of complexes I and II, without formation of further reactive oxygen species, consistent with lower levels of oxidative/nitrative damage and resistance to apoptotic cell death
physiological function
NADH-cytochrome b5 reductase 3 promotes colonization and metastasis formation in estrogen receptor-negative breast cancer
physiological function
-
NADH-cytochrome-b5 reductase 3 is the principal reductase involved in the mitochondrial amidoxime reducing component enzyme system and is an essential component of N reductive metabolism in human cells
physiological function
the enzyme regulates nitric oxide diffusion in the artery wall
physiological function
-
the enzyme up-regulates the expression of genes that negatively modulate angiogenesis in nasopharyngeal carcinoma cells and down-regulates the expression of vascular endothelial growth factor to reduce angiogenesis, thereby suppressing tumor formation
physiological function
-
Cb5R can use O2 as an electron acceptor using NADH as substrate. Cb5R uses one NADH molecule to reduce two O2 molecules, leading to production of superoxide anion radicals. Cytochrome c binds to purified Cb5R isoforms with dissociation constants similar to the Km values for the cytochrome c-stimulated superoxide anion radical production by Cb5R isoforms and close to the Km value obtained for the NADH-dependent production of superoxide anion radicals by synaptic plasma membrane vesicles
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NB5R4_HUMAN
521
0
59474
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
36000
32000
-
x * 32000, enzyme from erythrocyte cytosol and liver microsomal enzyme solubilized with cathepsin D, SDS-PAGE
32000
-
x * 32000, enzyme from liver microsomes solubilized with Triton X-100, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 32000, enzyme from erythrocyte cytosol and liver microsomal enzyme solubilized with cathepsin D, SDS-PAGE
?
-
x * 32000, enzyme from liver microsomes solubilized with Triton X-100, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 2 M (NH4)2SO4, 100 mM sodium/potassium phosphate, pH 6.2, 200 mM Li2SO4, at 4°C
structure of a construct comprising the naturally fused CHORD-Sgt1 and b5R domains with bound FAD and NAD+ or NADP+. The linker between the CHORD-Sgt1 and b5R cores is more ordered than predicted, with much of it extending the beta-sandwich motif of the CHORD-Sgt1 domain. This limits the flexibility between the two domains
vapor equilibrium method, 3.6% protein solution, 30% polyethyleneglycol 4000, preliminary X-ray data
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A178T
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, 16.6% of wild-type enzyme activity
A179T
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
A179V
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
C204R
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
C204Y
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
D239G
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant shows decreased specificity for NADH and increased specificity for NADPH, 28.5% of wild-type enzyme activity
D239T
-
the mutation changes the enzme preference for NADH to one for NADPH. Diseases related to CyB5R dysfunctions due to mutations in the gene encoding the enzyme, detailed overview
D240G
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
E213K
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
E255-
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant retains stoichiometric levels FAD comparable to wild-type
F157C
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G143D
mutation in the NADH-cytochrome b5 reductase gene in an Indian patient with type I recessive hereditary methemoglobinemia
G144D
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G291D
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant retains stoichiometric levels FAD comparable to wild-type and 35.2% of wild-type enzyme activity
G292D
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G72A
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G75S
-
natural mutation isolated in patient with recessive congenital methemoglobinaemia. Mutant retains stoichiometric levels of FAD, but shows decreased catalytic efficiency and reduced protein stability
G75S/V252M
-
natural mutation isolated in patient with recessive congenital methemoglobinaemia. Mutant retains stoichiometric levels of FAD, but shows decreased catalytic efficiency and reduced protein stability
G76S
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
I216T
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
I85S
L149P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
L217P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
L218P
-
the mutation is associated with type I recessive congenital methemoglobinemia
L239R
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
L73P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
M127V
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P145L
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P145S
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P275L
natural mutant from a patient with recessive congenital methemoglobinemia. Significant decrease in the affinity toward the physiological reducing substrate, NADH, without affecting the activity
P276L
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P65L
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P96H
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R159-/D239G
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, 40.8% of wild-type enzyme activity
R241G
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R259W
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R46W
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R50Q
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R58Q
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
S128P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
S54R
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
V106M
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
V252M
-
natural mutation isolated in patient with recessive congenital methemoglobinaemia. Mutant retains stoichiometric levels of FAD, but shows decreased catalytic efficiency and reduced protein stability
V253M
additional information
I85S
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
V253M
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
additional information
naturally occurring mutations of CYB5R3 detected in patients with recessive congenital methaemoglobinaemia
additional information
-
naturally occurring mutations of CYB5R3 detected in patients with recessive congenital methaemoglobinaemia
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme from erythrocyte loses its activity in the absence of EDTA after 5 d at 4°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, phosphate buffered saline, pH 7.4, protein concentration 2-3 mg/ml, stable for 3 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA bead chromatography, HiTrap Q column chromatography, HiTrap phenyl column chromatography, and Superdex 200 gel filtration
DEAE-cellulose column chromatography, DEAE-Sepharose column chromatography, DEAE-Trisacryl column chromatography, agarose-hexane-NAD column chromatography, ADP-agarose column chromatography, 5'-AMP-Sepharose column chromatography, blue-Ultrogel column chromatography, octylamino-Sepharose column chromatography, blue 2-Sepharose column chromatography, Sephadex G-100 gel filtration, 5'-ADP-hexane-agarose column chromatography, hydroxyapatite column chromatography, CM-Sephadex gel filtration, or NAD agarose column chromatography
-
native membrane-bound isozyme by solubiization from membranes, anion exchange chromatography, and affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme coexpressed together with cytochrome b5 and CYP2E1or with CYP2E1 but without cytochrome b5 in Salmonella typhimurium strain 7108
-
expression in Escherichia coli
expression of wild-type, K110A, K110M and K110R mutant enzymes in Escherichia coli
-
heterologous expression in Escherichia coli or in yeast cells via different expression vectors, in Aspergillus oryzae using pNGA142, Salmonella typhimurium using pIN, in Spodoptera frugiperda Sf9 insect cells using pFASTBAC baculovirus vectors, in cell-free systems, in plant cells using pRT, in lymphoid cells using Epstein-Barr virus, and in CHO cells using SV40 transfection method
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme transcript levels are decreased in nasopharyngeal carcinoma cell lines and tumor biopsies
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
analysis
microplate method based on a standard 96-well microplate format to simplify the quantification of NADH-CYB5R activity. Enzyme activity in 25 diagnosed cases of recessive congenital methemoglobinemia ranges from 6.09 to 10.07 IU/g Hb whereas normal control ranges from 13.42 to 21.58 IU/g Hb. Hemolysate samples have significant loss of activity when stored at 4°C and retain stable activity at -20°C for 1 week
medicine
-
potentially an important enzyme required for the reductive activation of bioreductive drugs that can be used in the treatment of solid tumours
medicine
-
enzyme and cytochrome b5 play a direct role in metabolic activation of antimicrobial prodrug DB289 to furamidine
medicine
-
isolation of mutations leading to type I recessive congenital methaemoglobinaemia
medicine
natural mutant P275L from a patient with recessive congenital methemoglobinemia shows significant decrease in the affinity toward the physiological reducing substrate, NADH, without affecting the activity
medicine
-
reduction of arylhydroxylamine carcinogens by enzyme and ferricytochrome b5 as a source of individual variability with respect to cancer susceptibility following exposure to arylhydroxylamines
medicine
to establish a diagnosis of recessive congenital methaemoglobinaemia (RCM), it is important to demonstrate enzyme deficiency of cb5r and this is usually done using a spectrophotometric method,. RCM type I patients manifest a deficiency of cb5r in erythrocytes only whereas type II patients harbour the deficiency in both erythrocytes and leucocytes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kitajima, S.; Yasukochi, Y.; Minakami, S.
Purification and properties of human erythrocyte membrane NADH-cytochrome b5 reductase
Arch. Biochem. Biophys.
210
330-339
1981
Homo sapiens
Rigby, J.S.; Bull, P.C.; Ashworth, A.; Shephard, E.A.; Santisteban, I.; Phillips, I.R.
Isolation and characterization of genes coding for cytochrome b5 and cytochrome-b5 reductase
Biochem. Soc. Trans.
17
194-195
1989
Homo sapiens
-
Palmieri, D.A.; Rangachari, A.; Butterfield, D.A.
Effects of domain-specific erythrocyte membrane modulators on acetylcholinesterase and NADH:cytochrome b5 reductase activities
Arch. Biochem. Biophys.
280
224-228
1990
Homo sapiens
Shirabe, K.; Yubisui, T.; Takeshita, M.
Expression of human erythrocyte NADH-cytochrome b5 reductase as an alpha-thrombin-cleavable fused protein in Escherichia coli
Biochim. Biophys. Acta
1008
189-192
1989
Homo sapiens
Murakami, K.; Yubisui, T.; Takeshita, M.; Miyata, T.
The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases
J. Biochem.
105
312-317
1989
Homo sapiens
Takano, T.; Ogawa, K.; Sato, M.; Bando, S.; Yubisui, T.
Preliminary X-ray data of NADH-cytochrome b5 reductase from human erythrocytes
J. Mol. Biol.
195
749-750
1987
Oryctolagus cuniculus, Homo sapiens
Tauber, A.I.; Wright, J.; Higson, F.K.; Edelman, S.A.; Waxman, D.J.
Purification and characterization of the human neutrophil NADH-cytochrome b5 reductase
Blood
66
673-678
1985
Homo sapiens
Kitajima, S.; Minakami, S.
Human NADH-cytochrome b5 reductases: comparison among those of erythrocyte membrane, erythrocyte cytosol, and liver microsomes
J. Biochem.
93
615-620
1983
Homo sapiens
Badwey, J.A.; Tauber, A.I.; Karnovsky, M.L.
Properties of NADH-cytochrome-b5 reductase from human neutrophils
Blood
62
152-157
1983
Homo sapiens
Yubisui, T.; Takeshita, M.
Characterization of the purified NADH-cytochrome b5 reductase of human erythrocytes as a FAD-containing enzyme
J. Biol. Chem.
255
2454-2456
1980
Homo sapiens
Hultquist, D.E.
Methemoglobin reduction system of erythrocytes
Methods Enzymol.
52
463-473
1978
Homo sapiens
Ortiz de Montellano, P.R.
Cytochrome P450-Structure, Mechanism and Biochemistry
Cytochrome P450. Structure, Mechanism Biochem. (Ortiz de Montellano, P. R. ed. ) Plenum Press, New York
1986
Homo sapiens
-
Hultquist, D.E.; Passon, P.G.
Catalysis of methaemoglobin reduction by erythrocyte cytochrome b5 and cytochrome b5 reductase
Nat. New Biol.
229
252-254
1971
Homo sapiens
Yubisui, T.; Naitoh, Y.; Zenno, S.; Tamura, M.; Takeshita, M.; Sakaki, Y.
Molecular cloning of cDNAs of human liver and placenta NADH-cytochrome b5 reductase
Proc. Natl. Acad. Sci. USA
84
3609-3613
1987
Homo sapiens
Fujimoto, Y.; Shirabe, K.; Nagai, T.; Yubisui, T.; Takeshita, M.
Role of Lys-110 of human NADH-cytochrome b5 reductase in NADH binding as probed by site-directed mutagenesis
FEBS Lett.
322
30-32
1993
Homo sapiens
Mota Vieira, L.; Kaplan, J.C.; Kahn, A.; Leroux, A.
Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts resulting from multiple alternative first exons
Eur. J. Biochem.
220
729-737
1994
Homo sapiens, Rattus norvegicus
Barham, H.M.; Inglis, R.; Chinje, E.C.; Stratford, I.J.
Development and validation of a spectrophotometric assay for measuring the activity of NADH: cytochrome b5 reductase in human tumour cells
Br. J. Cancer
74
1188-1193
1996
Homo sapiens
Kawano, M.; Shirabe, K.; Nagai, T.; Takeshita, M.
Role of carboxyl residues surrounding heme of human cytochrome b5 in the electrostatic interaction with NADH-cytochrome b5 reductase
Biochem. Biophys. Res. Commun.
245
666-669
1998
Homo sapiens
Bando, S.; Takano, T.; Yubisui, T.; Shirabe, K.; Takeshita, M.; Nakagawa, A.
Structure of human erythrocyte NADH-cytochrome b5 reductase
Acta Crystallogr. Sect. D
60
1929-1934
2004
Homo sapiens
Mokashi, V.; Li, L.; Porter, T.D.
Cytochrome b5 reductase and cytochrome b5 support the CYP2E1-mediated activation of nitrosamines in a recombinant Ames test
Arch. Biochem. Biophys.
412
147-152
2003
Homo sapiens
Baker, M.A.; Krutskikh, A.; Curry, B.J.; Hetherington, L.; Aitken, R.J.
Identification of cytochrome-b5 reductase as the enzyme responsible for NADH-dependent lucigenin chemiluminescence in human spermatozoa
Biol. Reprod.
73
334-42
2005
Homo sapiens (Q6BCY4), Homo sapiens
Bello, R.I.; Alcain, F.J.; Gomez-Diaz, C.; Lopez-Lluch, G.; Navas, P.; Villalba, J.M.
Hydrogen peroxide- and cell-density-regulated expression of NADH-cytochrome b5 reductase in HeLa cells
J. Bioenerg. Biomembr.
35
169-179
2003
Homo sapiens
Kurian, J.R.; Bajad, S.U.; Miller, J.L.; Chin, N.A.; Trepanier, L.A.
NADH cytochrome b5 reductase and cytochrome b5 catalyze the microsomal reduction of xenobiotic hydroxylamines and amidoximes in humans
J. Pharmacol. Exp. Ther.
311
1171-1178
2004
Homo sapiens
Percy, M.J.; Crowley, L.J.; Boudreaux, J.; Barber, M.J.
Expression of a novel P275L variant of NADH:cytochrome b5 reductase gives functional insight into the conserved motif important for pyridine nucleotide binding
Arch. Biochem. Biophys.
447
59-67
2006
Homo sapiens (P00387), Homo sapiens
Percy, M.J.; Crowley, L.J.; Roper, D.; Vulliamy, T.J.; Layton, D.M.; Barber, M.J.
Identification and characterization of the novel FAD-binding lobe G75S mutation in cytochrome b(5) reductase: an aid to determine recessive congenital methemoglobinemia status in an infant
Blood Cells Mol. Dis.
36
81-90
2006
Homo sapiens
Percy, M.J.; Crowley, L.J.; Davis, C.A.; McMullin, M.F.; Savage, G.; Hughes, J.; McMahon, C.; Quinn, R.J.; Smith, O.; Barber, M.J.; Lappin, T.R.
Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase
Br. J. Haematol.
129
847-853
2005
Homo sapiens
Kurian, J.R.; Chin, N.A.; Longlais, B.J.; Hayes, K.L.; Trepanier, L.A.
Reductive detoxification of arylhydroxylamine carcinogens by human NADH cytochrome b5 reductase and cytochrome b5
Chem. Res. Toxicol.
19
1366-1373
2006
Homo sapiens
Saulter, J.Y.; Kurian, J.R.; Trepanier, L.A.; Tidwell, R.R.; Bridges, A.S.; Boykin, D.W.; Stephens, C.E.; Anbazhagan, M.; Hall, J.E.
Unusual dehydroxylation of antimicrobial amidoxime prodrugs by cytochrome b5 and NADH cytochrome b5 reductase
Drug Metab. Dispos.
33
1886-1893
2005
Homo sapiens
Kedar, P.S.; Warang, P.; Nadkarni, A.H.; Colah, R.B.; Ghosh, K.
A novel G143D mutation in the NADH-cytochrome b5 reductase gene in an Indian patient with type I recessive hereditary methemoglobinemia
Blood Cells Mol. Dis.
40
323-327
2008
Homo sapiens (P00387)
Fermo, E.; Bianchi, P.; Vercellati, C.; Marcello, A.P.; Garatti, M.; Marangoni, O.; Barcellini, W.; Zanella, A.
Recessive hereditary methemoglobinemia: two novel mutations in the NADH-cytochrome b5 reductase gene
Blood Cells Mol. Dis.
41
50-55
2008
Homo sapiens (P00387), Homo sapiens
Percy, M.J.; Lappin, T.R.
Recessive congenital methaemoglobinaemia: cytochrome b(5) reductase deficiency
Br. J. Haematol.
141
298-308
2008
Homo sapiens (P00387), Homo sapiens, Rattus norvegicus (P20070)
Percy, M.J.; Aslan, D.
NADH-cytochrome b5 reductase in a Turkish family with recessive congenital methaemoglobinaemia type I
J. Clin. Pathol.
61
1122-1123
2008
Homo sapiens
Deng, B.; Parthasarathy, S.; Wang, W.; Gibney, B.R.; Battaile, K.P.; Lovell, S.; Benson, D.R.; Zhu, H.
Study of the individual cytochrome b5 and cytochrome b5 reductase domains of Ncb5or reveals a unique heme pocket and a possible role of the CS domain
J. Biol. Chem.
285
30181-30191
2010
Homo sapiens (Q7L1T6), Homo sapiens
Arikoglu, T.; Yarali, N.; Kara, A.; Bay, A.; Bozkaya, I.O.; Tunc, B.; Percy, M.J.
A novel L218P mutation in NADH-cytochrome b5 reductase associated with type I recessive congenital methemoglobinemia
Pediatr. Hematol. Oncol.
26
381-385
2009
Homo sapiens
Elahian, F.; Sepehrizadeh, Z.; Moghimi, B.; Mirzaei, S.A.
Human cytochrome b5 reductase: structure, function, and potential applications
Crit. Rev. Biotechnol.
2012
1-11
2012
Homo sapiens
Rawa, K.; Chelmecka-Hanusiewicz, L.; Plochocka, D.; Pawinska-Wasikowska, K.; Balwierz, W.; Burzynska, B.
Characterization of a novel mutation in the NADH-cytochrome b5 reductase gene responsible for rare hereditary methaemoglobinaemia type I
Acta Haematol.
130
122-125
2013
Homo sapiens
Hyun, D.; Lee, G.
Cytochrome b5 reductase, a plasma membrane redox enzyme, protects neuronal cells against metabolic and oxidative stress through maintaining redox state and bioenergetics
Age (Dordr)
37
122
2015
Homo sapiens
Amdahl, M.B.; Sparacino-Watkins, C.E.; Corti, P.; Gladwin, M.T.; Tejero, J.
Efficient reduction of vertebrate cytoglobins by the cytochrome b5/cytochrome b5 reductase/NADH system
Biochemistry
56
3993-4004
2017
Homo sapiens (P00387), Homo sapiens
Ming, H.; Lan, Y.; He, F.; Xiao, X.; Zhou, X.; Zhang, Z.; Li, P.; Huang, G.
Cytochrome b5 reductase 2 suppresses tumor formation in nasopharyngeal carcinoma by attenuating angiogenesis
Chin. J. Cancer
34
459-467
2015
Homo sapiens
Elahian, F.; Sepehrizadeh, Z.; Moghimi, B.; Mirzaei, S.
Human cytochrome b5 reductase Structure, function, and potential applications
Crit. Rev. Biotechnol.
34
134-143
2014
Homo sapiens, Arabidopsis thaliana (A0A178US77), Bos taurus (P07514)
-
Plitzko, B.; Havemeyer, A.; Bork, B.; Bittner, F.; Mendel, R.; Clement, B.
Defining the role of the NADH-cytochrome-b5 reductase 3 in the mitochondrial amidoxime reducing component enzyme system
Drug Metab. Dispos.
44
1617-1621
2016
Homo sapiens
Zambo, V.; Toth, M.; Schlachter, K.; Szelenyi, P.; Sarnyai, F.; Lotz, G.; Csala, M.; Kereszturi, E.
Cytosolic localization of NADH cytochrome b5 oxidoreductase (Ncb5or)
FEBS Lett.
590
661-671
2016
Homo sapiens (Q7L1T6)
Rahaman, M.M.; Reinders, F.G.; Koes, D.; Nguyen, A.T.; Mutchler, S.M.; Sparacino-Watkins, C.; Alvarez, R.A.; Miller, M.P.; Cheng, D.; Chen, B.B.; Jackson, E.K.; Camacho, C.J.; Straub, A.C.
Structure guided chemical modifications of propylthiouracil reveal novel small molecule inhibitors of cytochrome b5 reductase 3 that increase nitric oxide bioavailability
J. Biol. Chem.
290
16861-16872
2015
Homo sapiens (P00387)
Lund, R.R.; Leth-Larsen, R.; Caterino, T.D.; Terp, M.G.; Nissen, J.; Laenkholm, A.V.; Jensen, O.N.; Ditzel, H.J.
NADH-cytochrome b5 reductase 3 promotes colonization and metastasis formation and is a prognostic marker of disease-free and overall survival in estrogen receptor-negative breast cancer
Mol. Cell. Proteomics
14
2988-2999
2015
Homo sapiens (P00387), Homo sapiens
Xiao, X.; Zhao, W.; Tian, F.; Zhou, X.; Zhang, J.; Huang, T.; Hou, B.; Du, C.; Wang, S.; Mo, Y.; Yu, N.; Zhou, S.; You, J.; Zhang, Z.; Huang, G.; Zeng, X.
Cytochrome b5 reductase 2 is a novel candidate tumor suppressor gene frequently inactivated by promoter hypermethylation in human nasopharyngeal carcinoma
Tumour Biol.
35
3755-3763
2014
Homo sapiens
Benson, D.; Lovell, S.; Mehzabeen, N.; Galeva, N.; Cooper, A.; Gao, P.; Battaile, K.; Zhu, H.
Crystal structures of the naturally fused CS and cytochrome b5 reductase (b5R) domains of Ncb5or reveal an expanded CS fold, extensive CS-b5R interactions and productive binding of the NAD(P)+ nicotinamide ring
Acta Crystallogr. Sect. D
75
628-638
2019
Homo sapiens (Q7L1T6)
Samhan-Arias, A.K.; Almeida, R.M.; Ramos, S.; Cordas, C.M.; Moura, I.; Gutierrez-Merino, C.; Moura, J.J.G.
Topography of human cytochrome b5/cytochrome b5 reductase interacting domain and redox alterations upon complex formation
Biochim. Biophys. Acta Bioenerg.
1859
78-87
2018
Homo sapiens (P00387)
Kedar, P.; Desai, A.; Warang, P.; Colah, R.
A microplate reader-based method to quantify NADH-cytochrome b5 reductase activity for diagnosis of recessive congenital methaemoglobinemia
Hematology
22
252-257
2017
Homo sapiens (P00387)
Samhan-Arias, A.K.; Fortalezas, S.; Cordas, C.M.; Moura, I.; Moura, J.J.G.; Gutierrez-Merino, C.
Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c
Redox Biol.
15
109-114
2018
Homo sapiens, Rattus norvegicus
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