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Enzyme Nomenclature
Information on EC 1.6.2.2 - cytochrome-b5 reductase
for references in articles please use BRENDA:EC1.6.2.2
Word Map on EC 1.6.2.2
- 1.6.2.2
- erythrocyte
- methemoglobinemia
-
nadph-cytochrome
- hereditary
- fad
-
cyanosis
-
reductases
- ferricyanide
-
flavoproteins
- dt-diaphorase
-
desaturation
- aniline
- aminopyrine
-
hemolysate
- stearoyl-coa
- n-demethylase
-
amidoxime
-
bioreductive
-
nadh-binding
- medicine
-
methaemoglobin
-
oxyhemoglobin
-
n-hydroxylated
-
mixed-function
-
marc
-
methb
- analysis
- industry
- diagnostics
- drug development
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.6.2.2
-
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RECOMMENDED NAME
GeneOntology No.
cytochrome-b5 reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
electron-transport chain from NADH to a terminal oxidase desaturase, proposed electron transfer mechanism
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
ordered bi bi mechanism
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
hypothetical mechanism
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
Y93 forms contact with the FAD, but neither P92 nor Y93 preceeding the conserved motif RxYTSxxSN coordinating flavin binding are critical for flavin incorporation
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
reaction mechanism, overview
-
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
NADH:ferricytochrome-b5 oxidoreductase
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
9032-25-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
392811, 394195, 394196, 394199, 394200, 394203, 394210, 394213, 394216, 394222, 394225, 394234, 394235, 394237, 394238, 394251, 657460, 657648, 659107, 659784, 672788, 673060, 699189, 713187, 724801, 741542, 741562, 742304, 742321, 742351, 743878
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-
deficiency leads to 2 different types of recessive congenital methemoglobinemia, in type 1 the soluble enzyme in erythrocytes is affected, in type 2 both soluble and membrane-bound isoforms are affected
-
-
patients with recessive hereditary methemoglobinemia due to cytochrome b5 reductase deficiency
SwissProt
sequence of natural mutant gene from a patient with recessive congenital methemoglobinemia; patients with recessive congenital methemoglobinemia
SwissProt
cytochrome b5/cytochrome b5 reductase fusion protein, exists also as a variant where the whole exon 12 is deleted
SwissProt
-
394198, 394207, 394217, 394230, 394232, 394233, 394240, 394241, 394243, 394244, 394247, 394250, 394260, 657966, 672516, 696154, 712873, 713204, 742271, 742308, 742561, 743151
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cytochrome b5/cytochrome b5 reductase fusion protein, exists also as a variant where the whole exon 12 is deleted
SwissProt
-
-
-
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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
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
-
the progeny of plants heterozygous for the cbr1-2 allele segregate 6% homozygous mutants, while cbr1-3 and cbr1-4 heterozygotes segregate 1:1 heterozygous:wild-type, indicating a gametophyte defect. Homozygous cbr1-2 seeds are deformed and required Suc for successful germination and seedling establishment. Vegetative growth of cbr1-2 plants was relatively normal, and they produced abundant flowers, but very few seeds. The pollen produced in cbr1-2 anthers is viable, but when germinated on cbr1-2 or wild-type stigmas, most of the resulting pollen tubes do not extend into the transmitting tract, resulting in a very low frequency of fertilization, phenotype, overview
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
malfunction
-
the enzyme is required for desaturation to biosynthesize polyunsaturated fatty acids
malfunction
-
autosomal cytochrome b5 reductase gene deficiency manifests with the accumulation of oxidized Fe3+ and recessive congenital methemoglobinemia in humans
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
-
the quantity of methemoglobin is kept in balance by an efficient redox system within erythrocytes involving the enzyme, overview
metabolism
-
the NADH/cytochrome b5/enzyme system can act as the sole electron donor both for the first and second reduction of cytochrome P450 1A1 during the oxidation of benzo[a]pyrene in vitro
metabolism
the enzyme is involved in fatty acid, sphingolipid and sterol metabolism
metabolism
-
cytochrome b5/cytochrome b5 reductase can act as a sole electron donor to the P450 system in vitro and in vivo
metabolism
-
the enzyme participates as an alternative electron donor pathway for P450 enzymes involved in ergosterol biosynthesis
metabolism
-
the enzyme participates as an alternative electron donor pathway for P450 enzymes involved in ergosterol biosynthesis
-
metabolism
Zymoseptoria tritici CBS 115943
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the enzyme is involved in fatty acid, sphingolipid and sterol metabolism
-
physiological function
-
cytochrome b5 reductase is responsible for the reduction of methemoglobin back to hemoglobin
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
-
methemoglobin in rainbow trout erythrocytes can be reduced by NADH-dependent cytochrome b5 reductase, i.e. CB5R, or NADPH-dependent methemoglobin reductase. The nucleated red blood cells of rainbow trout use membrane-bound CB5R to reduce methemoglobin
physiological function
-
the enzyme catalyzes the electron transfer from NADH to cytochrome b5 and participates in fatty acid synthesis, cholesterol synthesis, and xenobiotic oxidation as a member of the electron transport chain on the endoplasmic reticulum. In erythrocytes, the enzyme also participates in the reduction of methemoglobin
physiological function
-
cytochrome b5 reductase encoded by CBR1 is essential for a functional male gametophyte in Arabidopsis thaliana. It provides electrons, via cytochrome b5, for a range of biochemical reactions in cellular metabolism, including for fatty acid desaturation in the endoplasmic reticulum. Cytochrome b5 reductase is not essential during vegetative growth but is required for correct pollen function and seed maturation
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
-
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
-
cytochrome b5 reductase 3 expression and activity is critical for nitric oxide-stimulated cGMP production and vasodilation
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
-
NADH-cytochrome b5 reductase 3 promotes colonization and metastasis formation in estrogen receptor-negative breast cancer
physiological function
-
enzyme overexpression extends lifespan, survival and improves lipid metabolism in Drosophila melanogaster
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
additional information
-
the NADH-cytochrome b5 reductase is a flavoprotein consisting of NADH and FAD binding domains, that catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dihydro-8-(4-methylpiperazin-1-yl)-4-phenylimidazol[3,2-e]pyrazine 5-oxide + NADH
1,2-dihydro-8-(4-methylpiperazin-1-yl)-4-phenylimidazol[3,2-e]pyrazine + NAD+
-
potential bioreductive drug, trivial name RB90740
-
?
2 ferricytochrome b5 + NADPH
2 ferrocytochrome b5 + NADP+ + H+
with NADPH the enzyme shows about 20% of the activity with NADH
-
-
?
2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt + NADH
?
-
-
-
?
aquacobalamin + NADH
reduced aquacobalamin + NAD+
-
in the presence of outer membrane cytochrome b, no activity with cyanocobalamin
-
?
Fe3+-ammonium sulfate + NADH
Fe2+-ammonium sulfate + NAD+
-
strongly elevated by the addition of cytochrome b5
-
?
Fe3+-histidine + NADH
Fe2+-histidine + NAD+
-
strongly elevated by the addition of cytochrome b5
-
?
Fe3+-nitrilotriacetate + NADH
Fe2+-nitrilotriacetate + NAD+
-
in the presence of cytochrome b5, iron chelate reduction in descending order: Fe3+-nitrolotriacetate, Fe3+-ADP, Fe3+-diphosphate, Fe3+-citrate
-
?
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
-
-
?
methemoglobin-ferrocyanide complex + NADH
reduced methemoglobin-ferrocyanide complex + NAD+
-
-
-
?
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
NADH + oxidized nitroblue tetrazolium
NAD+ + H+ + reduced nitroblue tetrazolium
-
-
-
-
?
NADPH + ferricytochrome b5
NADP+ + H+ + ferrocytochrome b5
-
low affinity for NADPH
-
-
?
sulfamethoxazole hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
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+
-
no acceptors: ubiquinone-30, menadione, dihydrofolate, lipoamide
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
poor donor: NADPH
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
artificial acceptor: ferricyanide, high reactivity with NADPH as electron donor
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + 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
-
-
?
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
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, removal of reactive oxygen species
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
uses both NADH and NADPH as electron donors, artificial acceptors: ferricyanide, 2,6-dichlophenolindophenol
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
low activity with trypsin-solubilized cytochrome b5
-
-
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+
-
additional acceptor: hemin
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
poor donor: NADPH
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
additional acceptor: methemoglobin-ferrocyanide complex
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
artificial acceptor: ferricyanide
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
additional acceptor: methemerythrin
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + 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+
-
recombinant enzyme, very low activity with NADPH
-
-
-
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in desaturation of fatty acids
-
?
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 defects causes methemoglobinemia type I or type II
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, mutations can cause methemoglobinemia type I or II
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, removal of reactive oxygen species
-
-
?
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+
-
enzyme complex drives the entire sterol 14-demethylation reaction
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in desaturation of fatty acids
-
?
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+
-
membrane bound form of somatic cells: essential for lipid metabolism
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
enzyme is assumed to be part of an endoplasmic reticulum associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 to endoplasmic reticulum associated fatty acyl desaturase and related hydroxylases as in mammals
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
increases in the presence of cytochrome b5
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
in the presence of outer membrane cytochrome b
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
cytochrome b5/cytochrome b5 reductase FAD-domain-fusion protein, NADPH is preferred
-
-
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
reduces also ferricyanide
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
isoforms I and II, 16% and 27% of Fe3+-citrate reduction respectively
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
isoforms I and II, 16% and 27% of Fe3+-citrate reduction respectively
-
?
Cu2+-citrate + NADH
Cu+-citrate + NAD+
isoforms I and II, 59 and 47% of Fe3+-citrate reduction respectively
-
?
Cu2+-citrate + NADH
Cu+-citrate + NAD+
isoforms I and II, 59 and 47% of Fe3+-citrate reduction respectively
-
?
Fe3+-ATP + NADH
Fe2+-ATP + NAD+
-
reconstituted system containing NADH, cytochrome b5 reductase, cytochrome b5 and microsomal lipids catalyzes lipid peroxidation in the presence of ferric-ATP, ferric-histidine and ferric-ammonium sulfate
-
-
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
additional information
?
-
-
poor activity with the anticancer drug mitomycin C, no activity with anticancer drug idarubicin. The quinone antitumor agents are used in the treatment of several human neoplasms
-
-
-
additional information
?
-
role of enzyme in fatty acid desaturation and conjugation
-
-
-
additional information
?
-
-
role of enzyme in fatty acid desaturation and conjugation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
-
-
-
-
?
sulfamethoxazole hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
-
?
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+
Q6BCY4
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+
Q3TDX8
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, removal of reactive oxygen species
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in desaturation of fatty acids
-
?
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 defects causes methemoglobinemia type I or type II
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, mutations can cause methemoglobinemia type I or II
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
Q68EJ0
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, removal of reactive oxygen species
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
enzyme complex drives the entire sterol 14-demethylation reaction
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
involved in desaturation of fatty acids
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
P83686
involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
membrane bound form of somatic cells: essential for lipid metabolism
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
Q8W2K4
enzyme is assumed to be part of an endoplasmic reticulum associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 to endoplasmic reticulum associated fatty acyl desaturase and related hydroxylases as in mammals
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
A0A178US77
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
Zymoseptoria tritici CBS 115943
F9X691
-
-
-
?
additional information
?
-
-
poor activity with the anticancer drug mitomycin C, no activity with anticancer drug idarubicin. The quinone antitumor agents are used in the treatment of several human neoplasms
-
-
-
additional information
?
-
Q5PY86
role of enzyme in fatty acid desaturation and conjugation
-
-
-
additional information
?
-
-
role of enzyme in fatty acid desaturation and conjugation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
calculated results suggest that the electron and/or hydride ion transfer reaction from NADH to FAD can be accelerated in the presence of heme(Fe3+)
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
-
redox state of FAD during the b5R catalytic cycle and crystal structures comparion of the fully reduced form and the oxidized form, overview
FAD
-
-
NADH
-
-
392811, 394195, 394196, 394199, 394200, 394203, 394210, 394213, 394216, 394222, 394225, 394234, 394235, 657460, 657648, 658252, 659107, 659784, 672826, 712469, 713187
NADH
-
-
394198, 394207, 394211, 394217, 394230, 394232, 394233, 657675, 657966, 658832, 671983, 672018, 712873, 713204
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
NADH
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
additional information
-
enzyme does not contain appreciable amounts of iron, copper, manganes, silver, mercury, lead, zinc, cobalt or nickel
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
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
-
myricetin
-
noncompetitive versus NADH, non-linear relationship indicating non-Michaelis-Menten kinetic binding with respect to cytochrome b5
NAD+
-
competitive, stronger inhibition of mutant enzymes compared to wild type enzyme
additional information
-
inhibitory potencies of flavonoids on the enzyme, structure-activity relationship, overview. No inhibition by naringenin, naringin, and chrysin. Flavonoids containing two hydroxyl groups in ring B and a carbonyl group at C-4 in combination with a double bond between C-2 and C-3 produced a much stronger inhibition, whereas substitution of a hydroxyl group at C-3 is associated with a less inhibitory effect
-
additional information
-
enzyme inhibition by dietary flavonoids: inhibitor structure-activity analysis, overview. No inhibition by morin, apigenin, (+)-catechin, (-)-epicatechin, naringenin and naringin
-
additional information
-
species-specific sensitivity to methemoglobin induction, in vitro induction of methemoglobin by 1 mM NaNO2, overview
-
additional information
-
the enzyme is not inhibited by Mg2+, Mn2+, or EDTA
-
additional information
-
species-specific sensitivity to methemoglobin induction, in vitro induction of methemoglobin by 1 mM NaNO2, overview
-
additional information
-
species-specific sensitivity to methemoglobin induction, in vitro induction of methemoglobin by 1 mM NaNO2, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
cytochrome c
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
additional information
additional information
-
detailed analysis of biphasic rate of reduction of cytochrome b5 in membranes. The initial rapid phase is completed within 10 msec and over 90% of cytochrome b5 are reduced in 40 msec. Evaluation of data in terms of two-dimensional random walk model
-
0.035
cytochrome b5
-
enzyme from liver microsome membrane, solubilized with Triton X-100
-
0.045
cytochrome b5
-
enzyme from liver microsome membrane, cathepsin D solubilized
-
0.00104
ferricyanide
-
mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247L
0.00723
ferricyanide
-
; wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.008
ferricyanide
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.008
ferricyanide
-
L148P mutant enzyme, pH 7.0, 25°C; P144L/L148P mutant enzyme, pH 7.0, 25°C; P144L mutant enzyme, pH 7.0, 25°C; wild type enzyme, pH 7.0, 25°C
0.008
ferricyanide
-
mutant G179A, pH 7.0; mutant G179T, pH 7.0; wild-type, pH 7.0
0.01096
ferricyanide
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247A
0.01563
ferricyanide
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248A
0.01568
ferricyanide
-
mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248L
0.02646
ferricyanide
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249A
0.03309
ferricyanide
-
mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249L
0.013
ferricytochome b5
-
P144L/L148P mutant enzyme, pH 7.0, 25°C; wild type enzyme, pH 7.0, 25°C
-
0.01
ferricytochrome b5
-
mutant Y93D, pH 7.0, 25°C; mutant Y93H, pH 7.0, 25°C
0.011
ferricytochrome b5
-
mutant Y93F, pH 7.0, 25°C; mutant Y93W, pH 7.0, 25°C
0.012
ferricytochrome b5
-
mutant P92G, pH 7.0, 25°C; mutant P92S, pH 7.0, 25°C; mutant Y93S, pH 7.0, 25°C
0.01353
ferricytochrome b5
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0207
ferricytochrome b5
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.03434
ferricytochrome b5
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.04481
ferricytochrome b5
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.006
NADH
-
D239E mutant enzyme, pH 7.0, 25°C; wild type enzyme, pH 7.0, 25°C
0.01097
NADH
-
ferricyanide as electron acceptor; wild type enzyme, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0135
NADH
-
mutant enzyme P248L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248L, ferricyanide as electron acceptor
0.0155
NADH
-
mutant enzyme P249L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249L, ferricyanide as electron acceptor
0.01713
NADH
-
mutant enzyme P247A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247A, ferricyanide as electron acceptor
0.02407
NADH
-
mutant enzyme P248A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248A, ferricyanide as electron acceptor
0.02467
NADH
-
mutant enzyme P247L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247L, ferricyanide as electron acceptor
0.02928
NADH
-
mutant enzyme P249A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249A, ferricyanide as electron acceptor
0.001
NADPH
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.3
cytochrome c
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
21.7
ferricyanide
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
30.8
ferricyanide
-
mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247L
83
ferricyanide
-
mutant Y93D, pH 7.0, 25°C; mutant Y93H, pH 7.0, 25°C; mutant Y93W, pH 7.0, 25°C
337
ferricyanide
-
; wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
357
ferricyanide
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247A
399
ferricyanide
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248A
504
ferricyanide
-
mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248L
838
ferricyanide
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249A
1241
ferricyanide
-
mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249L
147
ferricytochrome b5
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
167
ferricytochrome b5
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
301
ferricytochrome b5
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
540
ferricytochrome b5
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
21.7
NADH
-
mutant enzyme P247L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247L, ferricyanide as electron acceptor
354
NADH
-
mutant enzyme P247A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P247A, ferricyanide as electron acceptor
540
NADH
-
mutant enzyme P248L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248L, ferricyanide as electron acceptor
559
NADH
-
mutant enzyme P248A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P248A, ferricyanide as electron acceptor
681
NADH
-
mutant enzyme P249A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249A, ferricyanide as electron acceptor
742
NADH
-
ferricyanide as electron acceptor; wild type enzyme, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
754
NADH
-
mutant D239G, pH 7.0; mutant E255-, pH 7.0; mutant G291D, pH 7.0; wild-type, pH 7.0
1059
NADH
-
mutant enzyme P249L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C; mutant P249L, ferricyanide as electron acceptor
50
NADPH
-
F251R mutant enzyme, pH 7.0, 25°C; F251Y mutant enzyme, pH 7.0, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
25530
ferricyanide
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
29620
ferricyanide
-
mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
31670
ferricyanide
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
32140
ferricyanide
-
mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
32570
ferricyanide
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
37500
ferricyanide
-
mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
46610
ferricyanide
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
80700
ferricytochrome b5
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
87700
ferricytochrome b5
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
108600
ferricytochrome b5
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
120500
ferricytochrome b5
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
880
NADH
-
mutant enzyme P247L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
20670
NADH
-
mutant enzyme P247A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
23220
NADH
-
mutant enzyme P248A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
23260
NADH
-
mutant enzyme P249A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
40000
NADH
-
mutant enzyme P248L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
67640
NADH
-
wild type enzyme, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
68320
NADH
-
mutant enzyme P249L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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