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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 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
2 ferricytochrome b5 + NADPH
2 ferrocytochrome b5 + NADP+ + H+
with NADPH the enzyme shows about 20% of the activity with NADH
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt + NADH
?
-
-
-
?
5alpha-dihydrotestosterone + acceptor
?
-
-
-
-
r
aquacobalamin + NADH
reduced aquacobalamin + NAD+
-
in the presence of outer membrane cytochrome b, no activity with cyanocobalamin
-
?
benzamidoxime + NADH
?
-
in the presence of cytochrome b5
-
-
?
Cu2+-citrate + NADH
Cu+-citrate + NAD+
dapsone hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
deoxyhemerythrin + O2
?
-
-
-
-
?
Fe3+-ammonium sulfate + NADH
Fe2+-ammonium sulfate + NAD+
-
strongly elevated by the addition of cytochrome b5
-
?
Fe3+-ATP + NADH
Fe2+-ATP + NAD+
Fe3+-citrate + NADH
Fe2+-citrate + NAD+
Fe3+-EDTA + NADH
Fe2+-EDTA + NAD+
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
-
-
?
lucigenin + NADH
?
-
-
-
?
methemerythrin + NADH
deoxymethemerythrin + NAD+
methemoglobin + NADH
hemoglobin + NAD+
-
provides functional hemoglobin
-
-
?
methemoglobin-ferrocyanide complex + NADH
reduced methemoglobin-ferrocyanide complex + NAD+
-
-
-
?
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
NADH + ferricytochrome b5
NAD+ + H+ + 2 ferrocytochrome b5
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
-
-
-
-
?
NADH + ferricytochrome c
NAD+ + H+ + ferrocytochrome c
NADH + methemoglobin
NAD+ + hemoglobin
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
NADH + oxidized cytochrome c
NAD+ + H+ + reduced cytochrome c
-
-
-
-
?
NADH + oxidized nitroblue tetrazolium
NAD+ + H+ + reduced nitroblue tetrazolium
-
-
-
-
?
NADH + testosterone
?
-
-
-
-
r
NADPH + ferricyanide
NADP+ + H+ + ferrocyanide
NADPH + ferricytochrome b5
NADP+ + H+ + ferrocytochrome b5
sulfamethoxazole hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
additional information
?
-
2 ferricyanide + NADH

2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADPH

2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + 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+
-
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+
-
-
-
-
?
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+
-
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
-
-
?
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 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+
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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 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+
reduces also ferricyanide
-
?
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
-
?
Fe3+-ATP + NADH
Fe2+-ATP + NAD+
-
ferric-EDTA is not reduced
-
?
Fe3+-citrate + NADH

Fe2+-citrate + NAD+
isoforms I and II
-
?
Fe3+-citrate + NADH
Fe2+-citrate + NAD+
isoforms I and II
-
?
Fe3+-citrate + NADH
Fe2+-citrate + NAD+
reduces also ferricyanide
-
?
Fe3+-EDTA + NADH

Fe2+-EDTA + NAD+
isoforms I and II
-
?
Fe3+-EDTA + NADH
Fe2+-EDTA + NAD+
isoforms I and II
-
?
Fe3+-EDTA + NADH
Fe2+-EDTA + NAD+
reduces also ferricyanide
-
?
methemerythrin + NADH

deoxymethemerythrin + NAD+
-
-
-
?
methemerythrin + NADH
deoxymethemerythrin + NAD+
-
-
-
?
NADH + ferricyanide

NAD+ + H+ + ferrocyanide
-
-
-
?
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
?
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
r
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
?
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
?
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
r
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
r
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
r
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
r
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
r
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
?
NADH + ferricyanide
NAD+ + H+ + ferrocyanide
-
-
-
-
?
NADH + ferricytochrome b5

NAD+ + H+ + 2 ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + 2 ferrocytochrome b5
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + 2 ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5

NAD+ + H+ + ferrocytochrome b5
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
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
-
-
-
-
r
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
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
-
-
-
?
NADH + ferricytochrome c

NAD+ + H+ + ferrocytochrome c
-
-
-
-
?
NADH + ferricytochrome c
NAD+ + H+ + ferrocytochrome c
-
-
-
-
r
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
-
-
-
-
r
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + H+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + ferricyanide

NADP+ + H+ + ferrocyanide
-
-
-
-
r
NADPH + ferricyanide
NADP+ + H+ + ferrocyanide
-
-
-
-
r
NADPH + ferricytochrome b5

NADP+ + H+ + ferrocytochrome b5
-
-
-
-
r
NADPH + ferricytochrome b5
NADP+ + H+ + ferrocytochrome b5
-
low affinity for NADPH
-
-
?
NADPH + ferricytochrome b5
NADP+ + H+ + ferrocytochrome b5
-
-
-
-
r
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.
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
5alpha-dihydrotestosterone + acceptor
?
-
-
-
-
r
benzamidoxime + NADH
?
-
in the presence of cytochrome b5
-
-
?
dapsone hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
deoxyhemerythrin + O2
?
-
-
-
-
?
methemoglobin + NADH
hemoglobin + NAD+
-
provides functional hemoglobin
-
-
?
NADH + ferricytochrome b5
NAD+ + H+ + ferrocytochrome b5
NADH + ferricytochrome b5 + oxidized soluble guanylate cyclase
NAD+ + H+ + ferrocytochrome b5 + reduced soluble guanylate cyclase
-
-
-
-
?
NADH + methemoglobin
NAD+ + hemoglobin
-
-
-
-
?
sulfamethoxazole hydroxylamine + NADH
?
-
in the presence of cytochrome b5
-
-
?
additional information
?
-
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+
-
-
-
-
?
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+
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
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+
-
-
-
-
?
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+
-
-
-
-
?
2 ferricytochrome b5 + NADH
2 ferrocytochrome b5 + NAD+ + H+
-
-
-
?
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
-
?
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 + 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 + 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
-
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(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'-(p-fluorosulfonylbenzoyl)-adenosine
-
-
5-(prop-2-en-1-yl)-6-propyl-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
about 75% inhibition at 0.5 mM
5-propyl-2-thiouracil
-
25 mM, almost complete inhibition
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-Propyl-2-thiouracil
-
about 20% residual activity at 0.009 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
apocynin
-
90.1% inhibition at 0.2 mM
benzoate
-
complete inhibition at 1 mM
benzyl alcohol
-
100 mM, 52% inhibition, reversible, may be due to changes in membrane fluidity
Br-
-
competitive vs. cytochrome b5, reversible by dilution
Ca2+
-
23.5% residual activity at 1 mM
CaCl2
-
8 mM, 50% inhibition, competitive vs. cytochrome b5
dithiothreitol
-
80% residual activity at 1 mM
ebselen
-
almost complete inhibition at 0.02 mM
F-
-
competitive vs. cytochrome b5, reversible by dilution
I-
-
competitive vs cytochrome b5, reversible by dilution
Inositol hexaphosphate
-
-
iodoacetate
-
27.3% residual activity at 1 mM
iodoacetic acid
-
5 mM, complete inhibition
luteolin-7-O-glucoside
-
-
Mersalyl
-
complete inhibition at 1.0 mM
MgCl2
-
78.1 mM, 50% inhibition, competitive vs. cytochrome b5
NaCN
-
91.4% residual activity at 1 mM
para-chloromercuribenzenesulfonate
-
phosphate
-
competitive inhibition
propylthiouracil
complete inhibition at 0.5 mM
Thenoyltrifluoroacetone
-
-
Tris
-
reduction of cytochrome b5
Wheat germ agglutinin
-
-
-
Acrynol

-
0.1 mM, 75% inhibition
Acrynol
-
0.1 mM, 88% inhibition
adenine nucleotides

-
-
ADP

-
-
ADP
-
5 mM, 66% inhibition
Atebrin

-
1 mM, complete inhibition
Atebrin
-
0.1 mM, 44% inhibition
Atebrin
-
0.5 mM, complete inhibition
Cl-

-
-
Cl-
-
competitive vs. cytochrome b5, reversible by dilution
dicoumarol

-
0.3 mM, 57% inhibition
iodoacetamide

-
1 mM, complete inhibition
iodoacetamide
-
23.5% residual activity at 1 mM
K+ high ionic strength

-
reduction of cytochrome b5 or dichlorphenolindophenol
-
K+ high ionic strength
-
-
-
myricetin

-
-
myricetin
-
noncompetitive versus NADH, non-linear relationship indicating non-Michaelis-Menten kinetic binding with respect to cytochrome b5
N-ethylmaleimide

-
10 mM, 89% inhibition
N-ethylmaleimide
-
8 mM, 70% inhibition
N-ethylmaleimide
-
1 mM, 90% inhibition
NAD+

competitive, stronger inhibition of mutant enzymes compared to wild type enzyme
p-chloromercuribenzoate

-
0.001 mM, complete inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
0.005 mM, complete inhibition
p-chloromercuribenzoate
-
0.001 mM, complete inhibition
p-chloromercuribenzoate
-
complete inhibition at 0.4 mM
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate

-
0.1 mM, almost complete inhibition
p-hydroxymercuribenzoate
-
0.1 mM, complete inhibition
p-hydroxymercuribenzoate
-
complete inhibition at 1 mM
Proflavin

-
0.1 mM, 86% inhibition
Proflavin
-
0.1 mM, 98% inhibition
Proflavin
-
0.1 mM, 74% inhibition
quercetin

-
-
quercetin
-
about 20% residual activity at 0.02 mM
taurodeoxycholate

-
-
taurodeoxycholate
-
20 mM, 84% inhibition
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
-
high levels of H2O2 inhibit enzyme expression
-
additional information
-
species-specific sensitivity to methemoglobin induction, in vitro induction of methemoglobin by 1 mM NaNO2, overview
-
additional information
-
not inhibited by NAD+ and ferrocyanide
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.63
benzamidoxime
-
pH 7.4
0.00114 - 0.042
cytochrome b5
-
0.36
dapsone hydroxylamine
-
pH 7.4
0.0006 - 4.35
ferricyanide
0.01 - 0.013
ferricytochome b5
-
0.000007 - 14
ferricytochrome b5
0.007
ferricytochrome c
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.001 - 0.107
ferrocytochrome b5
0.008
methemoglobin-ferrocyanide complex
-
-
-
0.25
N-hydroxy-2-amino-1-methyl-6-phenylimidazol[4,5-b]pyridine
-
pH 7.4
0.22
N-Hydroxy-4-aminobiphenyl
-
pH 7.4
0.328 - 0.83
oxidized 2,6-dichlorophenolindophenol
0.36
sulfamethoxazole hydroxylamine
-
pH 7.4
0.025 - 0.089
testosterone
-
depending on phosphate concentration
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
-
0.00114
cytochrome b5

-
-
-
0.0025
cytochrome b5
-
G273 mutant enzyme
-
0.0028
cytochrome b5
-
-
-
0.003
cytochrome b5
K110Q mutant enzyme
-
0.0031
cytochrome b5
-
H49K mutant enzyme
-
0.004
cytochrome b5
K110E mutant enzyme
-
0.0088
cytochrome b5
-
native enzyme
-
0.0089
cytochrome b5
-
H49A mutant enzyme
-
0.009
cytochrome b5
K110R mutant enzyme
-
0.009
cytochrome b5
K110A mutant enzyme
-
0.0091
cytochrome b5
-
recombinant wild-type enzyme
-
0.01
cytochrome b5
recombinant wild-type enzyme
-
0.011
cytochrome b5
-
H49Y mutant enzyme
-
0.012
cytochrome b5
K110H mutant enzyme
-
0.015
cytochrome b5
-
-
-
0.017
cytochrome b5
-
DELTAF272 mutant enzyme
-
0.03
cytochrome b5
-
H49E mutant enzyme
-
0.03 - 0.04
cytochrome b5
-
lysosome- and detergent-solubilized enzyme
-
0.0362
cytochrome b5
-
L125A mutant enzyme
-
0.042
cytochrome b5
-
L41A mutant enzyme
-
0.0006
ferricyanide

-
H49K mutant enzyme
0.00104
ferricyanide
-
mutant P247L
0.00104
ferricyanide
-
mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0016
ferricyanide
pH 7.0, 25°C,T66V mutant enzyme
0.0022
ferricyanide
-
H49E mutant enzyme
0.0022
ferricyanide
pH 7.0, 25°C,T66A mutant enzyme
0.0025
ferricyanide
-
native enzyme
0.0025
ferricyanide
pH 7.0, 25°C, wild type enzyme
0.0026
ferricyanide
-
H49Y mutant enzyme
0.0028
ferricyanide
-
recombinant wild-type enzyme
0.0028
ferricyanide
-
H49A mutant enzyme
0.0031
ferricyanide
pH 7.0, 25°C,T66S mutant enzyme
0.005
ferricyanide
K110R mutant enzyme
0.0052
ferricyanide
-
DELTAF272 mutant enzyme
0.0052
ferricyanide
-
G273 mutant enzyme
0.0058
ferricyanide
mutant Y93S, pH 7.0, 25°C
0.006
ferricyanide
-
wild-type
0.006
ferricyanide
recombinant wild-type enzyme
0.006
ferricyanide
mutant P275L, 25°C, pH 7.0
0.0066
ferricyanide
mutant Y93F, pH 7.0, 25°C
0.0068
ferricyanide
mutant Y93W, pH 7.0, 25°C
0.007
ferricyanide
-
recombinant enzyme
0.007
ferricyanide
-
pH 7.0, wild type enzyme
0.007
ferricyanide
wild-type, 25°C, pH 7.0
0.007
ferricyanide
mutant G179P, pH 7.0
0.007
ferricyanide
mutant G179V, pH 7.0
0.007
ferricyanide
-
mutant G75S
0.007
ferricyanide
-
mutant V252M
0.0071
ferricyanide
wild-type, pH 7.0, 25°C
0.00723
ferricyanide
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0074
ferricyanide
mutant P92A, pH 7.0, 25°C
0.0078
ferricyanide
mutant P92S, pH 7.0, 25°C
0.008
ferricyanide
wild-type, pH 7.0
0.008
ferricyanide
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.008
ferricyanide
-
pH 7.0, 25°C
0.008
ferricyanide
L148P mutant enzyme, pH 7.0, 25°C
0.008
ferricyanide
P144L mutant enzyme, pH 7.0, 25°C
0.008
ferricyanide
P144L/L148P mutant enzyme, pH 7.0, 25°C
0.008
ferricyanide
-
pH 7.0, S127P mutant enzyme
0.008
ferricyanide
wild type enzyme, pH 7.0, 25°C
0.008
ferricyanide
mutant G179A, pH 7.0
0.008
ferricyanide
mutant G179T, pH 7.0
0.008
ferricyanide
-
mutant G75S/V252M
0.008
ferricyanide
mutant P92G, pH 7.0, 25°C
0.0083
ferricyanide
mutant Y93D, pH 7.0, 25°C
0.0083
ferricyanide
mutant Y93H, pH 7.0, 25°C
0.0086
ferricyanide
mutant Y93A, pH 7.0, 25°C
0.01096
ferricyanide
-
mutant P247A
0.01096
ferricyanide
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0136
ferricyanide
-
in the presence of 2 mM Ca2+
0.01563
ferricyanide
-
mutant P248A
0.01563
ferricyanide
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.01568
ferricyanide
-
mutant P248L
0.01568
ferricyanide
-
mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.02646
ferricyanide
-
mutant P249A
0.02646
ferricyanide
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.03309
ferricyanide
-
mutant P249L
0.03309
ferricyanide
-
mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.05
ferricyanide
K110H mutant enzyme
0.345
ferricyanide
-
at pH 6.4 and 25°C
0.37
ferricyanide
K110E mutant enzyme
0.38
ferricyanide
K110A mutant enzyme
0.76
ferricyanide
K110Q mutant enzyme
0.01
ferricytochome b5

L148P mutant enzyme, pH 7.0, 25°C
-
0.012
ferricytochome b5
P144L mutant enzyme, pH 7.0, 25°C
-
0.013
ferricytochome b5
P144L/L148P mutant enzyme, pH 7.0, 25°C
-
0.013
ferricytochome b5
wild type enzyme, pH 7.0, 25°C
-
0.000007
ferricytochrome b5

-
-
0.000088
ferricytochrome b5
-
-
0.0008
ferricytochrome b5
-
-
0.0008
ferricytochrome b5
-
yeast cytochrome b5
0.00148
ferricytochrome b5
-
S99A mutant enzyme
0.0015
ferricytochrome b5
-
calf cytochrome b5
0.004
ferricytochrome b5
wild-type, 25°C, pH 7.0
0.005
ferricytochrome b5
-
Y65A mutant enzyme
0.0053
ferricytochrome b5
-
in the presence of 2 mM Ca2+
0.0062
ferricytochrome b5
-
Y65F mutant enzyme
0.0066
ferricytochrome b5
-
recombinant wild-type enzyme
0.0069
ferricytochrome b5
-
K97R mutant enzyme
0.00693
ferricytochrome b5
-
mutant P247L
0.0073
ferricytochrome b5
-
R63K mutant enzyme
0.009
ferricytochrome b5
-
-
0.0099
ferricytochrome b5
-
S99V mutant enzyme
0.01
ferricytochrome b5
mutant Y93D, pH 7.0, 25°C
0.01
ferricytochrome b5
mutant Y93H, pH 7.0, 25°C
0.0104
ferricytochrome b5
-
recombinant wild-type enzyme
0.011
ferricytochrome b5
-
recombinant enzyme
0.011
ferricytochrome b5
mutant Y93F, pH 7.0, 25°C
0.011
ferricytochrome b5
mutant Y93W, pH 7.0, 25°C
0.0118
ferricytochrome b5
-
S99T mutant enzyme
0.012
ferricytochrome b5
mutant P275L, 25°C, pH 7.0
0.012
ferricytochrome b5
mutant P92G, pH 7.0, 25°C
0.012
ferricytochrome b5
mutant P92S, pH 7.0, 25°C
0.012
ferricytochrome b5
mutant Y93S, pH 7.0, 25°C
0.013
ferricytochrome b5
-
-
0.013
ferricytochrome b5
-
wild-type
0.013
ferricytochrome b5
wild-type, pH 7.0, 25°C
0.013
ferricytochrome b5
pH 7.0, 25°C,T66S mutant enzyme
0.013
ferricytochrome b5
-
pH 7.0, wild type enzyme
0.013
ferricytochrome b5
-
mutant V252M
0.01353
ferricytochrome b5
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.014
ferricytochrome b5
-
0.014
ferricytochrome b5
-
pH 7.0, S127P mutant enzyme
0.014
ferricytochrome b5
-
mutant G75S
0.014
ferricytochrome b5
-
mutant G75S/V252M
0.014
ferricytochrome b5
mutant Y93A, pH 7.0, 25°C
0.0142
ferricytochrome b5
-
recombinant K110A mutant enzyme
0.0143
ferricytochrome b5
-
-
0.015
ferricytochrome b5
mutant P92A, pH 7.0, 25°C
0.0161
ferricytochrome b5
-
K97A mutant enzyme
0.0167
ferricytochrome b5
-
recombinant K110R mutant enzyme
0.01735
ferricytochrome b5
-
-
0.0185
ferricytochrome b5
-
R63Q mutant enzyme
0.02
ferricytochrome b5
-
enzyme from eythrocyte membrane
0.02
ferricytochrome b5
-
enzyme from erythrocyte membrane
0.02
ferricytochrome b5
pH 7.0, 25°C, wild type enzyme
0.0207
ferricytochrome b5
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.024
ferricytochrome b5
-
-
0.02407
ferricytochrome b5
-
mutant P247A
0.0285
ferricytochrome b5
-
recombinant K110M mutant enzyme
0.03434
ferricytochrome b5
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0349
ferricytochrome b5
-
-
0.035
ferricytochrome b5
-
enzyme from liver microsome membrane, solubilized with Triton X-100
0.04
ferricytochrome b5
-
enzyme from eythrocyte cytosol
0.04148
ferricytochrome b5
-
mutant P248A
0.0421
ferricytochrome b5
-
R63A mutant enzyme
0.04481
ferricytochrome b5
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.045
ferricytochrome b5
-
enzyme from liver microsome membrane, cathepsin D solubilized
0.05238
ferricytochrome b5
-
mutant P249A
0.055
ferricytochrome b5
-
mutant P249L
0.08199
ferricytochrome b5
-
mutant P248L
0.111
ferricytochrome b5
pH 7.0, 25°C,T66V mutant enzyme
0.125
ferricytochrome b5
pH 7.0, 25°C,T66A mutant enzyme
14
ferricytochrome b5
-
-
0.001
ferrocytochrome b5

mutant G179P, pH 7.0
0.008
ferrocytochrome b5
mutant G179A, pH 7.0
0.012
ferrocytochrome b5
-
pH 7.0, 25°C
0.013
ferrocytochrome b5
wild-type, pH 7.0
0.043
ferrocytochrome b5
mutant G179T, pH 7.0
0.107
ferrocytochrome b5
mutant G179V, pH 7.0
0.00016
NADH

-
enzyme from erythrocyte
0.0003
NADH
-
H49E mutant enzyme
0.0004 - 0.0005
NADH
-
lysosome- and detergent-solubilized enzyme
0.0006
NADH
-
recombinant wild-type enzyme
0.0006
NADH
-
enzyme from erythrocyte membrane
0.0006 - 0.0007
NADH
-
enzyme from erythrocyte and liver
0.00064
NADH
-
G273 mutant enzyme
0.00084
NADH
-
DELTAF272 mutant enzyme
0.0015
NADH
-
recombinant wild-type enzyme
0.0016
NADH
-
native enzyme
0.0019
NADH
-
H49A mutant enzyme
0.0019
NADH
-
S99T mutant enzyme
0.0021
NADH
-
R63K mutant enzyme
0.0023
NADH
-
recombinant K110R mutant enzyme
0.0027
NADH
-
H49Y mutant enzyme
0.0028
NADH
pH 7.0, 25°C,T66S mutant enzyme
0.0028
NADH
pH 7.0, 25°C,T66V mutant enzyme
0.0028
NADH
-
at pH 7.4 and 37°C
0.0029
NADH
-
K97R mutant enzyme
0.0029
NADH
pH 7.0, 25°C,T66A mutant enzyme
0.003
NADH
-
Y65F mutant enzyme
0.003
NADH
F251Y mutant enzyme, pH 7.0, 25°C
0.003
NADH
-
pH 7.0, wild type enzyme with cytochrome b5 as substrate
0.0031
NADH
-
recombinant wild-type enzyme
0.0031
NADH
pH 7.0, 25°C, wild type enzyme
0.0038
NADH
mutant Y93S, pH 7.0, 25°C
0.0042
NADH
-
Y65A mutant enzyme
0.0044
NADH
-
K97A mutant enzyme
0.0048
NADH
mutant P92A, pH 7.0, 25°C
0.0049
NADH
mutant Y93D, pH 7.0, 25°C
0.005
NADH
D239S/F251Y mutant enzyme, pH 7.0, 25°C
0.006
NADH
-
recombinant enzyme
0.006
NADH
wild-type, pH 7.0
0.006
NADH
wild-type, pH 7.0, 25°C
0.006
NADH
D239E mutant enzyme, pH 7.0, 25°C
0.006
NADH
-
pH 7.0, wild type enzyme with ferricyanide as substrate
0.006
NADH
wild type enzyme, pH 7.0, 25°C
0.006
NADH
mutant P275L, cosubstrate ferricyanide, 25°C, pH 7.0
0.0065
NADH
mutant P92G, pH 7.0, 25°C
0.0067
NADH
mutant Y93F, pH 7.0, 25°C
0.007
NADH
-
pH 7.0, 25°C
0.0073
NADH
mutant Y93A, pH 7.0, 25°C
0.0077
NADH
mutant P92S, pH 7.0, 25°C
0.0088
NADH
mutant Y93H, pH 7.0, 25°C
0.0094
NADH
-
S99V mutant enzyme
0.01
NADH
-
H49K mutant enzyme
0.01097
NADH
-
ferricyanide as electron acceptor
0.01097
NADH
-
wild type enzyme, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0112
NADH
-
in the presence of 2 mM Ca2+
0.012
NADH
F251R mutant enzyme, pH 7.0, 25°C
0.0135
NADH
-
mutant P248L, ferricyanide as electron acceptor
0.0135
NADH
-
mutant enzyme P248L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
0.0155
NADH
-
mutant P249L, 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
0.017
NADH
D239S mutant enzyme, pH 7.0, 25°C
0.017
NADH
-
mutant G75S/V252M
0.01713
NADH
-
mutant P247A, 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
0.021
NADH
-
R63Q mutant enzyme
0.02407
NADH
-
mutant P248A, 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
0.02467
NADH
-
mutant P247L, 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
0.025
NADH
-
pH 7.0, S127P mutant enzyme with cytochrome b5 as substrate
0.025
NADH
mutant G179A, pH 7.0
0.026
NADH
-
S99A mutant enzyme
0.02928
NADH
-
mutant P249A, 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
0.052
NADH
-
mutant V252M
0.054
NADH
mutant Y93W, pH 7.0, 25°C
0.055
NADH
-
pH 7.0, S127P mutant enzyme with ferricyanide as substrate
0.104
NADH
-
R63A mutant enzyme
0.119
NADH
D239T mutant enzyme, pH 7.0, 25°C
0.121
NADH
-
recombinant K110A mutant enzyme
0.224
NADH
D239S/F251R mutant enzyme, pH 7.0, 25°C
0.512
NADH
D239T/F251R mutant enzyme, pH 7.0, 25°C
0.595
NADH
mutant G179P, pH 7.0
0.662
NADH
mutant G179T, pH 7.0
0.672
NADH
-
recombinant K110M mutant enzyme
1.077
NADH
mutant G179V, pH 7.0
2.623
NADH
wild-type, cosubstrate ferricyanide, 25°C, pH 7.0
0.001
NADPH

-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
0.009
NADPH
D239T mutant enzyme, pH 7.0, 25°C
0.022
NADPH
D239S/F251R mutant enzyme, pH 7.0, 25°C
0.025
NADPH
D239S/F251Y mutant enzyme, pH 7.0, 25°C
0.044
NADPH
D239T/F251R mutant enzyme, pH 7.0, 25°C
0.094
NADPH
D239E mutant enzyme, pH 7.0, 25°C
0.138
NADPH
F251R mutant enzyme, pH 7.0, 25°C
0.268
NADPH
D239S mutant enzyme, pH 7.0, 25°C
0.375
NADPH
mutant G179V, pH 7.0
0.507
NADPH
mutant G179T, pH 7.0
0.617
NADPH
F251Y mutant enzyme, pH 7.0, 25°C
0.924
NADPH
wild-type, pH 7.0
0.924
NADPH
wild type enzyme, pH 7.0, 25°C
1.36
NADPH
mutant G179A, pH 7.0
2.317
NADPH
mutant G179P, pH 7.0
0.328
oxidized 2,6-dichlorophenolindophenol

-
at pH 6.4 and 25°C
0.83
oxidized 2,6-dichlorophenolindophenol
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50.2
2,6-dichlorophenolindophenol
-
-
33 - 417
ferricytochome b5
-
1 - 911
ferricytochrome b5
10 - 600
ferrocytochrome b5
12
ferricyanide

mutant G179V, pH 7.0
21.7
ferricyanide
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
30.8
ferricyanide
-
mutant P247L
30.8
ferricyanide
-
mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
33
ferricyanide
mutant G179T, pH 7.0
40
ferricyanide
K110Q mutant enzyme
42
ferricyanide
mutant G179P, pH 7.0
76
ferricyanide
-
G273 mutant enzyme
77
ferricyanide
pH 7.0, 25°C,T66V mutant enzyme
83
ferricyanide
mutant Y93D, pH 7.0, 25°C
83
ferricyanide
mutant Y93H, pH 7.0, 25°C
83
ferricyanide
mutant Y93W, pH 7.0, 25°C
98.3
ferricyanide
-
enzyme from liver microsomes, protease solubilized
100
ferricyanide
P144L/L148P mutant enzyme, pH 7.0, 25°C
110
ferricyanide
-
H49E mutant enzyme
120
ferricyanide
K110E mutant enzyme
133
ferricyanide
-
mutant G75S
133
ferricyanide
mutant Y93S, pH 7.0, 25°C
187
ferricyanide
-
mutant G75S/V252M
200
ferricyanide
mutant Y93A, pH 7.0, 25°C
270
ferricyanide
K110A mutant enzyme
283
ferricyanide
P144L mutant enzyme, pH 7.0, 25°C
300
ferricyanide
L148P mutant enzyme, pH 7.0, 25°C
300
ferricyanide
-
pH 7.0, S127P mutant enzyme
337
ferricyanide
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
340
ferricyanide
K110H mutant enzyme
357
ferricyanide
-
mutant P247A
357
ferricyanide
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
399
ferricyanide
-
mutant P248A
399
ferricyanide
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
400
ferricyanide
-
DELTAF272 mutant enzyme
467
ferricyanide
mutant P92G, pH 7.0, 25°C
470
ferricyanide
-
H49A mutant enzyme
470
ferricyanide
K110R mutant enzyme
483
ferricyanide
mutant Y93F, pH 7.0, 25°C
490
ferricyanide
-
H49K mutant enzyme
504
ferricyanide
-
mutant P248L
504
ferricyanide
-
mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
517
ferricyanide
mutant P92A, pH 7.0, 25°C
559
ferricyanide
mutant G179A, pH 7.0
630
ferricyanide
-
native enzyme
633
ferricyanide
-
mutant V252M
677
ferricyanide
-
enzyme from erythrocyte membrane
684
ferricyanide
pH 7.0, 25°C,T66A mutant enzyme
700
ferricyanide
-
enzyme from erythrocyte cytosol
727
ferricyanide
-
H49Y mutant enzyme
767
ferricyanide
-
pH 7.0, 25°C
800
ferricyanide
-
wild-type
800
ferricyanide
recombinant wild-type enzyme
800
ferricyanide
wild-type, pH 7.0, 25°C
800
ferricyanide
-
pH 7.0, wild type enzyme
800
ferricyanide
wild type enzyme, pH 7.0, 25°C
800
ferricyanide
wild-type, pH 7.0
810
ferricyanide
-
recombinant wild-type enzyme
822
ferricyanide
pH 7.0, 25°C, wild type enzyme
827
ferricyanide
-
enzyme from liver microsomes, detergent solubilized
838
ferricyanide
-
mutant P249A
838
ferricyanide
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
880
ferricyanide
mutant P92S, pH 7.0, 25°C
976
ferricyanide
pH 7.0, 25°C,T66S mutant enzyme
1241
ferricyanide
-
mutant P249L
1241
ferricyanide
-
mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
33
ferricytochome b5

P144L/L148P mutant enzyme, pH 7.0, 25°C
-
117
ferricytochome b5
P144L mutant enzyme, pH 7.0, 25°C
-
130
ferricytochome b5
L148P mutant enzyme, pH 7.0, 25°C
-
417
ferricytochome b5
wild type enzyme, pH 7.0, 25°C
-
1
ferricytochrome b5

K110E mutant enzyme
4
ferricytochrome b5
K110Q mutant enzyme
8.3
ferricytochrome b5
-
cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein
14
ferricytochrome b5
mutant Y93D, pH 7.0, 25°C
19
ferricytochrome b5
mutant Y93W, pH 7.0, 25°C
21.3
ferricytochrome b5
-
-
27
ferricytochrome b5
mutant Y93H, pH 7.0, 25°C
27.2
ferricytochrome b5
-
mutant P247L
32
ferricytochrome b5
mutant Y93S, pH 7.0, 25°C
38
ferricytochrome b5
pH 7.0, 25°C,T66V mutant enzyme
57
ferricytochrome b5
-
G273 mutant enzyme
57
ferricytochrome b5
mutant Y93A, pH 7.0, 25°C
60
ferricytochrome b5
-
mutant G75S
67
ferricytochrome b5
mutant P275L, 25°C, pH 7.0
85
ferricytochrome b5
-
mutant G75S/V252M
90
ferricytochrome b5
K110A mutant enzyme
105
ferricytochrome b5
-
R63Q mutant enzyme
106
ferricytochrome b5
-
pH 7.0, S127P mutant enzyme
107
ferricytochrome b5
-
Y65A mutant enzyme
110
ferricytochrome b5
K110H mutant enzyme
121
ferricytochrome b5
-
R63A mutant enzyme
125
ferricytochrome b5
-
L41A mutant enzyme
147
ferricytochrome b5
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
160
ferricytochrome b5
-
H49E mutant enzyme
165
ferricytochrome b5
-
S99V mutant enzyme
167
ferricytochrome b5
-
-
167
ferricytochrome b5
-
mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
191
ferricytochrome b5
-
K97A mutant enzyme
200
ferricytochrome b5
K110R mutant enzyme
200
ferricytochrome b5
-
mutant P247A
270
ferricytochrome b5
recombinant wild-type enzyme
270
ferricytochrome b5
-
mutant P249L
275
ferricytochrome b5
-
mutant P248L
285
ferricytochrome b5
-
mutant V252M
288
ferricytochrome b5
-
mutant P248A
295
ferricytochrome b5
-
S99A mutant enzyme
295
ferricytochrome b5
mutant Y93F, pH 7.0, 25°C
301
ferricytochrome b5
-
mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
305
ferricytochrome b5
-
Y65F mutant enzyme
314
ferricytochrome b5
pH 7.0, 25°C,T66A mutant enzyme
315
ferricytochrome b5
mutant P92S, pH 7.0, 25°C
320
ferricytochrome b5
mutant P92A, pH 7.0, 25°C
335
ferricytochrome b5
mutant P92G, pH 7.0, 25°C
347
ferricytochrome b5
-
R63K mutant enzyme
360
ferricytochrome b5
-
wild-type
367
ferricytochrome b5
-
pH 7.0, wild type enzyme
380
ferricytochrome b5
-
H49A mutant enzyme
400
ferricytochrome b5
wild-type, pH 7.0, 25°C
415
ferricytochrome b5
-
K97R mutant enzyme
420
ferricytochrome b5
-
H49K mutant enzyme
441
ferricytochrome b5
-
mutant P249A
450
ferricytochrome b5
-
DELTAF272 mutant enzyme
472
ferricytochrome b5
-
L125A mutant enzyme
510
ferricytochrome b5
-
native enzyme
520
ferricytochrome b5
-
S99T mutant enzyme
540
ferricytochrome b5
-
mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
560
ferricytochrome b5
-
recombinant wild-type enzyme
563
ferricytochrome b5
-
recombinant K110M mutant enzyme
580
ferricytochrome b5
-
H49Y mutant enzyme
600
ferricytochrome b5
wild-type, 25°C, pH 7.0
661
ferricytochrome b5
-
recombinant wild-type enzyme
705
ferricytochrome b5
pH 7.0, 25°C,T66S mutant enzyme
742
ferricytochrome b5
-
recombinant K110A mutant enzyme
872
ferricytochrome b5
-
recombinant wild-type enzyme
877
ferricytochrome b5
-
recombinant K110R mutant enzyme
911
ferricytochrome b5
pH 7.0, 25°C, wild type enzyme
10
ferrocytochrome b5

mutant G179P, pH 7.0
17
ferrocytochrome b5
mutant G179V, pH 7.0
18
ferrocytochrome b5
mutant G179T, pH 7.0
245
ferrocytochrome b5
mutant G179A, pH 7.0
400
ferrocytochrome b5
wild-type, pH 7.0
600
ferrocytochrome b5
-
pH 7.0, 25°C
0.733
NADH

wild-type, cosubstrate ferricyanide, 25°C, pH 7.0
0.8
NADH
mutant P275L, cosubstrate ferricyanide, 25°C, pH 7.0
21.7
NADH
-
mutant P247L, ferricyanide as electron acceptor
21.7
NADH
-
mutant enzyme P247L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
53
NADH
-
G273 mutant enzyme
77
NADH
-
H49E mutant enzyme
100
NADH
pH 7.0, 25°C,T66V mutant enzyme
180
NADH
-
Y65A mutant enzyme
250
NADH
D239S/F251R mutant enzyme, pH 7.0, 25°C
310
NADH
-
DELTAF272 mutant enzyme
333
NADH
D239T mutant enzyme, pH 7.0, 25°C
354
NADH
-
mutant P247A, 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
367
NADH
F251Y mutant enzyme, pH 7.0, 25°C
375
NADH
-
S99V mutant enzyme
403
NADH
-
R63A mutant enzyme
412
NADH
-
R63Q mutant enzyme
433
NADH
D239S mutant enzyme, pH 7.0, 25°C
435
NADH
-
S99A mutant enzyme
440
NADH
-
H49A mutant enzyme
467
NADH
D239S/F251Y mutant enzyme, pH 7.0, 25°C
500
NADH
F251R mutant enzyme, pH 7.0, 25°C
501
NADH
-
Y65F mutant enzyme
515
NADH
-
R63K mutant enzyme
517
NADH
D239E mutant enzyme, pH 7.0, 25°C
540
NADH
-
mutant P248L, 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
559
NADH
-
mutant P248A, 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
570
NADH
-
recombinant wild-type enzyme
681
NADH
-
mutant P249A, 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
710
NADH
-
H49K mutant enzyme
717
NADH
D239T/F251R mutant enzyme, pH 7.0, 25°C
742
NADH
-
ferricyanide as electron acceptor
742
NADH
-
wild type enzyme, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
750
NADH
-
H49Y mutant enzyme
754
NADH
-
wild-type, pH 7.0
754
NADH
-
mutant D239G, pH 7.0
754
NADH
-
mutant E255-, pH 7.0
754
NADH
-
mutant G291D, pH 7.0
800
NADH
wild type enzyme, pH 7.0, 25°C
851
NADH
-
S99T mutant enzyme
909
NADH
-
K97R mutant enzyme
984
NADH
pH 7.0, 25°C,T66A mutant enzyme
1059
NADH
-
mutant P249L, ferricyanide as electron acceptor
1059
NADH
-
mutant enzyme P249L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C
1060
NADH
-
K97A mutant enzyme
1100
NADH
-
recombinant wild-type enzyme
1100
NADH
pH 7.0, 25°C, wild type enzyme
1150
NADH
pH 7.0, 25°C,T66S mutant enzyme
3
NADPH

-
mutant E255-, pH 7.0
5.2
NADPH
D239E mutant enzyme, pH 7.0, 25°C
8
NADPH
mutant G179V, pH 7.0
12
NADPH
mutant G179T, pH 7.0
17
NADPH
mutant G179P, pH 7.0
19
NADPH
-
mutant G291D, pH 7.0
33
NADPH
wild type enzyme, pH 7.0, 25°C
33
NADPH
-
wild-type, pH 7.0
33
NADPH
wild-type, pH 7.0
48
NADPH
mutant G179A, pH 7.0
50
NADPH
F251R mutant enzyme, pH 7.0, 25°C
50
NADPH
F251Y mutant enzyme, pH 7.0, 25°C
190
NADPH
-
mutant D239G, pH 7.0