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Information on EC 1.10.5.1 - ribosyldihydronicotinamide dehydrogenase (quinone) and Organism(s) Homo sapiens and UniProt Accession P16083
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1.10.5.1 ribosyldihydronicotinamide dehydrogenase (quinone)IUBMB Comments
A flavoprotein. Unlike EC 1.6.5.2, NAD(P)H dehydrogenase (quinone), this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17beta-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor . This enzyme can catalyse both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced .
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
quinone reductase 2, nrh:quinone oxidoreductase 2, quinone oxidoreductase 2, quinone reductase type 2, nrh:quinone oxidoreductase, dihydronicotinamide riboside:quinone oxidoreductase, dihydronicotinamide riboside:quinone reductase 2, dihydronicotinamide riboside:quinone oxidoreductase 2, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NQO2
-
-
NRH:quinone oxidoreductase 2
-
-
QR2
-
-
quinone reductase 2
-
-
SYSTEMATIC NAME
IUBMB Comments
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide:quinone oxidoreductase
A flavoprotein. Unlike EC 1.6.5.2, NAD(P)H dehydrogenase (quinone), this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17beta-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor [2]. This enzyme can catalyse both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced [3].
CAS REGISTRY NUMBER
COMMENTARY
667919-86-0
-
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-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone
1-(beta-D-ribofuranosyl)nicotinamide + a quinol
-
-
-
?
1-carbamoylmethyl-3-carbamoyl-1,4-dihydropyrimidine + menadione
1-carbamoylmethyl-3-carbamoylpyrimidine + menadiol
-
-
-
?
2,6-dichloroindophenol + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
2H-dibenzo[b,f]azepin-2-one + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
amodiaquine quinone imine + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
desethylamodiaquine quinone imine + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
diclofenac-1',4'-quinone imine + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
diclofenac-2,5-quinone imine + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
mefenamic acid-1',4'-quinone imine + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
mefenamic acid-2,5-quinone imine + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
N-acetyl-p-benzoquinone imine + dihydronicotinamide riboside
? + nicotinamide riboside
-
-
-
?
N-benzyldihydronicotinamide + 2,6-dichlorophenolindophenol
N-benzylnicotamide + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N-methyldihydronicotinamide + menadione
N-methylnicotinamide + menadiol
-
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone
1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone
-
-
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + co-enzyme Q
1-(beta-D-ribofuranosyl)nicotinamide + reduced co-enzyme Q
-
natural substrate nicotinamide riboside, NRH
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione
1-(beta-D-ribofuranosyl)nicotinamide + menadiol
1-benzyl-1,4-dihydronicotinamide + estradiol-3,4-quinone
1-benzyl-3-carbamoylpyridinium + estrone-3,4-quinone
-
-
-
-
r
17beta-17-hydroxyestr-1(10)-ene-3,4-dione + N-benzyldihydronicotinamide
17beta-estra-1(10),2,4-triene-3,4,17-triol + N-benzylnicotinamide
-
ping-pong mechanism, NQO2 is faster in reducing estrogen quinones than its homologue NQO1
-
-
?
5-(aziridin-1-yl)-2,4-dinitrobenzamide + menadiol
? + reduced menadiol
-
-
-
-
?
dihydronicotinamide riboside + 2,6-dichlorophenolindophenol
nicotinamide riboside + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
dihydronicotinamide riboside + 3-(4,5-dimethylthiazaol-2-yl)-2,5-diphenyltetrazolium
nicotinamide riboside + ?
-
-
-
-
?
dihydronicotinamide riboside + menadione/3-(4,5-dimethylthiazaol-2-yl)-2,5-diphenyltetrazolium
nicotinamide riboside + ?
-
-
-
-
?
estrone-3,4-quinone + N-benzyldihydronicotinamide
estrone-3,4-quinol + N-benzylnicotinamide
-
ping-pong mechanism, NQO2 is faster in reducing estrogen quinones than its homologue NQO1
-
-
?
N-benzyldihydronicotinamide + 2,6-dichlorophenolindophenol
N-benzylnicotinamide + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
N-benzyldihydronicotinamide + a quinone
N-benzylnicotinamide + a hydroquinone
-
synthetic substrate
-
-
?
N-benzyldihydronicotinamide + menadione
N-benzylnicotinamide + menadiol
-
-
-
-
?
N-benzyldihydronicotinamide + oxidized coenzyme Q0
N-benzylnicotinamide + reduced coenzyme Q20
-
-
-
-
?
N-benzyldihydronicotinamide + oxidized coenzyme Q1
N-benzylnicointamide + reduced coenzyme Q1
-
-
-
-
?
N-benzyldihydronicotinamide + oxidized coenzyme Q2
N-benzylnicotinamide + reduced coenzyme Q2
-
-
-
-
?
N-methyldihydronicotinamide + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
N-methylnicotinamide + ?
-
-
-
-
?
N-methyldihydronicotinamide + menadione
N-methylnicotinamide + menadiol
-
-
-
-
?
N-ribosylnicotinamide + menadiol
?
-
N-ribosylnicotinamide is a poor substrate
-
-
?
nicotinamide riboside + menadiol
dihydronicotinamide riboside + menadione
-
-
-
-
?
nicotinamide riboside + reduced 2,6-dichlorophenolindophenol
dihydronicotinamide riboside + 2,6-dichlorophenolindophenol
-
-
-
-
?
nicotinamide riboside + reduced coenzyme Q0
dihydronicotinamide riboside + coenzyme Q0
-
-
-
-
?
nicotinamide riboside + reduced coenzyme Q1
dihydronicotinamide riboside + coenzyme Q1
-
-
-
-
?
nicotinamide riboside + reduced coenzyme Q2
dihydronicotinamide riboside + coenzyme Q2
-
-
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione
1-(beta-D-ribofuranosyl)nicotinamide + menadiol
-
-
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione
1-(beta-D-ribofuranosyl)nicotinamide + menadiol
-
natural substrate nicotinamide riboside, NRH
-
-
?
additional information
?
-
high QR2 activity might make individuals more susceptible to Parkinsons disease. By inhibiting QR2, it seems that anti-malarial compounds such as quinacrine favour the red blood cell oxidative stress leading to the death of the parasite
-
-
?
additional information
?
-
knockdown K562 cells exhibit increased antioxidant and detoxification enzyme expression and reduced proliferation rates
-
-
?
additional information
?
-
enzyme cannot use NADH or NADPH as reducing agent
-
-
?
additional information
?
-
no substrate: 5-hydroxydiclofenac quinone imine
-
-
-
additional information
?
-
-
no substrate: 5-hydroxydiclofenac quinone imine
-
-
-
additional information
?
-
-
the expression of the NQO2 gene is induced in response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
-
-
?
additional information
?
-
-
no activity with one-electron acceptors such as potassium ferricyanide
-
-
?
additional information
?
-
-
the D allele in the promoter is associated with higher NQO2 activity and increases levels of ROS in the presence of dopamine, which would then increase susceptibility to Parkinson's disease
-
-
?
additional information
?
-
-
NQO2 catalyzes the reduction of electrophilic estrogen quinones and thereby may act as a detoxification enzyme
-
-
?
additional information
?
-
-
the enzyme does not accept conventional phosphorylated nicotinamides as hydride donors
-
-
?
additional information
?
-
-
NQO2 can function as a nitroreductase in activating the antitumor drug 5-aziridinyl-2,4-dinitrobenzamide
-
-
?
additional information
?
-
-
the enzyme catalyzes the reduction of quinones, such as menadione and co-enzyme Q
-
-
?
additional information
?
-
-
QR2 produces free radicals with pro-drug CB1954, i.e. 5-(aziridin-1-yl)-2,4-dinitrobenzamide. The anti-cancer pro-drug CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide) is transformed into a potent cytotoxic drug upon reduction of its 4-nitro group to a 4-hydroxylamine by quinone reductases or nitroreductase
-
-
?
additional information
?
-
-
quinone reductase 2 (QR2) is implicated in the reduction of quinone in the presence of natural derivatives of NADH such as N-ribosyldihydronicotinamide. QR2 does not recognize NADH or NADPH as co-substrates, unlike quinone reductase 1 (QR1)
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone
1-(beta-D-ribofuranosyl)nicotinamide + a quinol
-
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone
1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone
-
-
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + co-enzyme Q
1-(beta-D-ribofuranosyl)nicotinamide + reduced co-enzyme Q
-
natural substrate nicotinamide riboside, NRH
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione
1-(beta-D-ribofuranosyl)nicotinamide + menadiol
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione
1-(beta-D-ribofuranosyl)nicotinamide + menadiol
-
-
-
-
?
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione
1-(beta-D-ribofuranosyl)nicotinamide + menadiol
-
natural substrate nicotinamide riboside, NRH
-
-
?
additional information
?
-
high QR2 activity might make individuals more susceptible to Parkinsons disease. By inhibiting QR2, it seems that anti-malarial compounds such as quinacrine favour the red blood cell oxidative stress leading to the death of the parasite
-
-
?
additional information
?
-
knockdown K562 cells exhibit increased antioxidant and detoxification enzyme expression and reduced proliferation rates
-
-
?
additional information
?
-
-
the expression of the NQO2 gene is induced in response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
-
-
?
additional information
?
-
-
the D allele in the promoter is associated with higher NQO2 activity and increases levels of ROS in the presence of dopamine, which would then increase susceptibility to Parkinson's disease
-
-
?
additional information
?
-
-
NQO2 catalyzes the reduction of electrophilic estrogen quinones and thereby may act as a detoxification enzyme
-
-
?
additional information
?
-
-
NQO2 can function as a nitroreductase in activating the antitumor drug 5-aziridinyl-2,4-dinitrobenzamide
-
-
?
additional information
?
-
-
the enzyme catalyzes the reduction of quinones, such as menadione and co-enzyme Q
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
contains 1 FAD per monomer firmly bound to the enzyme through multiple interactions
FAD
-
mediates hydride transfer, very tightly bound to the enzyme. Activity of the purified enzyme is not further increased by added FAD
FAD
-
dstabilisation of the cofactor FAD by mutation N18E shows that 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine binding is closely linked to the conformational integrity of quinone oxidoreductase 2
FAD
-
flavoenzyme, binding structure, overview. 2 molecules per enzyme dimer, quantification, overview
additional information
enzyme cannot use NADH or NADPH as reducing agent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methoxy-6-((2-(6-methoxy-2-methylquinolin-4-yl)hydrazono)methyl)phenol
-
-
4-[(Z)-[(1H-imidazol-4-yl)methyl]diazenyl]-6-methoxy-2-methylquinoline
-
-
5-(2-(dimethylamino)ethylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
-
5-(2-(dimethylamino)ethylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one N-oxide
-
5-(2-(dimethylamino)ethylamino)-8-bromo-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
-
5-(2-(dimethylamino)ethylamino)-8-bromo-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one N-oxide
-
5-(2-(dimethylamino)ethylamino)-8-fluoro-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
-
5-(2-(dimethylamino)ethylamino)-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
-
5-(2-(dimethylamino)ethylamino)-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one N-oxide
-
5-(3-hydroxypropylamino)-8-bromo-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
-
5-(3-hydroxypropylamino)-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
-
8-bromo-5-[(3-methylbutyl)amino]-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
-
Chloroquine
binds preferentially to reduced NQO2, binding mode, closure of a flexible loop (Phe126-Leu136) over the active site, overview
imatinib
the structure of the imatinib-NQO2 complex demonstrates that imatinib inhibits NQO2 activity by competing with substrate for the active site
Melatonin
competitive inhibitor against N-methyldihydronicotinamide, uncompetitive against menadione. Melatonin and its analogues bind to and inhibit QR2 within the active site and not at an allosteric site
N,N'-[methylenedi(4,1-phenylene)]diacetamide
compound is inhibitory, and binding increases the thermal stability of NQO2
-
1,2-dimethoxy-4-{(1Z)-3,3,3-trifluoro-2-[3-(trifluoromethyl)phenyl]prop-1-en-1-yl}benzene
-
-
1,3-dimethoxy-5-[(1Z)-3,3,3-trifluoro-1-(4-methoxyphenyl)prop-1-en-2-yl]benzene
-
-
2-(2-methoxy-6H-pyrido[2',3':4,5]pyrrolo[2,1-a]isoindol-11-yl)ethylamine
-
IC50: 0.00087 mM
3-{[4-(dihydroxyamino)phenoxy]methyl}-5-methoxy-1,2-dimethyl-1H-indole-4,7-dione
-
-
5-[(4-aminobutyl)amino]-1,2-dimethyl-3-[(2,4,6-trifluorophenoxy)methyl]-1H-indole-4,7-dione
-
-
5-[(4-aminobutyl)amino]-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]-1H-indole-4,7-dione
-
-
5-[(8-aminooctyl)amino]-1,2-dimethyl-3-[(2,4,6-trifluorophenoxy)methyl]-1H-indole-4,7-dione
-
-
5-[butyl(methyl)amino]-1,2-dimethyl-3-[(2,4,6-trifluorophenoxy)methyl]-1H-indole-4,7-dione
-
-
5-[[4-(diethylamino)butyl]amino]-10-methoxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(diethylamino)butyl]amino]-7,10-dimethoxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(diethylamino)butyl]amino]-7-hydroxy-10-methoxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(diethylamino)butyl]amino]-7-hydroxy-8,9-dimethoxy-6H-imidazo[4,5,1-de]acridin-6-one
-
most potent inhibitor of NQO2
5-[[4-(diethylamino)butyl]amino]-8-hydroxy-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(diethylamino)butyl]amino]-8-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(diethylamino)butyl]amino]-8-methoxy-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(diethylamino)butyl]amino]-8-methoxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(diethylamino)butyl]amino]-9-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(dimethylamino)butyl]amino]-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(dimethylamino)butyl]amino]-8-hydroxy-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[4-(dimethylamino)butyl]amino]-8-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-[[6-(diethylamino)hexyl]amino]-8-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
-
-
5-{[2-(dimethylamino)ethyl]amino}-1,2-dimethyl-3-(phenoxymethyl)-1H-indole-4,7-dione
-
-
5-{[2-(dimethylamino)ethyl]amino}-1,2-dimethyl-3-[(2,4,6-trifluorophenoxy)methyl]-1H-indole-4,7-dione
-
-
5-{[2-(dimethylamino)ethyl]amino}-1-methyl-2-phenyl-3-[(2,4,6-trifluorophenoxy)methyl]-1H-indole-4,7-dione
-
-
5-{[2-(dimethylamino)ethyl]amino}-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]-1H-indole-4,7-dione
-
-
5-{[3-(dimethylamino)propyl]amino}-1,2-dimethyl-3-[(2,4,6-trifluorophenoxy)methyl]-1H-indole-4,7-dione
-
-
curcumol
-
curcumol directly targets NQO2 to cause reactive oxygen species generation, which triggers endoplasmic reticulum stress-C/EBP homologous protein death receptor signaling, sensitizing non-small cell lung cancer cells to tumor-necrosis-factor-related apoptosis-inducing ligand (TRAIl) induced apoptosis. Presence of curcumol increases thermal stability of NQO2. Residue Phe178 in NQO2 is a critical site for curcumol binding
-
ethyl 3-(2-((4-(N-(4-(tert-butoxycarbonylamino)butyl)-carbamimidoyl)phenylamino)methyl)-1-methyl-N-(pyridin-2-yl)-1H-benzo[d]imidazole-5-carboxamido)propanoate
-
-
ethyl N-[(2-{[(4-carbamimidoylphenyl)amino]methyl}-1H-benzimidazol-5-yl)carbonyl]-N-pyridin-2-yl-b-alaninate
-
-
methyl 2-((S)-1-cyclohexyl-2-((R)-2-(4-(4-(4-nitrophenylsulfonamido)butylcarbamoyl)benzylcarbamoyl)-azetidin-1-yl)-2-oxoethylamino)acetate
-
-
methyl N-{(1R)-1-cyclohexyl-2-oxo-2-[(2S)-2-{[4-({4-[(N-{17-oxo-21-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,8,12-trioxa-16-azahenicos-1-yl}-N2-{4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl}-L-alpha-asparaginyl)amino]butyl}carbamoyl)benzyl]carbamoyl}azetidin-1-yl]ethyl}glycinate
-
-
N-[2-(2-iodo-5-methoxy-1-methyl-4-nitroindol-3-yl)ethyl]acetamide
-
inhibits enzymatic mechanism of the enzyme through the MT3 binding site, IC50: 0.0003 mM
N-[2-(2-methoxy-6H-dipyrido[2,3-a:3,2-e]pyrrolizin-11-yl)ethyl]-2-furamide
-
IC50: 14 nM
N-[2-(2-methoxy-6H-pyrido[2',3':4,5]pyrrolo[2,1-a]isoindol-11-yl)ethyl]2-furamide
-
IC50: 0.0002 mM
N-[2-(8-methoxy-3,4-dihydro-2H-pyrido[2',3':4,5]pyrrolo[2,1-b][1,3]oxazin-10-yl)ethyl]-2-furamide
-
IC50: 0.005 mM
N-{(1R)-1-cyclohexyl-2-oxo-2-[(2S)-2-{[4-({4-[(N-{17-oxo-21-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,8,12-trioxa-16-azahenicos-1-yl}-N2-{4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl}-L-alpha-asparaginyl)amino]butyl}carbamoyl)benzyl]carbamoyl}azetidin-1-yl]ethyl}glycine
-
-
N-{[1-methyl-2-({[4-(N-{3-[(N-{17-oxo-21-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,8,12-trioxa-16-azahenicos-1-yl}-N2-{4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl}-L-alpha-asparaginyl)amino]propyl}carbamimidoyl)phenyl]amino}methyl)-1H-benzimidazol-5-yl]carbonyl}-N-pyridin-2-yl-beta-alanine
-
-
N1-[2-(2-methoxy-6H-pyrido[2',3':4,5]pyrrolo[2,1-a]isoindol-11-yl)ethyl]-acetamide
-
IC50: 0.0019 mM
N4-[2-(4-{4-[(4-methyl-3-{[4-(pyridin-3-yl)pyrimidin-2-yl]amino}phenyl)carbamoyl]benzyl}piperazin-1-yl)ethyl]-N1-{17-oxo-21-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,8,12-trioxa-16-azahenicos-1-yl}-N2-{4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl}-L-aspartamide
-
-
N4-[3-({N-[(2-{[(4-carbamimidoylphenyl)amino]methyl}-1-methyl-1H-benzimidazol-5-yl)carbonyl]-N-phenyl-b-alanyl}amino)propyl]-N1-{17-oxo-21-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,8,12-trioxa-16-azahenicos-1-yl}-N2-{4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl}-L-aspartamide
-
-
N4-[4-({N-[(1R)-2-{(2R)-2-[(4-carbamimidoylbenzyl)carbamoyl]cyclobutyl}-1-cyclohexylprop-2-en-1-yl]glycyl}amino)butyl]-N1-{17-oxo-21-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,8,12-trioxa-16-azahenicos-1-yl}-N2-{4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl}-L-aspartamide
-
-
NSC180969
-
i.e. 7,8-dimethoxy-4-(3,4,5-trimethoxyphenyl)-1,2-dihydro-3H-benzo[e]isoindol-3-one
NSC187208
-
i.e. N4-(7-chloro-4-quinolinyl)-N1,N1-diethyl-1,4-pentanediamine, chloroquine
NSC204996
-
i.e. 7,8-dimethoxy-4-(3,4,5-trimethoxyphenyl)-2,3-dihydro-1H-benzo[e]isoindole
NSC238146
-
i.e. N4-(6-((6-amino-2-methyl-4-quinolinyl)amino)hexyl)-2-methyl-4,6-quinolinediamine acetate
NSC300853
-
i.e. 3-amino-9-ethyl-2-((4-(hydroxy(oxido)amino)phenyl)diazenyl)-9H-carbazole
NSC306843
-
i.e. 1-methyl-4(1H)-quinolinone (1-methyl-4(1H)-quinolinylidene)hydrazone
NSC356819
-
i.e. 4-((2-hydroxy-5-(phenyldiazenyl)phenyl)diazenyl)benzenecarboximidamide
NSC356820
-
i.e. 4-((2-hydroxy-5-(2-phenylvinyl)phenyl)diazenyl)benzenecarboximidamide
NSC359466
-
i.e. 4-((4-(amino(imino)methyl)phenyl)diazenyl)-3-hydroxy-N-phenyl-2-naphthamide
NSC621351
-
i.e. 2-(2-fluorophenyl)-4-(2-naphthyl)-2,3-dihydro-1,5-benzothiazepine
NSC623234
-
i.e. 3-chloro-3-(3,4-dimethoxyphenyl)-2-(3,4,5-trimethoxyphenyl)acrylaldehyde
NSC640353
-
i.e. 1-(2-(3,5-diphenyl-1H-pyrazol-1-yl)-4-methyl-1,3-thiazol-5-yl)-4-methyl-5-phenyl-2,4-pentadien-1-one
NSC640556
-
i.e. 1-(2-(3,5-diphenyl-1H-pyrazol-1-yl)-4-methyl-1,3-thiazol-5-yl)-3-(4-(hydroxy(oxido)amino)phenyl)-2-propen-1-one
NSC640558
-
i.e 1-(2-(3,5-diphenyl-1H-pyrazol-1-yl)-4-methyl-1,3-thiazol-5-yl)-3-phenyl-2-propen-1-one
NSC640559
-
i.e. 1-(2-(3,5-diphenyl-1H-pyrazol-1-yl)-4-methyl-1,3-thiazol-5-yl)-3-(3-(hydroxy(oxido)amino)phenyl)-2-propen-1-one
NSC640566
-
i.e. 3-(4-chlorophenyl)-1-(2-(3,5-diphenyl-1H-pyrazol-1-yl)-4-methyl-1,3-thiazol-5-yl)-2-propen-1-one
NSC640583
-
i.e. 1-(2-(3,5-diphenyl-1H-pyrazol-1-yl)-4-methyl-1,3-thiazol-5-yl)-3-(4-methylphenyl)-2-propen-1-one
NSC640584
-
i.e. 3-(3,4-dichlorophenyl)-1-(2-(3,5-diphenyl-1H-pyrazol-1-yl)-4-methyl-1,3-thiazol-5-yl)-2-propen-1-one
NSC649091
-
i.e. 2-((diethylamino)methyl)-4-((10-methyl-10H-indolo[3,2-b]quinolin-11-yl)amino)phenol hydrochloride
NSC665126
-
i.e. 1-(2-(4-(hydroxy(oxido)amino)phenyl)vinyl)-3-phenylbenzo[f]quinoline
NSC669977
-
i.e. 6-imino-1-methyl-3-phenyl-2,6-dihydro-5(1H)-quinolinone hydrazone
NSC676468
-
i.e. N-(3-([1,10-biphenyl]-4-ylimino)-1-propenyl)[1,10-biphenyl]-4-amine
NSC693571
-
i.e. trifluoromethanesulfonic acid compound with N,N-dimethyl-4-((1-methyl-2-phenyl-4H-1lambda5-pyrazolo[1,5-a]indol-4-ylidene)methyl)aniline
NSC720622
-
i.e. trifluoromethanesulfonic acid compound with N,N-dimethyl-4-((1-methyl-6-nitro-2-phenylpyrazolo[1,5-a]indol-1-ium-4-ylidene)methyl)aniline
NSC97374
-
i.e. 1-ethyl-2-((1-ethyl-2(1H)-quinolinylidene)methyl)-1lambda5-quinoline
tert-butyl (S)-1-cyclohexyl-2-((R)-2-(4-(4-(4-nitrophenylsulfonamido)butylcarbamoyl)benzylcarbamoyl)-azetidin-1-yl)-2-oxoethylcarbamate
-
-
resveratrol
the chemopreventive and cardioprotective properties of resveratrol are possibly the results of QR2 activity inhibition, which in turn, up-regulates the expression of cellular antioxidant enzymes and cellular resistance to oxidative stress. All three resveratrol hydroxyl groups form hydrogen bonds with amino acids from QR2, anchoring a flat resveratrol molecule in parallel with the isoalloxazine ring of FAD
dabigatran
-
specific binding to the enzyme, protein interaction analysis, overview
Melatonin
-
QR2 is inhibited in the micromolar range by melatonin, but not when using N-benzyl dihydronicotinamide and coenzyme Q2 are used as substrates
resveratrol
-
i.e. 3,5,4'-trihydroxylstilbene, resveratrol binds tightly to the oxidized, FAD-form of the enzyme, and it acts as a competitive inhibitor against N-methyldihydronicotinamide. The amount of resveratrol consumed from dietary sources may be sufficient for effective inhibition of QR2
S29434
-
i.e. N-[2-(2-methoxy-6H-dipyrido[2,3-a:3,2-e]pyrrolizin-11-yl)ethyl]-2-furamide, inhibits QR2 activity with an IC50 in the low nanomolar range from 0.7 to 80 nM, depending on the substrates and co-substrates used
additional information
study on 4-aminoquinoline hydrazone inhibitors. A small substituent at the 2-position of the 4-aminoquinoline ring is important to reduce steric hindrance and improve engagement of the scaffold within the NQO2 active site. Both the hydrazone and hydrazide derivatives are functionally active as inhibitors of NQO2 in the cells
-
additional information
-
no inhibition by 4-methylquinolin-2(1H)-one. 6-Methoxy-9-methyl-[1,3]dioxolo[4,5-h]quinolin-8(9H)-one and its analogues merit further investigation as potential chemopreventive or chemotherapeutic agents
-
additional information
-
development of potent and selective mechanism-based inhibitors centered on the indolequinone pharmacophore. The compounds show remarkable selectivity for NQO2 over the closely related flavoprotein NQO1, with small structural changes defining selectivity, detailed overview. The inhibitor's mode of action involving alkylation of the flavin cofactor, provides significant advantages over existing competitive inhibitors in terms of potency and irreversibility
-
additional information
-
enzyme inhibitor design, synthesiis, and evaluation, inhibitory potencies of resveratrol analogues, overview. Inhibitor binding structure, modelling, overview
-
additional information
-
molecular dockings predicts and biological experiments confirm that dabigatran ethyl ester inhibits NQO2 even more effectively than the parent compound itself, usage of capture compounds, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.061
5-(aziridin-1-yl)-2,4-dinitrobenzamide
-
at 25°C in pH 8.5 buffer (50 mM Tris, 140 mM NaCl, and 0.1% Tween 20) with 0.1 mM menadione as co-substrate
0.0137
coenzyme Q0
-
using N-benzyl dihydronicotinamide as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0517
coenzyme Q1
-
using N-benzyl dihydronicotinamide as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0387
coenzyme Q2
-
using N-benzyl dihydronicotinamide as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
additional information
additional information
-
steady-state kinetic, overview
-
0.0102
2,6-dichlorophenolindophenol
-
using N-benzyl dihydronicotinamide as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.019
2,6-dichlorophenolindophenol
-
chimeric enzyme of the human NQO2 with 43 amino acids from the carboxyl terminus of human DT-diaphorase
0.0111
menadione
-
using N-benzyl dihydronicotinamide as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0113
N-benzyl dihydronicotinamide
-
using menadione as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0361
N-benzyl dihydronicotinamide
-
using coenzyme Q0 as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0404
N-benzyl dihydronicotinamide
-
using 2,6-dichlorophenolindophenol as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0451
N-benzyl dihydronicotinamide
-
using coenzyme Q1 as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0602
N-benzyl dihydronicotinamide
-
using coenzyme Q2 as cosubstrate, at 25°C, in 50 mM Tris-HCl, pH 8.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6
5-(aziridin-1-yl)-2,4-dinitrobenzamide
-
at 25°C in pH 8.5 buffer (50 mM Tris, 140 mM NaCl, and 0.1% Tween 20) with 0.1 mM menadione as co-substrate
91.8
2,6-dichlorophenolindophenol
-
chimeric enzyme of the human NQO2 with 43 amino acids from the carboxyl terminus of human DT-diaphorase
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0009
dabigatran ethyl ester
-
pH and temperature not specified in the publication
0.00003 - 0.00004
N-[2-(2-methoxy-6H-dipyrido[2,3-a:3,2-e]pyrrolizin-11-yl)ethyl]-2-furamide
0.000088
resveratrol
-
versus N-methyldihydronicotinamide, pH and temperature not specified in the publication
additional information
additional information
-
Michaelis-Menten inhibition kinetics
-
0.0072
Melatonin
pH 8, 25°C, competitive inhibitor against N-methyldihydronicotinamide
0.033
2-iodo-5-methoxycarbonylamino-N-acetyltryptamine
-
reduced form hQR2-FADH2
0.00008
N-[2-(2-iodo-5-methoxy-1-methyl-4-nitroindol-3-yl)ethyl]acetamide
-
oxidized form hQR2-FAD
0.00031
N-[2-(2-iodo-5-methoxy-1-methyl-4-nitroindol-3-yl)ethyl]acetamide
-
reduced form hQR2-FADH2
0.00003
N-[2-(2-methoxy-6H-dipyrido[2,3-a:3,2-e]pyrrolizin-11-yl)ethyl]-2-furamide
-
reduced form hQR2-FADH2
0.00004
N-[2-(2-methoxy-6H-dipyrido[2,3-a:3,2-e]pyrrolizin-11-yl)ethyl]-2-furamide
-
oxidized form hQR2-FAD
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
2-methoxy-6-((2-(6-methoxy-2-methylquinolin-4-yl)hydrazono)methyl)phenol
Homo sapiens
pH 7.4, 37°C
-
0.000068
4-(5-phenylfuran-2-yl)benzene-1-carboximidamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.00077
4-(5-phenylthiophen-2-yl)benzene-1-carboximidamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.071
4-[(Z)-(1H-imidazol-4-yl)diazenyl]-6-methoxy-2-methylquinoline
Homo sapiens
pH 7.4, 37°C
-
0.103
4-[(Z)-(4-fluorophenyl)diazenyl]-6-methoxy-2-methylquinoline
Homo sapiens
pH 7.4, 37°C
-
0.064
4-[(Z)-(6-methoxy-2-methylquinolin-4-yl)diazenyl]benzoic acid
Homo sapiens
pH 7.4, 37°C
-
0.055
4-[(Z)-(6-methoxy-2-methylquinolin-4-yl)diazenyl]phenol
Homo sapiens
pH 7.4, 37°C
-
0.09
4-[(Z)-[(1H-imidazol-4-yl)methyl]diazenyl]-6-methoxy-2-methylquinoline
Homo sapiens
pH 7.4, 37°C
-
0.001833
5-(2-(dimethylamino)ethylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000167
5-(2-(dimethylamino)ethylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one N-oxide
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.001483
5-(2-(dimethylamino)ethylamino)-8-bromo-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000117
5-(2-(dimethylamino)ethylamino)-8-bromo-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one N-oxide
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000783
5-(2-(dimethylamino)ethylamino)-8-fluoro-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.001333
5-(2-(dimethylamino)ethylamino)-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000098
5-(2-(dimethylamino)ethylamino)-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one N-oxide
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000483
5-(3-hydroxypropylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000987
5-(3-hydroxypropylamino)-8-bromo-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000517
5-(3-hydroxypropylamino)-8-methoxy-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000098
5-(4-methoxyphenylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000427
5-(isopentylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.000567
5-(phenethylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.046
5-[(Z)-(6-methoxy-2-methylquinolin-4-yl)diazenyl]benzene-1,3-diol
Homo sapiens
pH 7.4, 37°C
-
0.083
6-methoxy-2-methyl-4-[(Z)-(4-nitrophenyl)diazenyl]quinoline
Homo sapiens
pH 7.4, 37°C
-
0.018
6-methoxy-2-methyl-4-[(Z)-(5-nitrofuran-2-yl)diazenyl]quinoline
Homo sapiens
pH 7.4, 37°C
-
0.01
6-methoxy-2-methyl-4-[(Z)-(pyridin-3-yl)diazenyl]quinoline
Homo sapiens
pH 7.4, 37°C
-
0.000767
8-bromo-5-[(3-methylbutyl)amino]-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.00035
8-methoxy-5-(phenethylamino)-6H-[1,2,3]triazolo[4,5,1-de]acridin-6-one
Homo sapiens
in 50 mM phosphate buffer at pH 7.4, at 37°C
0.00087
2-(2-methoxy-6H-pyrido[2',3':4,5]pyrrolo[2,1-a]isoindol-11-yl)ethylamine
Homo sapiens
-
IC50: 0.00087 mM
0.000099
5-[[4-(diethylamino)butyl]amino]-10-methoxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000427
5-[[4-(diethylamino)butyl]amino]-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000017
5-[[4-(diethylamino)butyl]amino]-7,10-dimethoxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000031
5-[[4-(diethylamino)butyl]amino]-7-hydroxy-10-methoxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000006
5-[[4-(diethylamino)butyl]amino]-7-hydroxy-8,9-dimethoxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000016
5-[[4-(diethylamino)butyl]amino]-8-hydroxy-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000148
5-[[4-(diethylamino)butyl]amino]-8-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000009
5-[[4-(diethylamino)butyl]amino]-8-methoxy-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.001
5-[[4-(diethylamino)butyl]amino]-8-methoxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000953
5-[[4-(diethylamino)butyl]amino]-9-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000693
5-[[4-(dimethylamino)butyl]amino]-1-ethyl-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000323
5-[[4-(dimethylamino)butyl]amino]-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00083
5-[[4-(dimethylamino)butyl]amino]-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
5-[[4-(dimethylamino)butyl]amino]-8-hydroxy-1-methyl-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000296
5-[[4-(dimethylamino)butyl]amino]-8-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000597
5-[[6-(diethylamino)hexyl]amino]-8-hydroxy-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000172
5-[[6-(dimethylamino)hexyl]amino]-6H-imidazo[4,5,1-de]acridin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
dabigatran ethyl ester
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
N-[2-(2-iodo-5-methoxy-1-methyl-4-nitroindol-3-yl)ethyl]acetamide
Homo sapiens
-
inhibits enzymatic mechanism of the enzyme through the MT3 binding site, IC50: 0.0003 mM
0.000014
N-[2-(2-methoxy-6H-dipyrido[2,3-a:3,2-e]pyrrolizin-11-yl)ethyl]-2-furamide
Homo sapiens
-
IC50: 14 nM
0.0002
N-[2-(2-methoxy-6H-pyrido[2',3':4,5]pyrrolo[2,1-a]isoindol-11-yl)ethyl]2-furamide
Homo sapiens
-
IC50: 0.0002 mM
0.005
N-[2-(8-methoxy-3,4-dihydro-2H-pyrido[2',3':4,5]pyrrolo[2,1-b][1,3]oxazin-10-yl)ethyl]-2-furamide
Homo sapiens
-
IC50: 0.005 mM
0.0019
N1-[2-(2-methoxy-6H-pyrido[2',3':4,5]pyrrolo[2,1-a]isoindol-11-yl)ethyl]-acetamide
Homo sapiens
-
IC50: 0.0019 mM
0.125
3-[(Z)-(6-methoxy-2-methylquinolin-4-yl)diazenyl]phenol
Homo sapiens
pH 7.4, 37°C
-
0.137
3-[(Z)-(6-methoxy-2-methylquinolin-4-yl)diazenyl]phenol
Homo sapiens
pH 7.4, 37°C
-
0.000016
chrysoeriol
Homo sapiens
-
using nicotinamide riboside and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.000076
chrysoeriol
Homo sapiens
-
using nicotinamide riboside and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.00016
chrysoeriol
Homo sapiens
-
using N-benzyl dihydronicotinamide and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.00082
chrysoeriol
Homo sapiens
-
using N-benzyl dihydronicotinamide and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0028
Melatonin
Homo sapiens
-
using nicotinamide riboside and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0397
Melatonin
Homo sapiens
-
using nicotinamide riboside and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0415
Melatonin
Homo sapiens
-
using N-benzyl dihydronicotinamide and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.000129
resveratrol
Homo sapiens
-
using nicotinamide riboside and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.000143
resveratrol
Homo sapiens
-
using N-benzyl dihydronicotinamide and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0029
resveratrol
Homo sapiens
-
using nicotinamide riboside and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.07
resveratrol
Homo sapiens
-
using N-benzyl dihydronicotinamide and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0012
S26695
Homo sapiens
-
using nicotinamide riboside and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0025
S26695
Homo sapiens
-
using N-benzyl dihydronicotinamide and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0126
S26695
Homo sapiens
-
using nicotinamide riboside and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0151
S26695
Homo sapiens
-
using N-benzyl dihydronicotinamide and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0000007
S29434
Homo sapiens
-
using nicotinamide riboside and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.000005
S29434
Homo sapiens
-
using nicotinamide riboside and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.0000067
S29434
Homo sapiens
-
using N-benzyl dihydronicotinamide and menadione as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
0.000079
S29434
Homo sapiens
-
using N-benzyl dihydronicotinamide and coenzyme Q2 as substrates, at 25°C, in 50 mM Tris-HCl, pH 8.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
no significant difference in expression in normal and malignant biliary tissue. Activity of NQO2 is significatly lower than in hepatocellular tissue
-
the high NQO2 activity of intraperitoneal ovarian metastases relative to other tissues indicates a potential for tretazicar therapy in the treatment of this disease
additional information
in normal hepatocellular tissue, the two NQO isoforms are differentially regulated with a higher expression of NQO2 than NQO1. In malignant hepatocellular tissue NQO1 is up-regulated and NQO2 is down-regulated
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
-
specific inhibitors of QR2, tested in vivo, show outstanding properties impairing memory loss
physiological function
additional information
physiological function
quinone reductase 2 is an FAD-linked enzyme and the only known human target of two antimalarial drugs, primaquine and chloroquine, a functional role for NQO2 as a flavin redox switch
physiological function
cells overexpressing NQO2 show a significant increase in the ROS production due to the fast reduction of quinone into quinol that can re-oxidize to form superoxide radicals. NQO2 inhibition decreases the amount of superoxide cells overexpressing NQ2 by decreasing the amount of quinol formed, and it increases the toxicity of menadione in the cells co-expressing NQO2 with the conjugation enzyme UDPglucuronosyltransferase (UGT1A6, E.C. 2.4.1.17). For the cells coexpressing NQO2 and UGT1A6, the homeostasis dysregulation is lower in presence of menadione than for its counterpart expressing only NQO2
physiological function
knockdown of NQO2 enhances the albumin secretion of primary hepatocytes
physiological function
NQO2 catalyzes the reduction of quinone-like metabolites derived from acetaminophen, clozapine, 4'-hydroxydiclofenac, mefenamic acid, amodiaquine, and carbamazepine. NQO2 may be a genetic risk factor for clozapine-induced agranulocytosis
physiological function
silencing of NQO2 strongly reduces flavone-induced autophagic flux, although it increases basal LC3-II levels in HepG2 cells. Flavones apigenin and luteolin induce AMP kinase (AMPK) activation, while its reduction by AMPK beta (PRKAB1) silencing inhibits flavone-induced autophagy. The depletion of NQO2 levels by siRNA increases the basal AMPK phosphorylation but abrogates its further increase by apigenin
physiological function
-
ribosyldihydronicotinamide dehydrogenase is a detoxification oxidoreductase, it is a flavoprotein that catalyzes the 2-electron reduction of various quinones, redox dyes, and the vitamin K menadione. NQO2 predominantly uses dihydronicotinamide riboside as the electron donor
physiological function
-
the enzyme functions in metabolic reduction and detoxification processes. Evidence exists linking QR2 to the metabolic activation of quinones, which can lead to cell toxicity. Inhibition of the enzymme by resveratrol may protect cells against reactive intermediates and eventually cancer
physiological function
-
in NQ2 knockout cells, cell growth is slower. In a mouse model with xenografts formed by NQO2 knockout cells, the NQO2 knockout group exhibited significant smaller tumor volume and tumor weight than the control. Deletion of NQO2 suppresses cancer proliferation in vivo
additional information
-
QR2 does not share many features with QR1. Particularly, it does not seem to have a similar detoxifying function in cells. QR2 is overexpressed in neurodegenerative diseases
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NQO2_HUMAN
231
0
25919
Swiss-Prot
other Location (Reliability: 3), other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
the enzyme forms homodimers with two independent and equivalent active sites each containing a FAD cofactor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme in complex with resveratrol. Crystals of the native QR2 and QR2-resveratrol complex all belong to the P2(1)2(1)2(1) space group
purified NQO2 in complex with primaquine and chloroquine, hanging drop vapor diffusion method, against reservoirs containing 0.1 M HEPES, pH 7.5, and 1.3-2.0 M (NH4)2SO4, crystals of NQO2-CQ are soaked in 0.001 ml of reducing-soak solution consisting of 0.1 M HEPES, pH 7.5, 2.0 M (NH4)2SO4, 10 mM 1-(3-sulfonatopropyl)-3-carbamoyl-1,4-dihydropyrimidine and 1 mM chloroquine, X-ray diffraction structure determination and analysis at 1.2-1.4 A resolution
the crystal structure of melatonin and 2-iodomelatonin in complex with quinone reductase 2 provide a detailed description of the enzyme active site that can now be utilized in the design of new and potent inhibitors of the enzyme, hanging-drop vapour-diffusion method
X-ray crystal structure of NQO2 bound to imatinib to 1.75 A resolution. The X-ray structure provides an explanation for the binding specificity of NQO2 for imatinib and nilotinib, as well as for the effects of mutation of the reported phosphorylation sites on NQO2
purified recombinant enzyme, hanging-drop, vapor-diffusion method, mixing of 0.001 ml of 4 mg/ml protein solution with 0.001 ml of reservoir solution containing 1.3-1.7 M ammonium sulfate, 0.1 M Bis-Tris buffer, pH 6.0-7.0, 0.1 M NaCl, 5 mM DTT, 0.012 mM FAD, and resveratrol, complexed with different inhibitors, X-ray diffraction structure determination and analysis at resolutions of 1.40-1.63 A
-
X-ray crystallography studies of QR2 in complex with 6-methoxy-9-methyl-[1,3]dioxolo[4,5-h]quinolin-8(9H)-one
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C222F
-
mutation, which is distant from the determined binding site of the ligand, increases the affinity of [125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine for the enzyme
F126Y
-
substitution of the hydrophobic residue by tyrosines at the active site significantly increases enzymatic activity and decreases the affinity of a structural analog of melatonin, 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine
F178Y
-
substitution of the hydrophobic residue by tyrosines at the active site significantly increases enzymatic activity and decreases the affinity of a structural analog of melatonin, 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine
H11F
-
mutation of residue in FAD binding site, the enzymatic activity is unchanged
H173Y
-
mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding
H177R
-
mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding
I128Y
-
substitution of the hydrophobic residue by tyrosines at the active site significantly increases enzymatic activity and decreases the affinity of a structural analog of melatonin, 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine
N161A
-
mutation, which is distant from the determined binding site of the ligand, increases the affinity of [125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine for the enzyme
N161H
-
results in the total loss of the enzymatic activity towards activation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide, whereas the rates of reduction towards menadione are not altered
N18Q
-
mutation of residue in FAD binding site, the enzymatic activity is diminished
additional information
additional information
-
construction of a chimeric enzyme of the human NQO2 with 43 amino acids from the carboxyl terminus of human DT-diaphorase. HNQO2-hDT43 still uses dihydronicotinamide riboside as an electron donor. The chimeric enzyme is inhibited by quercetin but not dicoumarol
additional information
-
mutation of residue Phe178 completely abolishes the function of NQO2 and augments the TRAIL sensitization
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose, Superdex 75 column chromatography and Mono-Q column chromatography
-
recombinant His-tagged OR2 from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of recombinant QR2 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method
-
the His-tagged enzyme is expressed in the Sf9 Spodoptera frugiperda ovarian cell line ATCC CRL-1711
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
an increased risk of breast cancer is associated with the NQ2 I-29 allele. The I-29-containing genotype is significantly correlated with breast cancer under a dominant model. There is a significant association of the I-29/D polymorphism with luminal-like breast cancer but not with HER2-enriched or triple-negative subtypes
medicine
medicine
-
the high NQO2 activity of intraperitoneal ovarian metastases relative to other tissues indicates a potential for tretazicar therapy in the treatment of this disease
medicine
-
estrogen quinones, including estradiol estradiol-3,4-quinone, generated by estrogen metabolism, are thought to be responsible for estrogen-initiated carcinogenesis. NQO2 could be a novel target for prevention of breast cancer initiation
medicine
-
NQO2 protein level is significantly higher in non-small cell lung cancer tissues as compared with their normal tissues. NQO2 score at clinical stages III and IV is higher than stage I, and there exists a significant correlation between tumor NQO2 expression level and the pathologic T stage
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, K.; Knox, R.; Sun, X.Z.; Joseph, P.; Jaiswal, A.K.; Zhang, D.; Deng, P.S.K.; Chen, S.
Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase
Arch. Biochem. Biophys.
347
221-228
1997
Homo sapiens
Vella, F.; Ferry, G.; Delagrange, P.; Boutin, J.A.
NRH:quinone reductase 2: an enzyme of surprises and mysteries
Biochem. Pharmacol.
71
1-12
2005
Mus musculus, Homo sapiens (P16083)
Mailliet, F.; Ferry, G.; Vella, F.; Berger, S.; Coge, F.; et.al.
Characterization of the melatoninergic MT3 binding site on the NRH:quinone oxidoreductase 2 enzyme
Biochem. Pharmacol.
71
74-88
2005
Homo sapiens
Buryanovskyy, L.; Fu, Y.; Boyd, M.; Ma, Y.; Hsieh, T.; Wu, J.M.; Zhang, Z.
Crystal structure of quinone reductase 2 in complex with resveratrol
Biochemistry
43
11417-11426
2004
Homo sapiens (P16083)
Long, D.J.2nd.; Jaiswal, A.K.
NRH:quinone oxidoreductase2 (NQO2)
Chem. Biol. Interact.
129
99-112
2000
Homo sapiens
Boutin, J.A.; Chatelein-Egger, F.; Vella, F.; Delagrange, P.; Ferry, G.
Quinone reductase 2 substrate specificity and inhibitgion pharmacology
Chem. Biol. Interact.
151
213-228
2005
Homo sapiens
Nosjean, O.; Ferro, M.; Coge, F.; Beauverger, P.; et al.
Identification of the melatonin-binding site MT3 as the quinone reductase 2
J. Biol. Chem.
275
31311-31317
2000
Homo sapiens, Mesocricetus auratus
Strassburg, A.; Strassburg, C.P.; Manns, M.P.; Tukey, R.H.
Differential gene expression of NAD(P)H:quinone oxidoreductase and NRH:quinone oxidoreductase in human hepatocellular and biliary tissue
Mol. Pharmacol.
61
320-325
2002
Homo sapiens (P16083), Homo sapiens
Graves, P.R.; Kwiek, J.J.; Fadden, P.; et al.
Discovery of novel targets of quinoline drugs in the human purine binding proteome
Mol. Pharmacol.
62
1364-1372
2002
Homo sapiens
Zhao, Q.; Yang, X.L.; Holtzclaw, W.D.; Talalay, P.
Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)
Proc. Natl. Acad. Sci. USA
94
1669-1674
1997
Bos taurus, Homo sapiens
Fu, Y.; Buryanovskyy, L.; Zhang, Z.
Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954
Biochem. Biophys. Res. Commun.
336
332-338
2005
Homo sapiens
Wang, W.; Jaiswal, A.K.
Nulear factor Nrf2 and antioxidant response element regulate NRH:quinone oxidoreductase 2 (NQO2) gene expression and antioxidant induction
Free Radic. Biol. Med.
40
1119-1130
2006
Homo sapiens
Okada, S.; Farin, F.M.; Stapleton, P.; Viernes, H.; Quigley, S.D.; Powers, K.M.; Smith-Weller, T.; Franklin, G.M.; Longstreth, W.T.; Swanson, P.D.; Checkoway, H.
No associations between Parkinsons disease and polymorphisms of the quinone oxidoreductase (NQO1, NQO2) genes
Neurosci. Lett.
375
178-180
2005
Homo sapiens
Jamieson, D.; Wilson, K.; Pridgeon, S.; Margetts, J.P.; Edmondson, R.J.; Leung, H.Y.; Knox, R.; Boddy, A.V.
NAD(P)H:quinone oxidoreductase 1 and NRH:quinone oxidoreductase 2 activity and expression in bladder and ovarian cancer and lower NRH:quinone oxidoreductase 2 activity associated with an NQO2 exon 3 single-nucleotide polymorphism
Clin. Cancer Res.
13
1584-1590
2007
Homo sapiens
Wang, W.; Le, W.; Pan, T.; Stringer, J.L.; Jaiswal, A.K.
Association of NRH:quinone oxidoreductase 2 gene promoter polymorphism with higher gene expression and increased susceptibility to Parkinsons disease
J. Gerontol. A Biol. Sci. Med. Sci.
63
127-134
2008
Homo sapiens
Boutin, J.A.; Saunier, C.; Guenin, S.P.; Berger, S.; Moulharat, N.; Gohier, A.; Delagrange, P.; Coge, F.; Ferry, G.
Studies of the melatonin binding site location onto quinone reductase 2 by directed mutagenesis
Arch. Biochem. Biophys.
477
12-19
2008
Homo sapiens
Calamini, B.; Santarsiero, B.D.; Boutin, J.A.; Mesecar, A.D.
Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2
Biochem. J.
413
81-91
2008
Homo sapiens (P16083)
Winger, J.A.; Hantschel, O.; Superti-Furga, G.; Kuriyan, J.
The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2)
BMC Struct. Biol.
9
7
2009
Homo sapiens (P16083), Homo sapiens
Gaikwad, N.W.; Yang, L.; Rogan, E.G.; Cavalieri, E.L.
Evidence for NQO2-mediated reduction of the carcinogenic estrogen ortho-quinones
Free Radic. Biol. Med.
46
253-262
2009
Homo sapiens
Maiti, A.; Reddy, P.V.; Sturdy, M.; Marler, L.; Pegan, S.D.; Mesecar, A.D.; Pezzuto, J.M.; Cushman, M.
Synthesis of casimiroin and optimization of its quinone reductase 2 and aromatase inhibitory activities
J. Med. Chem.
52
1873-1884
2009
Homo sapiens
Nolan, K.A.; Humphries, M.P.; Bryce, R.A.; Stratford, I.J.
Imidazoacridin-6-ones as novel inhibitors of the quinone oxidoreductase NQO2
Bioorg. Med. Chem. Lett.
20
2832-2836
2010
Homo sapiens
Nolan, K.A.; Caraher, M.C.; Humphries, M.P.; Bettley, H.A.; Bryce, R.A.; Stratford, I.J.
In silico identification and biochemical evaluation of novel inhibitors of NRH:quinone oxidoreductase 2 (NQO2)
Bioorg. Med. Chem. Lett.
20
7331-7336
2010
Homo sapiens
Nolan, K.A.; Humphries, M.P.; Barnes, J.; Doncaster, J.R.; Caraher, M.C.; Tirelli, N.; Bryce, R.A.; Whitehead, R.C.; Stratford, I.J.
Triazoloacridin-6-ones as novel inhibitors of the quinone oxidoreductases NQO1 and NQO2
Bioorg. Med. Chem.
18
696-706
2010
Homo sapiens (P16083)
Ferry, G.; Hecht, S.; Berger, S.; Moulharat, N.; Coge, F.; Guillaumet, G.; Leclerc, V.; Yous, S.; Delagrange, P.; Boutin, J.A.
Old and new inhibitors of quinone reductase 2
Chem. Biol. Interact.
186
103-109
2010
Homo sapiens
John, S.E.St.; Jensen, K.C.; Kang, S.; Chen, Y.; Calamini, B.; Mesecar, A.D.; Lipton, M.A.
Design, synthesis, biological and structural evaluation of functionalized resveratrol analogues as inhibitors of quinone reductase 2
Bioorg. Med. Chem.
21
6022-6037
2013
Homo sapiens
Dufour, M.; Yan, C.; Siegel, D.; Colucci, M.A.; Jenner, M.; Oldham, N.J.; Gomez, J.; Reigan, P.; Li, Y.; De Matteis, C.I.; Ross, D.; Moody, C.J.
Mechanism-based inhibition of quinone reductase 2 (NQO2): selectivity for NQO2 over NQO1 and structural basis for flavoprotein inhibition
ChemBioChem
12
1203-1208
2011
Homo sapiens
Reybier, K.; Perio, P.; Ferry, G.; Bouajila, J.; Delagrange, P.; Boutin, J.A.; Nepveu, F.
Insights into the redox cycle of human quinone reductase 2
Free Radic. Res.
45
1184-1195
2011
Homo sapiens
Antoine, M.; Marcheteau, E.; Delagrange, P.; Ferry, G.; Boutin, J.
Characterization of cofactors, substrates and inhibitor binding to flavoenzyme quinone reductase 2 by automated supramolecular nano-electrospray ionization mass spectrometry
Int. J. Mass Spectrom.
312
87-96
2012
Homo sapiens
-
Leung, K.K.; Shilton, B.H.
Chloroquine binding reveals flavin redox switch function of quinone reductase 2
J. Biol. Chem.
288
11242-11251
2013
Homo sapiens (P16083), Homo sapiens
Michaelis, S.; Marais, A.; Schrey, A.K.; Graebner, O.Y.; Schaudt, C.; Sefkow, M.; Kroll, F.; Dreger, M.; Glinski, M.; Koester, H.; Metternich, R.; Fischer, J.J.
Dabigatran and dabigatran ethyl ester: potent inhibitors of ribosyldihydronicotinamide dehydrogenase (NQO2)
J. Med. Chem.
55
3934-3944
2012
Homo sapiens
Riches, Z.; Liu, Y.; Berman, J.M.; Walia, G.; Collier, A.C.
The ontogeny and population variability of human hepatic dihydronicotinamide riboside: quinone oxidoreductase (NQO2)
J. Biochem. Mol. Toxicol.
31
e21921
2017
Homo sapiens (P16083), Homo sapiens
Schepers, A.; Shan, J.; Cox, A.; Huang, A.; Evans, H.; Walesky, C.; Fleming, H.; Goessling, W.; Bhatia, S.
Identification of NQO2 As a protein target in small molecule modulation of hepatocellular function
ACS Chem. Biol.
16
1770-1778
2021
Homo sapiens (P16083)
Zhang, J.; Zhou, Y.; Li, N.; Liu, W.; Liang, J.; Sun, Y.; Zhang, W.; Fang, R.; Huang, S.; Sun, Z.; Wang, Y.; He, Q.
Curcumol overcomes TRAIL resistance of non-small cell lung cancer by targeting NRH quinone oxidoreductase 2 (NQO2)
Adv. Sci. (Weinh.)
7
2002306
2020
Homo sapiens
Janda, E.; Martino, C.; Riillo, C.; Parafati, M.; Lascala, A.; Mollace, V.; Boutin, J.A.
Apigenin and luteolin regulate autophagy by targeting NRH-quinone oxidoreductase 2 in liver cells
Antioxidants (Basel)
10
776
2021
Homo sapiens (P16083)
Alnabulsi, S.; Hussein, B.; Santina, E.; Alsalahat, I.; Kadirvel, M.; Magwaza, R.N.; Bryce, R.A.; Schwalbe, C.H.; Baldwin, A.G.; Russo, I.; Stratford, I.J.; Freeman, S.
Evaluation of analogues of furan-amidines as inhibitors of NQO2
Bioorg. Med. Chem. Lett.
28
1292-1297
2018
Plasmodium falciparum, Homo sapiens (P16083)
Den Braver-Sewradj, S.; Den Braver, M.; Toorneman, R.; Van Leeuwen, S.; Zhang, Y.; Dekker, S.; Vermeulen, N.; Commandeur, J.; Vos, J.
Reduction and scavenging of chemically reactive drug metabolites by NAD(P)H quinone oxidoreductase 1 and NRH quinone oxidoreductase 2 and variability in hepatic concentrations
Chem. Res. Toxicol.
31
116-126
2018
Homo sapiens (P16083), Homo sapiens
Hussein, B.; Ikhmais, B.; Kadirvel, M.; Magwaza, R.N.; Halbert, G.; Bryce, R.A.; Stratford, I.J.; Freeman, S.
Discovery of potent 4-aminoquinoline hydrazone inhibitors of NRH quinoneoxidoreductase-2 (NQO2)
Eur. J. Med. Chem.
182
111649
2019
Homo sapiens (P16083)
Zhou, J.Q.; Zhu, S.Y.; He, Y.; Yu, K.D.
Association between a tri-allelic polymorphism in the estrogen metabolism oxidoreductase NRH quinone oxidoreductase 2 gene and risk of breast cancer by molecular subtype
Front. Genet.
12
658285
2021
Homo sapiens (P16083), Homo sapiens
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