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Information on EC 1.6.3.1 - NAD(P)H oxidase (H2O2-forming)
for references in articles please use BRENDA:EC1.6.3.1
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EC Tree 1 Oxidoreductases
1.6 Acting on NADH or NADPH
1.6.3 With oxygen as acceptor
1.6.3.1 NAD(P)H oxidase (H2O2-forming)
IUBMB Comments
Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.6.3.1
- endothelial
- neutrophil
- artery
- p22phox
- dismutase
- angiotensin
- cardiovascular
- apocynin
- hypertension
- oxidases
- nicotinamide
- granulomatous
- cardiac
- fibrosis
- aortic
- atherosclerosis
- catalase
- sod
- leukocyte
- monocyte
-
chemiluminescence
- tnf
- pkc
-
phorbol
- diphenyleneiodonium
-
ii-induced
- iodonium
-
diphenylene
- myeloperoxidase
-
endothelium-dependent
- hypothyroidism
-
oxidase-derived
-
renin-angiotensin
- fmlp
- dihydroethidium
- losartan
-
tempol
- lucigenin
-
nitrotyrosine
- peroxynitrite
-
microbicidal
-
oxidase-dependent
-
vsmcs
-
flavocytochrome
- rac2
- medicine
-
ros-generating
- tiron
-
oxidase-mediated
- synthesis
- agriculture
-
fmlp-induced
- thyroperoxidase
- industry
Synonyms
nad(p)h oxidase, p47phox, gp91phox, nadph-oxidase, p67phox, duox2, duox1, nadph oxidase 4, phagocyte nadph oxidase, nadph oxidase 2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dual oxidase
-
-
-
-
Duox
-
-
-
-
Duox1
Duox2
gp91phox
large NOX
-
-
-
-
LNOX
-
-
-
-
NAD(P)H oxidase
NAD(P)H oxidase 4
NADPH oxidase
NADPH oxidase 4
NADPH oxidase 5
NADPH oxidase type 4
NADPHox
NOX
NOX1
Nox2
NOX3
Nox4
NOX5
p138 thyroid-oxidase
-
-
-
-
p138tox
-
-
-
-
p47phox
p67phox
RBOH
RdxA
rth5
SsNOX38
superoxide-generating NADPH oxidase
ThOX
-
-
-
-
ThOX2
-
-
-
-
thyroid NADPH oxidase
-
-
-
-
thyroid oxidase
-
-
-
-
thyroid oxidase 2
-
-
-
-
NADPH oxidase
-
-
-
-
NADPH oxidase
-
the phagocyte NADPH oxidase is a multicomponent enzyme complex comprising six proteins, namely p22phox (phox: phagocyte oxidase), gp91phox, p47phox, p67phox, p40phox and the small G-protein Rac1 or Rac2
NADPH oxidase
-
-
RdxA
-
the RdxA nitroreductase possesses NAD(P)H oxidase and metronidazole reductase activities
RdxA
-
the RdxA nitroreductase possesses NAD(P)H oxidase and metronidazole reductase activities
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
model of electron transport from NADPH to the terminal electron acceptor O2
-
NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
flavoprotein
-
-
-
NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones
-
-
-
NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
in stable conformation, the active site adopts a closed conformation not allowing the substrate to bind. In presence of urea, an open conformation of the active site with 0.9 nm distance between the indole ring of W47 and the isoalloxazine ring of FMN412 is favored
-
NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
a cytosolic C-terminal dehydrogenase domain includes an FAD cofactor and an NADPH substrate binding site. On activation, electrons are transferred from NADPH to FAD and across the membrane, via heme irons, to molecular oxygen, thus producing superoxide anion, which can be dismutated into hydrogen peroxide
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:oxygen oxidoreductase (H2O2-forming)
Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones.
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CAS REGISTRY NUMBER
COMMENTARY
9032-22-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADPH + H+ + O2
?
-
Substrates: the protein shows NADH-ubiquinone-1 oxidoreductase activity (EC 1.6.5.3), NADPH oxidase (EC 1.6.3.1) and NADPH-ubiquinone-1 oxidoreductase (EC 1.6.5.2) activities
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Products: -
?
NADPH + H+ + O2
NAD(P)+ + H2O2
Substrates: -
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: -
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: enzyme deficiency causes serious hypothyroidism
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
Products: -
Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: involved in Grave's disease
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: involved in Grave's disease
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: NAD(P)H oxidase transfers electrons across membranes to oxygen and generate superoxide anions which rapidly dismutate to hydrogen peroxide
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: enzyme is an important factor for the generation of reactive oxygen species in astrocytes, and the reactive oxygen species generated by enzyme play an essential role in astrocyte survival
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: -
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NADH + H+ + O2
NAD+ + H2O2
-
Substrates: -
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Products: -
?
NADH + H+ + O2
NAD+ + H2O2
-
Substrates: 2 electrons are transferred from cytosolic NADPH to FAD and in succession across the membrane, via redox changes in heme irons. Finally, each electron reduces a molecule of oxygen to a superoxide radical, which is subsequently released outside the cell or in a topologically equivalent compartment, such as a vesicle lumen
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?
NADH + H+ + O2
NAD+ + H2O2
-
Substrates: oxidizes NADH and, less efficiently, NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
Saccharolobus solfataricus MT-4 / DSM 5833
-
Substrates: oxidizes NADH and, less efficiently, NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
Substrates: -
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Products: -
?
NADH + H+ + O2
NAD+ + H2O2
Substrates: -
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?
NADH + H+ + O2
NAD+ + H2O2
Substrates: activity with NADPH is much lower than with NADH
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?
NADPH + H+ + O2
NADP+ + H2O2
Substrates: -
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?
NADPH + H+ + O2
NADP+ + H2O2
-
687742, 710782, 711166, 711688, 711763, 712075, 712673, 712711, 712713, 713338, 724704, 724778, 741619, 742310, 742556, 742557, 743686
Substrates: -
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?
NADPH + H+ + O2
NADP+ + H2O2
-
Substrates: -
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?
NADPH + H+ + O2
NADP+ + H2O2
Substrates: NOX3 is a relevant source of reactive oxygen species generation in the cochlear and vestibular systems. NOX3-dependent ROS generation might contribute to hearing loss and balance problems in response to toxic drugs
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?
NADPH + H+ + O2
NADP+ + H2O2
-
Substrates: -
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?
NADPH + H+ + O2
NADP+ + H2O2
-
Substrates: -
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?
NADPH + H+ + O2
NADP+ + H2O2
Substrates: NOX3 is a relevant source of reactive oxygen species generation in the cochlear and vestibular systems. NOX3-dependent ROS generation might contribute to hearing loss and balance problems in response to ototoxic drugs
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?
NADPH + H+ + O2
NADP+ + H2O2
-
Substrates: the active enzyme complex produces O2 radicals, which are converted into superoxide-derived oxidants such as H2O2, hydroxyl radicals, and peroxynitrite
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?
NADPH + H+ + O2
NADP+ + H2O2
-
Substrates: oxidizes NADH and, less efficiently, NADPH (2fold lower activity)
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Products: -
?
NADPH + H+ + O2
NADP+ + H2O2
Saccharolobus solfataricus MT-4 / DSM 5833
-
Substrates: oxidizes NADH and, less efficiently, NADPH (2fold lower activity)
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Products: -
?
NADPH + H+ + O2
NADP+ + H2O2
Substrates: -
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Products: -
?
NADPH + H+ + O2
NADP+ + H2O2
Substrates: -
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Products: -
?
NADPH + H+ + O2
NADP+ + H2O2
Substrates: activity with NADPH is much lower than with NADH
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?
NADPH + O2
NADP+ + O2-
-
Substrates: enzyme is stimulated by phagocytizable particles
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?
NADPH + O2
NADP+ + O2-
-
Substrates: part of defense mechanism against a wide variety of bacteria
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NADPH + O2
NADP+ + O2-
-
Substrates: in pathological conditions where an increase in NADH concentration occurs, the NADH oxidation catalysed by xanthine dehydrogenase may constitute an important pathway for reactive oxygen species-mediated tissue injuries
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?
NADPH + O2
NADP+ + O2-
-
Substrates: reaction catalyzed by xanthine oxidase and xanthine dehydrogenase
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?
additional information
?
-
-
Substrates: lignin deposition induced by cellulose biosynthesis inhibition is regulated by JAR1-1 and NADPH oxidase-dependent signalling processes
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?
additional information
?
-
-
Substrates: enzyme provides hydrogen peroxide for iodine metabolism in the thyroid
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?
additional information
?
-
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Substrates: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappaB
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?
additional information
?
-
-
Substrates: the production of reactive oxygen species is initiated by the phygocyte NADPH oxidase
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?
additional information
?
-
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Substrates: enzyme isoform Nox3 plays an integral role in insulin-induced p42/44 MAPK signal transmission and VEGF-A production
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?
additional information
?
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Substrates: essential role of enzyme-generated reactive oxigen species in insulin-stimulated activation of hypoxia-inducible factor 1
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?
additional information
?
-
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Substrates: formation of a complex consisting of enzyme, guanine exchange factor for Rac, betaPix, and enzyme organizer NoxO1 is a critical step in EGF-induced generation of reactive oxygen species
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?
additional information
?
-
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Substrates: active NAD(P)H oxidase is required for vascular endothelial growth factor activation of phosphoinositide 3-kinase-Akt-forkhead, and p38 mitogen-activated kinase, but not extracellular signal-related kinase 1/2 or c-Jnu N-terminal kinase. The permissive role of NADPH oxidase on phosphoinositide 3-kinase-Akt-forkhead signaling is mediated at post-vascular endothelial growth factor receptor levels and involves the nonreceptor tyrosine kinase Src
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?
additional information
?
-
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Substrates: NAD(P)H oxidase plays an essential role in maintaining basal levels of reactive oxygen species in NB-4 cells
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?
additional information
?
-
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Substrates: subunit p40phox functions primarily to regulate Fcgamma receptor-induced NADPH oxidase activity rather than assembly of the enzyme, and stimulates superoxide production via a phosphoinositol 3-phosphate signal that increases after phagosome internalization
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?
additional information
?
-
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Substrates: chronic granulomatous disease is a rare inherited immunodeficiency syndrome caused by mutations in four genes encoding essential nicotinamide adenine dinucleotide phosphate (NADPH) oxidase complex components
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?
additional information
?
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Substrates: Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells
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?
additional information
?
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Substrates: Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells
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?
additional information
?
-
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Substrates: NADPH oxidase mediates angiotensin II-stimulated protein synthesis downstream of the type 1 receptor AT1 in myometrium smooth muscle cells
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?
additional information
?
-
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Substrates: the membrane-bound NADPH oxidase in phagocytes, gp91phox/Nox2, produces superoxide, a precursor of microbicidal oxidants, thereby playing a crucial role in host defense. Activation of gp91phox/Nox2 requires assembly with the cytosolic proteins p67phox and p47phox, each containing two SH3 domains. p67phox-SH3(N) specifically functions in gp91phox/Nox2 activation probably via facilitating oxidase assembly
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additional information
?
-
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Substrates: the potent anti-inflammatory, cytokine interleukin-10, acts as a down-regulator of the Nox1-based oxidase in the colon, and suggests an important role of ROS derived from Nox1-based oxidase in the initiation of inflammatory responses of the colon
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?
additional information
?
-
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Substrates: Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. NOX2-produced superoxide can be released outside the cell when Nox2 is located at the plasma membrane, thus allowing it to intercept, e.g., with endothelial-derived nitric oxide before it reaches the adjacent smooth muscle cell layer in vessels
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?
additional information
?
-
Substrates: NOX1 generates superoxide when coexpressed with the p47(phox) and p67(phox) subunits of the phygocyte NADPH oxidase but not when expressed by itself
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?
additional information
?
-
-
Substrates: reactive oxygen species generated by the transverse tubule NADPH oxidase enzyme activate via redox modification the neighboring RyR1 Ca2+ release channels
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?
additional information
?
-
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Substrates: angiotensin II-evoked expression of endothelin-1 in adventitial fibroblasts is mediated, at least in part, by NADPH oxidase. This mechanism stimulates collagen expression thereby implicating the adventitia as a potential contributor to the vascular pathophysiology associated with oxidative stress and vascular remodeling
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?
additional information
?
-
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Substrates: superoxide anions play a key role in suppressing K +secretion during K+ restriction and isoform NoxII is involved in mediating the effect of low K +intake on renal K+ secretion and ROMK channel activity
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?
additional information
?
-
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Substrates: decreased hepatic fibrosis after chronic CCl4 administration in mice with NADPH oxidase deficiency occurs in the setting of greater necrosis and inflammation but decreased apoptosis
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?
additional information
?
-
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Substrates: NADPH oxidase is an important molecular sources responsible for superoxide overproduction after high-glucose exposure
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additional information
?
-
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Substrates: NADPH oxidase may play a potential role in oxidative stress-induced arterial tetrahydrobiopterin and GTP cyclohydrolase I deficiency, resulting in endothelial dysfunction in Ins2Akita type 1 diabetic mice fed a high-cholesterol diet
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?
additional information
?
-
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Substrates: isoform NOX-1 is required for sexual and asexual development, and normal hyphal growth, while isoform NOX-2 is specifically involved in sexual spore function. Regulatory subunit NOR-1 is required for NOX-1 and NOX-2 functions at different developmental stages
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?
additional information
?
-
-
Substrates: hypoosmotic swelling of cardiac myocytes activates volume-sensitive Cl- current via the angiotensin II-reactive oxygen species signalling cascade
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?
additional information
?
-
-
Substrates: enzyme-derived reactive oxigen species modulate cerebral vascular tone under physiological conditions
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?
additional information
?
-
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Substrates: glucose-mediated down-regulation of protein kinase G-I expression in vascular smooth muscle cells occurs through protein kinase C-dependent activation of NAD(P)H oxidase derived superoxide production, contributing to diabetes-associated vessel dysfunctions
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?
additional information
?
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Substrates: NAD(P)H oxidase/superoxide and RhoA/Rho kinase are involved in the interaction between alpha2-adrenoceptors and angiotensin II on renal vascular resistance by mediating signaling events downstream of the phospholipase C/protein kinase C/c-src pathway
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?
additional information
?
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Substrates: involvement of reactive oxygen species from NADPH oxidase in cytokine induction of secretory phospholipase A2-IIA in astrocytes
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additional information
?
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Substrates: L-carnitine inhibits angiotensin II increased NADPH oxidase activity and intracellular ROS levels in cardiac fibroblasts
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?
additional information
?
-
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Substrates: the activated Nox enzyme complex generates superoxide from oxygen by utilizing NADPH as an electron donor, thereby leading to the formation of other species of reactive oxygen
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?
additional information
?
-
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Substrates: the activated Nox enzyme complex generates superoxide from oxygen by utilizing NADPH as an electron donor, thereby leading to the formation of other species of reactive oxygen
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?
additional information
?
-
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Substrates: calcium-dependent kinase CDPK5 induces phosphorylation of the catalytic subunit at resiude S82 and thereby regulates the oxidative burst
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?
additional information
?
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Substrates: the initial burst of superoxide in response to wounding is mediated by isoform Strboh A
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additional information
?
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Substrates: KOD1 (TkNOX) catalyzes oxidation of NADH and NADPH with oxygen from atmospheric air as an electron acceptor
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additional information
?
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Substrates: plasma membrane NADPH oxidase participates in the Ni-induced production of reactive oxygen species, and Ca2+ may be involved in the oxidative stress induced by nickel in wheat roots
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADPH + H+ + O2
NAD(P)+ + H2O2
Substrates: -
Products: -
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: -
Products: -
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
Products: -
Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: enzyme deficiency causes serious hypothyroidism
Products: -
Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
Products: -
Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
Products: -
Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
Products: -
Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
Products: -
Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: involved in Grave's disease
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: involved in Grave's disease
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: enzyme is an important factor for the generation of reactive oxygen species in astrocytes, and the reactive oxygen species generated by enzyme play an essential role in astrocyte survival
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?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
Substrates: production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
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Products: -
?
NADH + H+ + O2
NAD+ + H2O2
-
Substrates: 2 electrons are transferred from cytosolic NADPH to FAD and in succession across the membrane, via redox changes in heme irons. Finally, each electron reduces a molecule of oxygen to a superoxide radical, which is subsequently released outside the cell or in a topologically equivalent compartment, such as a vesicle lumen
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Products: -
?
NADPH + H+ + O2
NADP+ + H2O2
Substrates: -
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?
NADPH + H+ + O2
NADP+ + H2O2
-
Substrates: -
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?
NADPH + H+ + O2
NADP+ + H2O2
-
Substrates: -
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NADPH + H+ + O2
NADP+ + H2O2
Substrates: NOX3 is a relevant source of reactive oxygen species generation in the cochlear and vestibular systems. NOX3-dependent ROS generation might contribute to hearing loss and balance problems in response to toxic drugs
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NADPH + H+ + O2
NADP+ + H2O2
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NADPH + H+ + O2
NADP+ + H2O2
Substrates: NOX3 is a relevant source of reactive oxygen species generation in the cochlear and vestibular systems. NOX3-dependent ROS generation might contribute to hearing loss and balance problems in response to ototoxic drugs
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NADPH + O2
NADP+ + O2-
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Substrates: enzyme is stimulated by phagocytizable particles
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NADPH + O2
NADP+ + O2-
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Substrates: part of defense mechanism against a wide variety of bacteria
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NADPH + O2
NADP+ + O2-
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Substrates: in pathological conditions where an increase in NADH concentration occurs, the NADH oxidation catalysed by xanthine dehydrogenase may constitute an important pathway for reactive oxygen species-mediated tissue injuries
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Substrates: lignin deposition induced by cellulose biosynthesis inhibition is regulated by JAR1-1 and NADPH oxidase-dependent signalling processes
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Substrates: enzyme provides hydrogen peroxide for iodine metabolism in the thyroid
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Substrates: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappaB
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Substrates: the production of reactive oxygen species is initiated by the phygocyte NADPH oxidase
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Substrates: enzyme isoform Nox3 plays an integral role in insulin-induced p42/44 MAPK signal transmission and VEGF-A production
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Substrates: essential role of enzyme-generated reactive oxigen species in insulin-stimulated activation of hypoxia-inducible factor 1
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Substrates: formation of a complex consisting of enzyme, guanine exchange factor for Rac, betaPix, and enzyme organizer NoxO1 is a critical step in EGF-induced generation of reactive oxygen species
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Substrates: active NAD(P)H oxidase is required for vascular endothelial growth factor activation of phosphoinositide 3-kinase-Akt-forkhead, and p38 mitogen-activated kinase, but not extracellular signal-related kinase 1/2 or c-Jnu N-terminal kinase. The permissive role of NADPH oxidase on phosphoinositide 3-kinase-Akt-forkhead signaling is mediated at post-vascular endothelial growth factor receptor levels and involves the nonreceptor tyrosine kinase Src
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Substrates: NAD(P)H oxidase plays an essential role in maintaining basal levels of reactive oxygen species in NB-4 cells
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Substrates: subunit p40phox functions primarily to regulate Fcgamma receptor-induced NADPH oxidase activity rather than assembly of the enzyme, and stimulates superoxide production via a phosphoinositol 3-phosphate signal that increases after phagosome internalization
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Substrates: chronic granulomatous disease is a rare inherited immunodeficiency syndrome caused by mutations in four genes encoding essential nicotinamide adenine dinucleotide phosphate (NADPH) oxidase complex components
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Substrates: Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells
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Substrates: Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells
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Substrates: NADPH oxidase mediates angiotensin II-stimulated protein synthesis downstream of the type 1 receptor AT1 in myometrium smooth muscle cells
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Substrates: the membrane-bound NADPH oxidase in phagocytes, gp91phox/Nox2, produces superoxide, a precursor of microbicidal oxidants, thereby playing a crucial role in host defense. Activation of gp91phox/Nox2 requires assembly with the cytosolic proteins p67phox and p47phox, each containing two SH3 domains. p67phox-SH3(N) specifically functions in gp91phox/Nox2 activation probably via facilitating oxidase assembly
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Substrates: the potent anti-inflammatory, cytokine interleukin-10, acts as a down-regulator of the Nox1-based oxidase in the colon, and suggests an important role of ROS derived from Nox1-based oxidase in the initiation of inflammatory responses of the colon
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Substrates: Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. NOX2-produced superoxide can be released outside the cell when Nox2 is located at the plasma membrane, thus allowing it to intercept, e.g., with endothelial-derived nitric oxide before it reaches the adjacent smooth muscle cell layer in vessels
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Substrates: reactive oxygen species generated by the transverse tubule NADPH oxidase enzyme activate via redox modification the neighboring RyR1 Ca2+ release channels
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Substrates: angiotensin II-evoked expression of endothelin-1 in adventitial fibroblasts is mediated, at least in part, by NADPH oxidase. This mechanism stimulates collagen expression thereby implicating the adventitia as a potential contributor to the vascular pathophysiology associated with oxidative stress and vascular remodeling
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Substrates: superoxide anions play a key role in suppressing K +secretion during K+ restriction and isoform NoxII is involved in mediating the effect of low K +intake on renal K+ secretion and ROMK channel activity
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Substrates: decreased hepatic fibrosis after chronic CCl4 administration in mice with NADPH oxidase deficiency occurs in the setting of greater necrosis and inflammation but decreased apoptosis
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Substrates: NADPH oxidase is an important molecular sources responsible for superoxide overproduction after high-glucose exposure
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Substrates: NADPH oxidase may play a potential role in oxidative stress-induced arterial tetrahydrobiopterin and GTP cyclohydrolase I deficiency, resulting in endothelial dysfunction in Ins2Akita type 1 diabetic mice fed a high-cholesterol diet
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Substrates: isoform NOX-1 is required for sexual and asexual development, and normal hyphal growth, while isoform NOX-2 is specifically involved in sexual spore function. Regulatory subunit NOR-1 is required for NOX-1 and NOX-2 functions at different developmental stages
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Substrates: hypoosmotic swelling of cardiac myocytes activates volume-sensitive Cl- current via the angiotensin II-reactive oxygen species signalling cascade
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Substrates: enzyme-derived reactive oxigen species modulate cerebral vascular tone under physiological conditions
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Substrates: glucose-mediated down-regulation of protein kinase G-I expression in vascular smooth muscle cells occurs through protein kinase C-dependent activation of NAD(P)H oxidase derived superoxide production, contributing to diabetes-associated vessel dysfunctions
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Substrates: NAD(P)H oxidase/superoxide and RhoA/Rho kinase are involved in the interaction between alpha2-adrenoceptors and angiotensin II on renal vascular resistance by mediating signaling events downstream of the phospholipase C/protein kinase C/c-src pathway
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Substrates: involvement of reactive oxygen species from NADPH oxidase in cytokine induction of secretory phospholipase A2-IIA in astrocytes
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Substrates: L-carnitine inhibits angiotensin II increased NADPH oxidase activity and intracellular ROS levels in cardiac fibroblasts
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Substrates: the activated Nox enzyme complex generates superoxide from oxygen by utilizing NADPH as an electron donor, thereby leading to the formation of other species of reactive oxygen
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Substrates: the activated Nox enzyme complex generates superoxide from oxygen by utilizing NADPH as an electron donor, thereby leading to the formation of other species of reactive oxygen
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Substrates: calcium-dependent kinase CDPK5 induces phosphorylation of the catalytic subunit at resiude S82 and thereby regulates the oxidative burst
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Substrates: the initial burst of superoxide in response to wounding is mediated by isoform Strboh A
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Substrates: KOD1 (TkNOX) catalyzes oxidation of NADH and NADPH with oxygen from atmospheric air as an electron acceptor
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Substrates: plasma membrane NADPH oxidase participates in the Ni-induced production of reactive oxygen species, and Ca2+ may be involved in the oxidative stress induced by nickel in wheat roots
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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contains 1 FAD molecule/subunit, the enzyme requires the presence of FAD as cofactor
FAD
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a dehydrogenase domain is binding FAD and NADPH, Nox1, Nox2, and Nox4 requires FAD and NADPH. Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites
FAD
Nox1 protein reveals the presence of six transmembrane domains and one FAD/NADPH binding cytosolic domain
heme
-
4 conserved histidine residues in transmembrane helices III and V, thought to coordinate 2 heme molecules, mutation of these histidines abolishes binding to p22phox
NADH
preference to NADPH versus NADH as an electron donor during oxygen reduction
NADPH
-
-
NADPH
-
a dehydrogenase domain is binding FAD and NADPH, Nox1, Nox2, and Nox4 requires FAD and NADPH. Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites
NADPH
Nox1 protein reveals the presence of six transmembrane domains and one FAD/NADPH binding cytosolic domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Ni2+
-
treatment of root with Ni2+ results in significant increase in level of membrane lipid peroxidation, content of H2O2, the production rate of superoxide radicals and the activity of the PM NADPH oxidase. Effects of Ni2+ are inhibitied by treratment with enzyme inhibitors diphenylene idonium, imidazole and pyridine
Zn2+
additional information
Ca2+
-
Ca2+-induced conformation change of NADPH oxidase 5 N-terminus leads to enzyme activation through an intramolecular interaction
Ca2+
-
store-operated Ca2+ entry is required at the beginning of NADPH oxidase activation in response to N-formyl-L-methionyl-L-leucyl-Lphenylalanine in neutrophil-like HL-60 cells. When extracellular Ca2+ is initially removed, early addition of Ca2+ after stimulation causes a complete restoration of Ca2+ entry and H2O2production. Both Ca2+ entry and H2O2 production are decreased by purported SOCE blockers, 2-aminoethoxydiphenyl borane (2-APB) and SK&F 96365. Ca2+ influx in HL-60 cells relies on different membrane transient receptor potential canonical channels and Orai1 for allowing NADPH oxidase activation
Ca2+
-
an increase in cytosolic calcium concentration triggers high superoxide production by Nox5. Calcium induces binding of the N-terminal domain of Nox5 to the dehydrogenase domain, thus relieving autoinhibition. Two mechanisms may increase Nox5 sensitivity, allowing activation by resting calcium concentrations: (1) calcium-dependent binding of calmodulin to another site in the dehydrogenase domain157 and (2) phosphorylation of serine and threonine residues by protein kinase C and calcium/calmodulin-dependent kinase II
Ca2+
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the activity of NOX5 appears to be regulated by a self-contained Ca2+ binding domain, residues 1-169, the conformational change of the domain upon Ca2+ binding is essential for domain-domain interaction and superoxide production. Ca2+ binding to Ca2+ binding domain induces a conformational change that exposes hydrophobic patches and increases the quenching accessibilities of its Trp residues and 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid at Cys107, no significant changes in the secondary structures of Ca2+ binding domain upon metal binding. The C-terminal half of the domain has a higher Ca2+ binding affinity, a higher chemical stability, and a slow Ca2+ dissociation. the N- and C-terminal halves of the domain are not completely structurally independent
Ca2+
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Ca2+ may regulate the interaction between cytosolic regulator subunit Rac and the N-terminal extension of the catalytic subunit in a dynamic manner
Ca2+
-
regulates enzyme activity
Ca2+
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a Ca2+/NADPH-dependent H2O2 generating system is associated with isoform Duox2 protein expression
Ca2+
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pretreatments of wheat seedlings with Ca2+ channel blockers inhibits Ni-induced increase in plasma membrane NADPH oxidase activity
additional information
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Mg2+ cannot substitute for Ca2+, metal binding/dissociation kinetics, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epicatechin
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serves as prodrug for conversion into apocynin-like NAD(P)H oxidase inhibitors
(-)-epicatechin glucuronide
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acts both as a superoxide anion scavenger,and inhibitory to NAD(P)H oxidase, with apocynin-like mode of NADPH oxidase inhibition
(-)-epigallocatechin-3-O-(3-O-methyl)-gallate
-
inhibition of intracellular reactive oxygen species generation
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundec-3-yn-1-yl]octahydro-2,2'-bifuran-5-yl]dodec-4-yn-1-ol
-
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(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]dodecan-1-ol
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(1R,1'R)-1,1'-((2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyl)-bis-(6-(4-n-butylphenoxy)hex-3-yn-1-ol)
-
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(1R,1'R)-1,1'-((2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyl)-bis-(6-(4-n-butylphenoxy)hexan-1-ol)
-
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(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide
-
complete inhibition at 0.01 mM
(3Z)-3-(3,4-dihydroxybenzylidene)-5-nitro-1,3-dihydro-2H-indol-2-one
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complete inhibition at 0.01 mM
(3Z)-3-[4-hydroxy-3,5-di(propan-2-yl)benzylidene]-1,3-dihydro-2H-indol-2-one
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complete inhibition at 0.01 mM
(5'Z)-5'-[(4-heptyl-5-methyl-1H-pyrrol-2-yl)methylidene]-4'-methoxy-1H,5'H-2,2'-bipyrrole
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i.e. PG-L-1, prodigosin analogue, a red pigment isolated from marine bacterial strain. Significant inhibition of superoxide anion production by phorbol 12-myristate 13-acetate stimulated RAW 264.7 cells. (5'Z)-5'-[(4-heptyl-5-methyl-1H-pyrrol-2-yl)methylidene]-4'-methoxy-1H,5'H-2,2'-bipyrrole strongly inhibits the association of subunits p47phox and Rac in the plasma membrane
1-(2-chlorobenzyl)-4-methyl-5-[3-(2-oxopyrrolidin-1-yl)propyl]-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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1-(4-fluorobenzyl)-5-[2-(1H-indol-3-yl)ethyl]-4-methyl-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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1-acetyl-2-(2-chlorophenyl)-4-methyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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1-acetyl-4-methyl-2-(2-methylphenyl)-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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1-acetyl-4-methyl-2-phenyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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1-[(3-methoxyphenyl)acetyl]-4-methyl-2-phenyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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15-cis-(4-propyl-cyclohexyl)-16,17,18,19,20-pentanor-9-deoxy-9alpha,6-nitrilo-prostaglandin F1 methyl ester
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0.021 mM, 50% inhibition of the enzyme in neutrophils possible due to scavenging of O2-, inhibition of SDS-induced activation in cell free extracts, 0.22 mM, 50% inhibition
2,3,8,9-tetrahydroxy-5-(2-hydroxy-5-nitrobenzyl)phenanthridin-6(5H)-one
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complete inhibition at 0.01 mM
2,3,8,9-tetrahydroxy-5-(3-nitrobenzyl)phenanthridin-6(5H)-one
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complete inhibition at 0.01 mM
2,3,8,9-tetrahydroxy-5-(4-nitrobenzyl)phenanthridin-6(5H)-one
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93% inhibition at 0.01 mM
2,3,8,9-tetrahydroxy-5-[2-(phenylsulfonyl)benzyl]phenanthridin-6(5H)-one
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95% inhibition at 0.01 mM
2,4-dimethyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
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2-(1,3-benzothiazol-2-yl)-1-(2-chlorobenzyl)-4-methyl-5-(morpholin-4-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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2-(1,3-benzothiazol-2-yl)-4-ethyl-5-(2-methoxyethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
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2-(1,3-benzothiazol-2-yl)-4-methyl-1-(pyridin-2-ylmethyl)-5-(tetrahydrofuran-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
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2-(1,3-benzothiazol-2-yl)-4-methyl-5-(morpholin-4-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
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2-(1,3-benzothiazol-2-yl)-5-[2-(1H-imidazol-4-yl)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(1,3-benzothiazol-2-yl)-5-[2-(1H-indol-3-yl)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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2-(2,5-dichlorobenzyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
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2-(2-chloro-4-fluorobenzyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
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2-(2-chloro-4-fluorophenyl)-4,5-dimethyl-1H-pyrazolo[4,3-c]-pyridine-3,6(2H,5H)-dione
-
-
2-(2-chloro-4-fluorophenyl)-4-methyl-5-(pyridin-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chloro-4-fluorophenyl)-5-(2-pyridin-2-ylethyl)-4-(pyrrolidin-1-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-(2-fluorophenyl)-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
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2-(2-chlorophenyl)-4-([methyl(phenyl)amino]methyl)-5-[2-(pyridin-2-yl)ethyl]-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-methyl-5-(3-phenylprop-2-yn-1-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-methyl-5-(4-[(4-methylpiperazin-1-yl)methyl]benzyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-methyl-5-(pyridin-2-ylmethyl)-1H-pyrazolo-[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-methyl-5-[(6-morpholin-4-ylpyridin-2-yl)-methyl]-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-methyl-5-[4-(4-methylpiperazin-1-yl)-4-oxobutyl]-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-[(4-fluorophenoxy)methyl]-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-[[4-(3-methoxyphenyl)piperazin-1-yl]-methyl]-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-4-[[methyl(phenyl)amino]methyl]-5-(pyridin-4-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-5-(3-ethoxypropyl)-4-methyl-1-(pyridin-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-5-(3-hydroxypropyl)-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-5-(cyclohexylmethyl)-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-5-[(1-methyl-1H-pyrazol-3-yl)methyl]-4-[[methyl(pyridin-3-ylmethyl)amino]methyl]-1H-pyrazolo[4,3-c]-pyridine-3,6(2H,5H)-dione
-
-
2-(2-chlorophenyl)-5-[2-(dimethylamino)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(2-methoxyethyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
-
2-(3,4-dihydroxyphenyl)-3,7-dihydroxy-6-methoxy-4H-chromen-4-one
-
complete inhibition at 0.01 mM
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
-
complete inhibition at 0.01 mM
2-(3,4-dihydroxyphenyl)-5-hydroxy-3,7-dimethoxy-4H-chromen-4-one
-
88% inhibition at 0.01 mM
2-(4-chlorobenzyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
-
2-(4H-3,1-benzothiazin-2-yl)-1-benzyl-4-methyl-5-(tetrahydrofuran-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
2-(7-chloroquinolin-4-yl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
-
2-benzyl-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
-
2-[(2,3,8,9-tetrahydroxy-6-oxophenanthridin-5(6H)-yl)methyl]benzonitrile
-
97% inhibition at 0.01 mM
2-[(2E)-2-(3,4-dihydroxybenzylidene)hydrazinyl]-N-(3-nitrophenyl)-2-oxoacetamide
-
96% inhibition at 0.01 mM
2-[2-(4-chlorophenoxy)ethyl]-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
-
2-[4-(benzyloxy)phenyl]-4,5-dimethyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
3,5,7-trihydroxy-2-(4-hydroxy-3-methylphenyl)-4H-chromen-4-one
-
94% inhibition at 0.01 mM
3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
complete inhibition at 0.01 mM
3-(3,4-dihydroxycyclohexa-2,4-dien-1-yl)-2,7-dihydroxy-4H-chromen-4-one
-
86% inhibition at 0.01 mM
3-(3-chlorophenyl)-N-[2-(piperazin-1-yl)phenyl]-1,4,6,7-tetrahydro-5H-pyrazolo[4,3-c]pyridine-5-carboxamide
-
Shionigi compound
3-(3-chlorophenyl)-N-[4-(piperidin-4-yl)phenyl]pyrazolo[1,5-a]pyrimidine-5-carboxamide
-
-
3-(4,5-dimethyl-3,6-dioxo-1,3,5,6-tetrahydro-2H-pyrazolo[4,3-c]pyridin-2-yl)benzonitrile
-
-
4,5-dimethyl-2-(4-phenyl-1,3-thiazol-2-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4,5-dimethyl-2-(5-[(4-methylpiperazin-1-yl)sulfonyl]pyridin-2-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4-(2-aminoethyl)benzenesulfonyl fluoride
-
significantly reduces reactive oxygen species production, NADPH oxidase activity, and all the apoptotic events, and cell death induced by both 5 mM KCl and staurosporin
4-methyl-2-(2-methylphenyl)-5-(pyridine-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4-methyl-2-phenyl-5-(2-phenylethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4-methyl-2-phenyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]-pyridine-3,6(2H,5H)-dione
-
-
4-methyl-3-methylidene-2-(2-phenylethyl)-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
-
4-methyl-3-methylidene-2-[2-(morpholin-4-yl)ethyl]-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
-
4-methyl-5-(3-phenoxybenzyl)-2-([1,2,4]triazolo[4,3-b]pyridazin-6-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4-[(4-fluorophenoxy)methyl]-5-(2-methoxyethyl)-2-(2-morpholin-4-ylethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4-[(benzyloxy)methyl]-2-(2-chlorophenyl)-5-(pyrazin-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4-[[(2-chlorobenzyl)oxy]methyl]-2-(2-chlorophenyl)-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
4-[[2-(1,3-benzothiazol-2-yl)-4-methyl-3,6-dioxo-1,2,3,6-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl]methyl]benzoic acid
-
-
4-[[2-(2-chlorophenyl)-4-methyl-3,6-dioxo-1,2,3,6-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl]methyl]benzenesulfonamide
-
-
4-[[benzyl(methyl)amino]methyl]-2-(2-chloro-4-fluorophenyl)-5-(3-methoxypropyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
complete inhibition at 0.01 mM
5-(1,3-benzodioxol-5-ylmethyl)-4-methyl-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
5-(E)-6,9-deoxa-6,9alpha-methylene-15-cyclopentyl-16,17,18,19,20-pentanor-prostaglandin I2
-
inhibition of sodiumdodecylsulfate-induced activation in cell free extracts, 0.17 mM, 50% inhibition
5-(furan-2-ylmethyl)-4-methyl-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
5-benzyl-2-(4-fluorophenyl)-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
-
5-cyclopropyl-2-[1-(2-fluoro-benzyl)-1H-pyrazolo[3,4-b]pyridine-3-yl]pyrimidin-4-ylamine
-
i.e. BAY 41-2272, inhibits the induction of the expression of subunits p22phox and gp91phox by 11alpha,9alpha-epoxymethanoprostaglandin F 2alpha. Enhances nitric oxide-induced relaxations in a concentration-dependent manner
5-[(2,5-dihydroxybenzyl)amino]-2-hydroxybenzoic acid
-
82% inhibition at 0.01 mM
aminoethylbenzenesulfonylfluoride
-
treatment blocks the induction of reactive oxygen species production by the dopaminergic toxin MPP+. Co-treatment with inhibitors aminoethylbenzenesulfonylfluoride, apocynin, or diphenylene iodinium significantly suppresses MPP*-induced cell death and attenuates MPP*-induced increases in caspase-3 enzymatic activity
angiotensin
-
angiotensin-(1-7) decreases the elevated levels of renal NADPH oxidase activity and attenuates the activation of subunit NOX-4 gene expression in the diabetic hypertensive kidney. Angiotensin-(1-7) treatment increases sodium excretion but does not affect mean arterial pressure in diabetic hypertensive rats. The significant increase in urinary protein in the diabetic compared to control hypertensive rat is reduced by angiotensin-(1-7). Angiotensin-(1-7) treatment also attenuates the diabetes-induced increase in renal vascular responsiveness to endothelin-1, norepinephrine, and angiotensin II in hypertensive rats, but significantly increases the vasodilation of the renal artery of hypertensive and diabetic hypertensive rats to the vasodilator agonists
betaPix
-
guanine nucleotide exchange factor, overexpression of the central PH domain of betaPix results in inhibition of superoxide anion generation in response to EGF
-
betulinic acid
-
attenuates the expression of NAD(P)H oxidase subunits Nox4 and p22phox, thereby reducing oxidative stress and improving endothelial nitric oxide synthase function. Treated cells show in increased production of bioactive nitric oxide
Cdc42
-
a small monomeric GTPase, competitive inhibitor of Nox2, might also be a competitive inhibitor of Nox1
-
CoA
NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not; NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not; NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not; NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not
endothelin-1
-
inhibits NADPH oxidase activity, superoxide generation, and cell proliferation in human abdominal aortic endothelial cells via the ETB1-Pyk2-Rac1-Nox1 pathway. Endothelin-1 significantly attenuates NADPH oxidase activity and cell proliferation, which can be abolished by silencing of the Nox1 gene. RNA interference silencing of ETB1 receptors significantly increases NADPH oxidase activity, and blocks the inhibitory effect of endothelin-1 on NADPH oxidase activity. Endothelin-1 also attenuates angiotensin II-induced activation of NADPH oxidase and cell proliferation
gp91ds
-
fusion peptide that inhibits assembly of NADPH oxidase by mimicking the gp91phox docking site for the cytoplasmic p47phox subunit. gp91ds prevents NADPH oxidase activity, cytokine release, and neurotoxicity induced by HIV regulatory protein Tat in primary microglia
-
hemin
-
hemin treatment increases hemin oxidase-1 expression and activity in aorta and kidney of apolipoprotein Edeficient mice and significantly reduces both NADPH oxidase activity and superoxide generation in situ
N'1,N'2-bis[(E)-(2,3-dihydroxyphenyl)methylidene]ethanedihydrazide
-
complete inhibition at 0.01 mM
N'1,N'2-bis[(E)-(3,4-dihydroxyphenyl)methylidene]ethanedihydrazide
-
complete inhibition at 0.01 mM
N-(3-aminophenyl)-N'-[1-(4-hydroxy-3-methoxyphenyl)ethyl]ethanediamide
-
complete inhibition at 0.01 mM
N-[(3Z)-3-(4-hydroxy-3-methoxybenzylidene)-2-oxo-2,3-dihydro-1H-indol-5-yl]acetamide
-
complete inhibition at 0.01 mM
N-[1-(3,4-dihydroxyphenyl)ethyl]-N'-(3-nitrophenyl)ethanediamide
-
complete inhibition at 0.01 mM
N-[2-(2-chlorophenyl)-4-methyl-3,6-dioxo-1,2,3,6-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl]-2-(4-fluorophenoxy)acetamide
-
-
N-[2-(4-hydroxy-phenyl)-ethyl]-2-(2, 5-dimethoxy-phenyl)-3-(3-methoxy-4-hydroxy-phenyl)-acrylamide
N-[3-(4,5-dimethyl-3,6-dioxo-1,3,5,6-tetrahydro-2H-pyrazolo[4,3-c]pyridin-2-yl)phenyl]acetamide
-
-
N4-(3-aminophenyl)[1]benzothieno[3,2-d]pyrimidine-4,8-diamine
-
98% inhibition at 0.01 mM
N4-(4-aminophenyl)[1]benzothieno[3,2-d]pyrimidine-4,8-diamine
-
complete inhibition at 0.01 mM
nitroglycerin
-
in rats treated with nitroglycerin for three days, superoxide production is increased in all aortic layers, while expression of isoforms nox1, nox2 and nox4 is significantly decreased. In vascular smooth muscle cells exposed to nitroglycerin for 6-24 h, NAD(P)H oxidase activity is increased, in spite of nox1 downregulation
O-methyl-epicatechin
-
inhibits endothelial NAD(P)H oxidase activity and prevents superoxide anion formation
phallacidin
-
pretreatment of human pulmonary artery endothelial cells before induction of hyperoxia attenuates hyperoxia-induced cortical actin thickening and reactive oxygen species production
procyanidin B2
-
acts both as a superoxide anion scavenger, and inhibitory to NAD(P)H oxidase, with apocynin-like mode of NADPH oxidase inhibition
prostaglandin E1
-
inhibition of sodiumdodecylsulfate-induced activation in cell free extracts, 0.044 mM, 50% inhibition
rosuvastatin
-
rosuvastatin reduces systolic blood pressure in spontaneously hypertensive rats but does not change plasma lipid levels. Rosuvastatin treatment in spontaneously hypertensive rats significantly decreases reactive oxygen species levels, NAD(P)H activity in retinal ganglion cells, and increases retinal plasmalogen content in spontaneously hypertensive rats, but does not modify the electroretinogram response
sepiapterin
-
induction of oxidative stress, p22phox mRNA, endothelial nitric oxide synthase mRNA, and protein by glucose are lowered by concurrent incubation with sepiapterin
sinomenine
-
morphinan analog, inhibits NAD(P)H oxidase cytosolic subunit p47phox translocation to the cell membrane and thus reduces lipopolysaccharide-induced extracellular reactive oxygen species production. Protects neuron-glial cell cultures at both micro- and sub-picomolar concentrations against dopaminergic neuron death, but not protection is seen at nanomolar concentrations
taxol
-
induces concentration-dependent neuronal death with apoptotoic features. Neuronal death is significantly attenuated by anti-apoptotic rugs and by antioxidants such as trolox, ascorbic acid, and tempol. Exposure to taxol increases the expression of NAD(P)H oxidase subunits p45phox and gp91phox and induces translocation of p47phox protein to the membrane in cortical cultures
telmisartan
-
0.01 mM telmisartan decreases NAD(P)H oxidase activity by 32% in MIN-6 cells
tetramethylpyrazine
-
inhibits the induction of NAD(P)H oxidase activity by angiotensin II and the concomitant increase of intracellular reactive oxygen species levels and ERK phosphorylation
(-)-epigallocatechin gallate
-
inhibition of intracellular reactive oxygen species generation, inhibition of translocation of cytosolic subunits into membrane
(-)-epigallocatechin gallate
-
inhibition of intracellular reactive oxygen species generation
apocynin
-
in cells continuously treated with nitric oxide donors, including nitroglycerin, over 2-3 days, basal production of nitrite and nitrate is diminished. The diminished basal nitric oxide levels are mitigated by intermittent treatment allowing an 8-h daily nitrate-free interval during the 2- to 3-day treatment period. Addition of the NAD(P)H oxidase inhibitor apocynin restores the basal levels of nitric oxides that are decreased by continuous nitroglycerin treatment. Apocynin causes significant improvement of increased mRNA and protein levels of endothelial nitric oxide synthase in cells given nitroglycerin continuously over the treatment period. Apocynin also reduces endothelial production of reactive oxygen species after continuous nitroglycerin treatment
apocynin
-
blocks production of superoxide anion in sarcoplasmic reticulum of coronary arterial myocytes
apocynin
-
in sarcoplasmic reticulum vesicles isolated after exercise and tachycardia, apocynin prevents the increase in ryanodine receptor-2 S-glutathionylation, reduced calcium release activity, and completely prevents the protective effects of exercise and tachycardia on infarct size
apocynin
-
enzyme inhibitor, pretreatment of cells completely blocks insulin-stimulated activation of hypoxia-inducible factor 1
apocynin
-
significantly blunts both the generation of reactive oxygen species and induction of apoptosis induced by apigenin
apocynin
-
4-hydroxy-3-methoxyacetophenonesubstituted, a natural molecule structurally related to vanillin, acts on p47phox, requires a peroxidase such as MPO
apocynin
-
paraquat-induced reactive oxygen species production is inhibited by NADPH oxidase inhibitors, apocynin and diphenylene iodonium. Apocynin and diphenylene iodonium also rescue cells from paraquat-induced toxicity. The inhibitors for protein kinase C delta or extracellular signal-regulated kinases ERK1/2 can partially attenuate paraquat-induced reactive oxygen species production and cell death
apocynin
-
treatment significantly decreases angiotensin II-induced endothelin-1 RNA and peptide expression, superoxide production as well as collagen expression
apocynin
-
aortic rings from mice deificient in subunit p47phox are more sensitive to apocynin-induced dilation than wild-type aortic rings. Rho kinase inhibition reduces or prevents the inhibitory effect of apocynin on agonist-induced vasoconstriction and apocynin inhibits the phosphorylation of Rho kinase substrates
apocynin
-
inhibition of NAD(P)H oxidase by apocynin in ischemia-induced mice prevents blood-brain barrier damage in the ischemic hemisphere I after reperfusion
apocynin
-
inhibits NADPH oxidase and induces increased nitric oxide synthesis by eliciting a generation of reactive oxygen species, which in turn causes transcription factor NF-kappaB activation and increased expression of inducible nitric oxides
apocynin
-
selective NADPH oxidase inhibitor, inhibition of NADPH oxidase protects photoreceptors from light-induced degeneration
apocynin
-
when luminal NaCl in kidney is switched from 10 to 80 mM, a situation of initiating maximum tubuloglomerular feedback response, superoxide anion production significantly increases. In the presence of apocynin, superoxide anion production is inhibited by 80%
apocynin
-
after 14 days, local treatment with apocynin via the adventitia, reduces superoxide generation. Apocynin significantly reduces neointima formation and proliferation of cells in both the neointima and adventitia. Nitric oxide-dependent vasorelaxation to acetylcholine, which is normally impaired in collared arteries, is improved, and apocynin suppresses the endothelial expression of intracellular adhesion molecule- and vascular cell adhesion molecule-
apocynin
-
in rabbits with heart failure induced by myocardial infarction, apocynin reduces NADPH oxidase activity, subunit p47phox protein, oxidative stress, myocyte apoptosis, and Bax protein, increases Bcl-2 protein, and ameliorates left ventricular dilatation and dysfunction
apocynin
-
also named acetovanillone, 4'-hydroxy-3'-methoxyacetophenone
apocynin
-
smoking impaires acetylcholine-induced relaxations of carotid arteries, which can be improved by the NAD(P)H oxidase inhibitor apocynin. Vascular mRNA expression of the proinflammatory cytokines IL-1, IL-6, and TNF-alpha and that of inducible nitric oxide synthase is significantly increased by both smoking and cigarette smoke extract exposure, which can be prevented by apocynin, diphenyleneiodinium, or scavenging of H2O2
apocynin
-
blocks up-regulation of epidermal growth factor receptor ligands and Akt activation by transforming growth factor-beta
apocynin
-
prevents inflammation-mediated toxicity to motor neurons induced by lipopolysaccharide
apocynin
-
apocynin does not reduce arterial pressure acutely in spontaneously hpertensive rats when given orally over 1-week intervals or when given i.v. Apocynin potently inhibits granulocyte NADPH oxidase but not vascular NADPH-oxidase dependent oxygen radical formation unless exogenous peroxidase is added to vascular preparations. Apocynin dilates rat intrarenal and coronary arteries independently of pharmacological interventions that reduce vascular superoxide radical abundance and actions
apocynin
-
inhibition of NAD(P)H oxidase in alveolar macrophage by apocynin results in down-regulation of arginase activity and decrease in arginase I mRNA
apocynin
-
apocynin reduces avascularity and apoptosis in the oxygen-induced retinopathy model
apocynin
-
treatment blocks the induction of reactive oxygen species production by the dopaminergic toxin MPP+. Co-treatment with inhibitors aminoethylbenzenesulfonylfluoride, apocynin, or diphenylene iodinium significantly suppresses MPP*-induced cell death and attenuates MPP*-induced increases in caspase-3 enzymatic activity
apocynin
-
significantly attenuates hypoxia/reoxygenation-induced reactive oxygen species formation in porcine coronary artery endothelial cells and suppresses the hypoxia/reoxygenation-induced endothelial spheroid sprouting
bilirubin
-
bilirubin concentration-dependently reduces NADPH oxidase-dependent superoxide production stimulated by phorbol 12-myristate 13-acetate
bilirubin
-
bilirubin concentration-dependently reduces NADPH oxidase-dependent superoxide production stimulated by angiotensin II in vascular smooth muscle cells
diphenylene iodinium
-
inhibition of NAD(P)H oxidase, causes wild-type plants to phenocopy the isoform rdh2/Atrbohc mutant
diphenylene iodinium
-
treatment of NB-4 cells blocks basal generation of reactive oxygen species and arsenic trioxide-induced apoptosis
diphenylene iodinium
-
significant suppression of release of reactive oxygen species in astrocytes caused by calcium ionophores or opsonized zymosan
diphenylene iodinium
-
NaCl-induced increase in total Ca2+ in plasma membrane vesicles is partially abolished by the addition of diphenyleneiodinium
diphenylene iodinium chloride
-
enzyme inhibitor, pretreatment of cells completely blocks insulin-stimulated activation of hypoxia-inducible factor 1
diphenylene iodinium chloride
-
inhibition of enzyme, resulting in inhibitied growth and reactive oxygen species formation in tobacco pollen tube cultures
diphenylene iodinium chloride
-
inhibits NAD(P)H oxidase, effectively inhibits wound healing in potato tuber, and increases susceptibility to microbial infection and decay in 1-month-old tubers
diphenylene iodonium
-
blocks production of superoxide anion in sarcoplasmic reticulum of coronary arterial myocytes
diphenylene iodonium
-
significantly blunts both the generation of reactive oxygen species and induction of apoptosis induced by apigenin
diphenylene iodonium
-
inhibition of NADPH oxidase. In cells deficient for von Hippel-Lindau tumor suppressor gene, presence of diphenyleneiodonium decreases the expression of hypoxia-inducible factor 2alpha
diphenylene iodonium
-
directly inhibits the activity of enzyme component gp91phox/NOX2, the inhibitor targets the FAD binding sequence found in other flavoproteins and is therefore not specific for NOX2
diphenylene iodonium
-
paraquat-induced reactive oxygen species production is inhibited by NADPH oxidase inhibitors, apocynin and diphenylene iodonium. Apocynin and diphenylene iodonium also rescue cells from paraquat-induced toxicity. The inhibitors for protein kinase C delta or extracellular signal-regulated kinases ERK1/2 can partially attenuate paraquat-induced reactive oxygen species production and cell death
diphenylene iodonium
-
significantly inhibits RCC 786-O tumor formation in athymic mice
diphenylene iodonium
-
significantly reduces reactive oxygen species production, NADPH oxidase activity, and all the apoptotic events, and cell death induced by both 5 mM KCl and staurosporin
diphenylene iodonium
-
treatment blocks the induction of reactive oxygen species production by the dopaminergic toxin MPP+. Co-treatment with inhibitors aminoethylbenzenesulfonylfluoride, apocynin, or diphenylene iodinium significantly suppresses MPP*-induced cell death and attenuates MPP*-induced increases in caspase-3 enzymatic activity
diphenyleneiodonium
-
inhibition of NAD(P)H oxidase abolishes depolarisation of the neutrophil plasma membrane by electron current
diphenyleneiodonium
-
treatment significantly decreases angiotensin II-induced endothelin-1 RNA and peptide expression, superoxide production as well as collagen expression
diphenyleneiodonium
-
vascular mRNA expression of the proinflammatory cytokines IL-1, IL-6, and TNF-alpha and that of inducible nitric oxide synthase is significantly increased by both smoking and cigarette smoke extract exposure, which can be prevented by apocynin, diphenyleneiodinium, or scavenging of H2O2
diphenyleneiodonium
-
blocks up-regulation of epidermal growth factor receptor ligands and Akt activation by transforming growth factor-beta
diphenyleneiodonium
-
NAD(P)H oxidase inhibitor, complete inhibition at 0.001 mM
diphenyleneiodonium
-
significantly attenuates hypoxia/reoxygenation-induced reactive oxygen species formation in porcine coronary artery endothelial cells and suppresses the hypoxia/reoxygenation-induced endothelial spheroid sprouting
gp91ds-tat
-
peptidyl inhibitor. Treatment of engineered tissue blocks of a chamber model significantly reduces the level of reactive oxygen species and retards the tissue formation process. Vessels in treated tissues have smaller lumens than control
honokiol
-
submicromolar concentrations of honokiol suppress the increases of NADPH oxidase activity, Rac-1 phosphorylation, p22phox protein expression, and reactive oxygen species production in high glucose-stimulated HUVEC cells. Honokiol also suppresses high glucose-induced cyclooxygenase-2 upregulation and prostaglandin E2 production. Honokiol can reduce increased caspase-3 activity and the subsequent apoptosis and cell death triggered by high glucose medium
N-[2-(4-hydroxy-phenyl)-ethyl]-2-(2, 5-dimethoxy-phenyl)-3-(3-methoxy-4-hydroxy-phenyl)-acrylamide
-
i.e. FLZ, squamosamide derivative. FLZ inhibits the translocation of the cytosolic subunit p47phox to the membrane and thus inhibits the activation of NAD(P)H oxidase. In vivo, FLZ significantly protects against 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-induced dopaminergic neuronal loss
N-[2-(4-hydroxy-phenyl)-ethyl]-2-(2, 5-dimethoxy-phenyl)-3-(3-methoxy-4-hydroxy-phenyl)-acrylamide
-
i.e. FLZ, squamosamide derivative, mediates anti-inflammatory and neuroprotective effects in both lipopolysaccharide-and 1-methyl-4-phenylpyridinium-mediated models of Parkinson's disease. FLZ inhibits the translocation of the cytosolic subunit p47phox to the membrane and thus inhibits the activation of NAD(P)H oxidase
neopterin
-
significantly blunts both the generation of reactive oxygen species and induction of apoptosis induced by apigenin
Phenylarsine oxide
-
partial inactivation and desensitization of activity to Ca2+, effect is completely reversed by addition of 2,3-dimercaptopropanol
rosiglitazone
-
activates 5'-AMP-activated protein kinase which, in turn, prevents hyperactivity of NAD(P)H oxidase induced by high glucose, possibly through protein kinase C inhibition. Rosiglitazone protects endothelial cells against glucose-induced oxidative stress with an 5'-AMP-activated protein kinase-dependent and a PPARgamma-independent mechanism
rosiglitazone
-
treatment of animals for 1 week significantly reduces aortic superoxide production and the mRNA expression of enzyme subunits Nox-1, Nox-2, and Nox-4
VAS3947
-
i.e. 3-benzyl-7-(2-oxazolyl)thio-1,2,3-triazolo[4,5-d]pyrimidine, specific low micromolar NADPH oxidase inhibitor
VAS3947
-
i.e. 3-benzyl-7-(2-oxazolyl)thio-1,2,3-triazolo[4,5-d]pyrimidine, specific low micromolar NADPH oxidase inhibitor
additional information
-
metronidazole has no measurable inhibitory effect on the NADPH oxidase activity of RdxA
-
additional information
-
unidentified inhibitor found in 3000 g particulate fraction from patients with Grave's disease
-
additional information
-
epicatechin is a superoxide anion scavenger, but not inhibitory to NAD(P)H oxidase. HUVEC cells are able to convert (-)-epicatechin to its inhibitory O-methyl esters. IC50-values of (-)epicatechin and (+)catechin are above 0.1 mM in cell lysates
-
additional information
-
presence of Candida albicans inhibits by contrasting the assembly of the enzyme on dedritic cell's plasma membrane
-
additional information
-
trimer hydroxylated quinone is the major active compound in AOP-1, with strong inhibitory activity against vascular endothelial cell NADPH oxidase with an IC50 of 0.000031 mM at 22°C, pH not specified in the publication
-
additional information
-
Francisella tularensis inhibits NADPH oxidase activity in a cell-free assay; the regulatory factor fevR is essential for NADPH oxidase inhibition, whereas iglI and iglJ, candidate secretion system effectors, and the acid phosphatase acpA are not
-
additional information
-
V204A mutant is a competitive inhibitor of wild-type p67phox
-
additional information
-
knockout of adenosine A2A receptor significantly decreases NADPH-dependent superoxide anion production in mouse hearts compared to age-matched wild-type controls, accompanied by a significant decrease in catalytic subunit Nox2 protein expression, and down-regulation of ERK1/2, p38MAPK, and JNK phosphorylation. In wild-type mice, intraperitoneal injection of the selective adenosine A2A receptor antagonist SCH58261 inhibits phosphorylation of regulatory subunit p47phox, which is accompanied by a down-regulated cardiac reactive oxygen species production, and decreased JNK and ERK1/2 activation
-
additional information
-
K+ depletion increases superoxide levels, phosphorylation of c-Jun, expression of c-Src, and tyrosine phosphorylation of ROMK channel in renal cortex and outer medulla in wild-type mice. Low K+ intake decreases mean product of channel number and open probability of ROMK channels. In mice lacking the NAD(P)H oxidase subunit gp91phox, the effects of low K intake are significantly attenuated
-
additional information
-
treatment of animals by oral administration of isoobtusilactone A for two weeks does not result in significant difference between control animals and treated animals with respect to the body weight gain, the body weight ratio of liver, spleen and kidney, haematological and clinical chemistry parameters
-
additional information
-
trimer hydroxylated quinone is the major active compound in AOP-1, with strong inhibitory activity against vascular endothelial cell NADPH oxidase with an IC50 of 0.000031 mM at 22°C, pH not specified in the publication
-
additional information
-
mGluR5 activation inhibits microglial NADPH oxidase activity
-
additional information
-
inhibition by addition of hexokinase and glucose to remove ATP
-
additional information
-
non-iodinated lipid aldehydes inhibit depending on their chain length, maximum inhibition with dodecanal and tridecanal, no inhibition with octanal
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11alpha,9alpha-epoxymethanoprostaglandin F 2alpha
-
induces the expression of subunits p22phox and gp91phox
2,4,6-trinitrophenyl-bovine serum albumin
-
induces reactive oxygen species generation, which occurrs immediately. 2,4,6-Trinitrophenyl-bovine serum albumin but not TG causes extracellular release of superoxide anion/hydrogen peroxide, which is blocked by diphenyleneiodonium, apocynin, and wortmannin. When used together, 2,4,6-trinitrophenyl-bovine serum albumin and thapsigargin evoke the release of leukotriene C4, tumor necrosis factor-alpha, and interleukin-13 as well as reactive oxygen species generation synergistically
-
5-cyclopropyl-2-[1-(2-fluoro-benzyl)-1H-pyrazolo[3,4-b] pyridin-3-yl]-pyrimidin-4-ylamine
-
i.e. BAY 41-2272. THP-1 cells treated with BAY 41-2272 for 48 h significantly increase the superoxide anion release. BAY 41-2272 increases subunit gp91phox gene expression and causes a significant increase in cGMP and cAMP levels
A23187
-
calcium ionophore. HaCaT keratinocytes overexpressing calcium- and arachidonic acid binding proteins S100A8/S100A9 showed enhanced, transient reactive oxygen species generation in response to A23187, as well as nuclear factor kappaB activation and increase in interleukin-8 mRNA levels
apigenin
-
apigenin reduces cell viability, and induces apoptotic cell death in a dose-dependent manner. In addition, it evokes a dose-related elevation of intracellular reactive oxygen species level. Treatment with various inhibitors of the NADPH oxidase significantly blunts both the generation of reactive oxygen species and induction of apoptosis induced by apigenin
arachidonic acid
-
maximal enzyme activity in the presence of 0.25-0.35 mM, inhibition above
betaPix
-
a Rac1 guanine nucleotide exchange factor, appears to be constitutively bound to Nox1 and essential for its activity
-
bovine serum albumin
-
time-dependent increases in NAD(P)H oxidase activity with bovine serum albumin stimulation that is inhibited in a concentration-dependent manner with the HMG-CoA reductase inhibitor rosuvastatin, or with Rac1 inhibitor NSC23766. Following albumin stimulation, Rac1 translocates to plasma membrane for NAD(P)H oxidase activation
-
calyculin
isoform RbohD is directly phosphorylated in vivo. Phophorylation is enhanced in presence of protein phosphatase inhibitor calyculin. Calyculin itself induces reactive oxygen species production and dramatically enhances the ionomycin-induced reactive oxygen species production of isoform RbohD
cytochalasin D
-
enhancement of basal and hyperoxia-induced reactive oxygen species formation
doxorubicin
-
induction of superoxide production by doxorubicin is much higher in hearts of wild-type mice than in subunit gp91phox knock-out mice
glucose
-
oxidative stress and expression of the NADPH oxidase subunit, p22phox, are both increased, superoxide dismutase 1 and 3 expression lowered and endothelial nitric oxide synthase significantly elevated in microvessel endothelial cells treated with 40mM glucose for 72 h compared to low glucose medium. Oxidative stress, p22phox mRNA, endothelial nitric oxide synthase mRNA, and protein are lowered by concurrent incubation with sepiapterin
H2O2
-
Nox5 can be upregulated and activated by minute concentrations of hydrogen peroxide
heat shock protein 90
-
binding of heat shock protein 90 to the C-terminus of Nox5 appears to stabilize the protein and enhance expression and activity
-
HIV regulatory protein Tat
-
NADPH oxidase mediates Tat-induced superoxide release in microglia and macrophages
-
isoobtusilactone A
-
isoobtusilactone A elicits a concentration-dependent growth impediment with IC50 value of 37.5 microM. Treated cells also display transient increase of reactive oxygen species during the earlier stage of the experiment, followed by the disruption of mitochondrial transmembrane potential. The presence of a reactive oxygen species scavenger N-acetyl-L-cysteine and the inhibitor of NADPH oxidase diphenyleneiodonium chloride block reactive oxygen species production and the subsequent apoptotic cell death
latrunculin A
-
enhancement of basal and hyperoxia-induced reactive oxygen species formation
lipopolysaccharide
-
exposure tolipopolysaccharide leads to the demise of motor neurons in a dose- and time-dependent manner, whereas interneurons are impaired relatively mildly. NADPH oxidase is activated upon lipopolysaccharide challenge, and inhibitor apocynin prevents inflammation-mediated toxicity to motor neurons
NaCl
-
salt stress results in activiation of plasma membrane NAD(P)H oxidase. NaCl-induced increase in total Ca2+ is partially abolished by the addition of NAD(P)H oxidase inhibitor diphenyleneiodinium
nitroglycerin
-
in vascular smooth muscle cells exposed to nitroglycerin for 6-24 h, NAD(P)H oxidase activity is increased, in spite of isoform nox1 downregulation
p67phox
-
activation domain of p67phox triggers FAD reduction by Nox2. P40phox appears to increase oxidase activity in cooperation with p47phox not by inducing translocation to the membrane, but by retaining the oxidase at the phagosome
-
paraquat
-
paraquat-induced reactive oxygen species production including superoxide anions in BV-2 cells is accompanied by translocation of the p67phox cytosolic subunit of NADPH oxidase to the membrane. Paraquat-induced reactive oxygen species production is inhibited by NADPH oxidase inhibitors, apocynin and diphenylene iodonium. Apocynin and diphenylene iodonium also rescue cells from paraquat-induced toxicity. The inhibitors for protein kinase C delta or extracellular signal-regulated kinases ERK1/2 can partially attenuate paraquat-induced reactive oxygen species production and cell death
phosphatidylinositol 3-phosphate
-
subunit p40phox phosphatidylinositol 3-phosphate binding PX domain has phosphatidylinositol 3-phosphate-dependent and -independent functions. Translocation of subunit p67phox requires the PX domain but not 3-phosphoinositide binding. Activation of the oxidase by p40phox, however, requires both phosphatidylinositol 3-phosphate binding and an Src homology 3 domain competent to bind to poly-Pro ligands
platelet-derived growth factor
-
increases H2O2 production in NIH-3T3 fibroblasts through NADPH oxidase activation mediated by Gi-protein coupled receptors and c-Src kinase
-
Poldip2
-
reactive oxygen species production is enhanced by the multifunctional Poldip2, which also interacts with p22phox, presumably at the beginning of the cytosolic C-terminus, upstream of the region dispensable for Nox4 activity
-
Rac guanine nucleotide exchange factors
-
activate in conjunction with ATP and nucleoside diphosphate kinase
-
Rac1
-
in addition to cytosolic organizers and activators, Nox1 also requires Rac1 for activity. Rac1 interacts directly with the C-terminus of Nox1, even in the absence of Noxa1. Nox1 is stimulated by constitutively active Rac1 and inhibited by Rac1 knockdown. Rac1 provides a crucial mechanism for activation by agonists, particularly in cells that exclusively express Nox1/Noxo1/Noxal. Rac1 does not activate Nox4 in transfected cells. Rac1 may participate in Nox5 activation
-
salbutamol
-
salbutamol treatment enhances superoxide anion production in asthma patients through nitric oxide-mediated mechanisms. It exerts beneficial antioxidant effects through activation of catalase and attenuation of lipid peroxidation
sphingosine 1-phosphate
-
increases H2O2 production in NIH-3T3 fibroblasts through NADPH oxidase activation mediated by Gi-protein coupled receptors and c-Src kinase
SRC2 protein
-
enhances the reactive oxygen species-producing activity of NADPH oxidase RbohF
-
thapsigargin
-
evokes a robust burst of intracellular reactive oxygen specie, which occurrs with a significant lag tim. When used together, 2,4,6-trinitrophenyl-bovine serum albumin and thapsigargin evoke the release of leukotriene C4, tumor necrosis factor-alpha, and interleukin-13 as well as reactive oxygen species generation synergistically
transforming growth factor-beta
-
up-regulates isoform nox4 and increases the levels of Rac1 protein, a known regulator of both isoforms Nox1 and Nox2, in a transforming growth factor-beta receptor I-dependent manner and mediates activation of the nuclear factor-kappaB pathway. The inhibitors diphenyleneiodonium and apocynin, and SB431542, an inhibitor of the transforming growth factor-beta receptor I, block up-regulation of epidermal growth factor receptor ligands and Akt activation
-
tumor necrosis factor
-
treatment of fibroblasts induces the formation of a signaling complex containing TNF-R1-associated death domain protein TRADD, receptor interacting protein RIP1, NAD(P)H oxidase Nox1, and the small GTPase Rac1. Formation of this complex plays a key role in tumor necrosis factor-induced necrotic cell death
-
tumor necrosis factor-alpha
-
treatment of monocytic cells and isolated monocytes results in up-regulation of the NAD(P)H oxidase gene, neutrophil cytosolic factor 2. Treated cells have increased levels of mRNA and up-regulated expression of NADPH oxidase subunits p47phox, p67phox, and gp91phox, as well as increased oxidase activity. Pharmacological inhibitors of NF-kappaB activation block tumor necrosis factor-induced up-regulation, which correlates with a reduction in expression of the corresponding oxidase proteins and decreased superoxide anion production
-
Urea
-
increase of activity by 250% in presence of 1 M urea with no apparent perturbation in enzyme structure. Presence of urea prohibits the closing of the active site thus allowing the substrate to bind
(+)-(S)-2-(6-methoxynaphthalen-2-yl)propanoic acid
-
i.e. naproxen, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
(+)-(S)-2-(6-methoxynaphthalen-2-yl)propanoic acid
-
i.e. naproxen, nonsteroidal anti-inflammatory drug. Marked increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
2-(2-(2,6-dichlorophenylamino)-phenyl)acetic acid
-
i.e. diclofenac, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
2-(2-(2,6-dichlorophenylamino)-phenyl)acetic acid
-
i.e. diclofenac, nonsteroidal anti-inflammatory drug. Marked increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
4-(4-methylsulfonylphenyl)-3-phenyl-5H-furan-2-one
-
i.e. rofecoxib, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
4-(4-methylsulfonylphenyl)-3-phenyl-5H-furan-2-one
-
i.e. rofecoxib, nonsteroidal anti-inflammatory drug. Moderate increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
4-[5-(4-methylphenyl)-3-(trifluoromethyl)pyrazol-1-yl]benzenesulfonamide
-
i.e. celecoxib, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
4-[5-(4-methylphenyl)-3-(trifluoromethyl)pyrazol-1-yl]benzenesulfonamide
-
i.e. celecoxib, nonsteroidal anti-inflammatory drug. Moderate increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
angiotensin II
-
potent stimulator of NAD(P)H oxidase O2- production in the vasculature
angiotensin II
-
potent stimulator of NAD(P)H oxidase O2- production in the vasculature
angiotensin II
-
potent stimulator of NAD(P)H oxidase O2- production in the vasculature
angiotensin II
-
potent stimulator of NAD(P)H oxidase O2- production in the vasculature
formyl-Met-Leu-Phe
-
stimulation. In addition, heterologous expression of subunit p40phox markedly enhances superoxide production in stimulated cells. Upon stimulation with phorbol 12-myristate 13-acetate or formyl-Met-Leu-Phe, p40phox translocates to plasma membrane in a p67phox- and p47phox-dependent manner
ionomycin
reactive oxygen species production by isoform RbohD is induced in presence of ionomycin. Ionomycin induces calcium influx into the cell, and following Ca2+ binding to the EF-hand motif of RbohD, conformational changes result in activation
N-formyl-L-methionyl-L-leucyl-L-phenylalanine
-
store-operated Ca2+ entry is required at the beginning of NADPH oxidase activation in response to N-formyl-L-methionyl-L-leucyl-L-phenylalanine in neutrophil-like HL-60 cells. When extracellular Ca2+ is initially removed, early addition of Ca2+ after stimulation causes a complete restoration of Ca2+ entry and H2O2production. Both Ca2+ entry and H2O2 production are decreased by purported SOCE blockers, 2-aminoethoxydiphenyl borane (2-APB) and SK&F 96365. Ca2+ influx in HL-60 cells relies on different membrane transient receptor potential canonical channels and Orai1 for allowing NADPH oxidase activation
N-formyl-L-methionyl-L-leucyl-L-phenylalanine
-
stimulation. Conditional expression of p21-activated kinase-1 PAK1 dominant-positive mutants enhances, whereas dominant-negative mutants inhibit, NADPH oxidase-mediated superoxide generation stimulated by N-formyl-L-methionyl-L-leucyl-L-phenylalanine. Both Rac1 and the GTP exchange factor VAV1 are required as upstream signaling proteins, and the effect of p21-activated kinase-1 PAK1 on the respiratory burst is mediated through phosphorylation of subunit p47phox
NOXA1
-
in contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Noxa1 contains four Rac-binding TPR motifs, a Nox activation domain and an SH3 domain that interacts with the prolinerich region of an organizer subunit, But the p40phox-binding PB1 domain is not well conserved and the SH3 domain in the middle of the molecule is missing. Phosphorylation of Noxa1 by protein kinase A favors binding to 14-3-3 and dissociation from Nox1, whereas other kinases appear to decrease Noxa1 affinity for Rac1 and Nox1. In contrast, phosphorylation of Noxa1 by Src on tyrosine 110 increases Nox1 activity
-
NOXA1
i.e. NOX activator 1 activates, the protein is expressed predominantly in colon elithelium and is thus likely to be a physiologically relevant partner of NOX1
-
NOXO1
-
In contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Unlike p47phox, because Noxo1 lacks an autoinhibitory domain, it is thought to constitutively bind the cytochrome, but similar to p47phox, Noxo1 facilitates oxidase assembly by binding both an activator subunit and p22phox. The proline-rich region of Noxo1 binds to an SH3 domain of the activator, whereas the tandem SH3 domains of Noxo1 bind to the proline-rich region of p22phox. Noxo1 also binds to the dehydrogenase domain of Nox1. The PX domain of Noxo1 provides an essential affinity for membrane phosphoinositides
-
NOXO1
i.e. NOX organizer 1 activates, the protein is expressed predominantly in colon elithelium and is thus likely to be a physiologically relevant partner of NOX1
-
phorbol 12-myristate 13-acetate
-
after transfection with calcium- and arachidonic acid binding proteins S100A8/S100A9 genes, HeLa cells show dramatically increased activation of NAD(P)H oxidase in presence of phorbol 12-myristate 13-acetate
phorbol 12-myristate 13-acetate
-
stimualtion. Treated dendritic cells are are more competent in killing Candida albicans
phorbol 12-myristate 13-acetate
-
stimulation. In addition, heterologous expression of subunit p40phox markedly enhances superoxide production in stimulated cells. Upon stimulation with phorbol 12-myristate 13-acetate or formyl-Met-Leu-Phe, p40phox translocates to plasma membrane in a p67phox- and p47phox-dependent manner
phorbol 12-myristate 13-acetate
-
upon treatment, plasma membranes from stimulated cells show an increased amount of regulatory protein Rac1, but other components of the NAD(P)H oxidase complex do not change before and after the stimulation. When the constitutively active form of Rac, Q61L or GTP-bound Rac1 is added exogenously to the membrane, superoxied anion producing activity is enhanced up to 1.5-fold above the basal level,but GDP-loaded Rac1 does not affect superoxide generating kinetics
phorbol 12-myristate 13-acetate
-
stimulation. Conditional expression of p21-activated kinase-1 PAK1 dominant-positive mutants enhances, whereas dominant-negative mutants inhibit, NADPH oxidase-mediated superoxide generation stimulated by N-formyl-L-methionyl-L-leucyl-L-phenylalanine
Rac
-
small GTPase Rac plays a positive role in isoform Nox3 activation in the presence of subunit p47phox and either subunits p67phox or Noxa1, whereas Rac fails to upregulate Nox3 activity when p47phox is replaced with Noxo1. Expression of constitutively active Rac1 mutant Q61L enhances not only superoxide production but also membrane translocation of p67phox
-
Rac
-
for the activation of Nox enzymes, cytosolic regulatory components (Rac, p67phox, p47phox, and p40phox) are recruited into the integral membrane protein flavocytochrome b558, consisting of the catalytic subunits gp91phox and p22phox
-
thrombin
-
administration of thrombin to endothelial cells leads to upregulation of enzyme subunit p22phox accompanied by a delayed increase in generation of reactive oxygen species and enhanced proliferation. Existence of a positive feedback mechanism, whereby reactive oxygen species lead to elevated levels of p22phox and thus, sustained generation of reactive oxygen species as is observed in endothelial dysfunction
-
thrombin
-
after addition to cell culture, expression of NADPH oxidase subunits p47phox and p67phox occurs, accompanied by up-regulation in the expression of cytosolic enzyme components Rac 1 and p67phox, and the translocation of cytosolic subunits p47phox and p67phox to the membrane. Thrombin-induced reactive oxygen species production, protein oxidation, and loss of cultured hippocampal neurons are partially attenuated by NADPH oxidase inhibition and/or by several antioxidants
-
TNF-alpha
-
activation of enzyme, resulting in an increase in intracellular H2O2 that stimulates Ca2+ sparks and transient Kca currents, leading to a reduction in global concentration of Ca2+ and vasodilation
-
additional information
-
upregulated by agents activationg cAMP pathway
-
additional information
-
presence of Candida albicans does not activate NADPH oxidase in dendritic cells
-
additional information
-
NADPH oxidase can be activated in a cell-free system by mixing cytosol and plasma membranes isolated from resting neutrophils or macrophages in the presence of Mg2+, GTP and an anionic amphiphile such as arachidonic acid or sodium dodecyl sulfate
-
additional information
-
activation of NADPH oxidase in phagocytes can be induced by a large number of inflammatory stimuli such as opsonized bacteria, opsonized zymosan, bacterial formylated peptides such as formyl-Met-Leu-Phe, C5a and platelet-activating factor, and also by pharmacological agents such as calcium ionophores A23127, ionomycin and PKC activators such as phorbol myristate acetate. In intact cells, NADPH oxidase activation is accompanied by phosphorylation of enzyme components p47phox, p67phox, p40phox, p22phox and gp91phox, along with several protein-protein interactions. In human neutrophils, various protein kinases have been implicated in the activation of NADPH oxidase, among which the PKC and MAP kinase families appear to play a major role
-
additional information
-
agonists appear to stimulate Nox1 in specific locations, thus determining where superoxide is produced: extracellularly by muscarinic agonists and thrombin, in endosomes by IL-1beta and TNF-alpha, both inside and outside cells by angiotensin II. Nox activators comprise p67phox and the structurally similar Noxa1. In colon the cytosolic subunits p47phox and p67phox are not expressed and are replaced by Noxo1 and Noxa1. Besides p47phox, other possible organizers include Tks4 and Tks5, two Src substrates with a PX domain and multiple SH3 domains capable of binding p22phox and Noxa1, but not p67phox. Cdc42 cannot activate Nox1
-
additional information
-
superoxide production is induced by addition of NADPH cytochrome P450 reductase
-
additional information
-
when luminal NaCl in kidney is switched from 10 to 80 mM, a situation of initiating maximum tubuloglomerular feedback response, superoxide anion production significantly increases. In the presence of apocynin, superoxide anion production is inhibited by 80%
-
additional information
-
treatment of animals by oral administration of isoobtusilactone A for two weeks does not result in significant difference between control animals and treated animals with respect to the body weight gain, the body weight ratio of liver, spleen and kidney, haematological and clinical chemistry parameters
-
additional information
-
depolarization of membrane potential of endothelial cells leads to activation of NAD(P)H oxidase and, consequently, superoxide anion production
-
additional information
-
StCDPK4 and StCDPK5 phosphorylate and activate the plasma membrane NADPH oxidase
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
NADPH
-
subunit p40phox-depleted cytosol in the absencee of recombinant wild-type p40phox, pH 7.3, 37°C
0.024
NADPH
-
subunit p40phox-depleted cytosol in the presence of recombinant wild-type p40phox, pH 7.3, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000301
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundec-3-yn-1-yl]octahydro-2,2'-bifuran-5-yl]dodec-4-yn-1-ol
-
-
0.0000123
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]dodecan-1-ol
-
-
0.0000388
(1R,1'R)-1,1'-((2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyl)-bis-(6-(4-n-butylphenoxy)hex-3-yn-1-ol)
-
-
0.0000196
(1R,1'R)-1,1'-((2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyl)-bis-(6-(4-n-butylphenoxy)hexan-1-ol)
-
-
0.03
1-(2-chlorobenzyl)-4-methyl-5-[3-(2-oxopyrrolidin-1-yl)propyl]-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C
0.03
1-(4-fluorobenzyl)-5-[2-(1H-indol-3-yl)ethyl]-4-methyl-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C
0.00024
1-acetyl-2-(2-chlorophenyl)-4-methyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000398
1-acetyl-4-methyl-2-(2-methylphenyl)-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000409
1-acetyl-4-methyl-2-phenyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000285
1-[(3-methoxyphenyl)acetyl]-4-methyl-2-phenyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.002175
2,4,5-trimethyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000387
2,4-dimethyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.03
2-(1,3-benzothiazol-2-yl)-1-(2-chlorobenzyl)-4-methyl-5-(morpholin-4-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C
0.03
2-(1,3-benzothiazol-2-yl)-4-methyl-1-(pyridin-2-ylmethyl)-5-(tetrahydrofuran-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C
0.001208
2-(1,3-benzothiazol-2-yl)-4-methyl-5-(morpholin-4-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.004729
2-(1,3-benzothiazol-2-yl)-5-[2-(1H-imidazol-4-yl)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.001845
2-(1,3-benzothiazol-2-yl)-5-[2-(1H-indol-3-yl)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000218
2-(2,5-dichlorobenzyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000342
2-(2-chloro-4-fluorobenzyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000213
2-(2-chloro-4-fluorophenyl)-4,5-dimethyl-1H-pyrazolo[4,3-c]-pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000235
2-(2-chloro-4-fluorophenyl)-4-methyl-5-(pyridin-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000114
2-(2-chloro-4-fluorophenyl)-5-(2-pyridin-2-ylethyl)-4-(pyrrolidin-1-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000215
2-(2-chlorophenyl)-4,5-dimethyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000128
2-(2-chlorophenyl)-4-(2-fluorophenyl)-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000172
2-(2-chlorophenyl)-4-([methyl(phenyl)amino]methyl)-5-[2-(pyridin-2-yl)ethyl]-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000158
2-(2-chlorophenyl)-4-methyl-5-(3-phenylprop-2-yn-1-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000515
2-(2-chlorophenyl)-4-methyl-5-(4-[(4-methylpiperazin-1-yl)methyl]benzyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000165
2-(2-chlorophenyl)-4-methyl-5-(pyridin-2-ylmethyl)-1H-pyrazolo-[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000236
2-(2-chlorophenyl)-4-methyl-5-[(6-morpholin-4-ylpyridin-2-yl)-methyl]-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000428
2-(2-chlorophenyl)-4-methyl-5-[4-(4-methylpiperazin-1-yl)-4-oxobutyl]-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000114
2-(2-chlorophenyl)-4-[(4-fluorophenoxy)methyl]-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000065
2-(2-chlorophenyl)-4-[[4-(3-methoxyphenyl)piperazin-1-yl]-methyl]-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000151
2-(2-chlorophenyl)-4-[[methyl(phenyl)amino]methyl]-5-(pyridin-4-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.03
2-(2-chlorophenyl)-5-(3-ethoxypropyl)-4-methyl-1-(pyridin-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C
0.000565
2-(2-chlorophenyl)-5-(3-hydroxypropyl)-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.00052
2-(2-chlorophenyl)-5-(cyclohexylmethyl)-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000047
2-(2-chlorophenyl)-5-[(1-methyl-1H-pyrazol-3-yl)methyl]-4-[[methyl(pyridin-3-ylmethyl)amino]methyl]-1H-pyrazolo[4,3-c]-pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000235
2-(2-chlorophenyl)-5-[2-(dimethylamino)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000308
2-(2-fluorophenyl)-4,5-dimethyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000313
2-(2-methoxyethyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.00034
2-(3-chlorophenyl)-4,5-dimethyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000259
2-(4-chlorobenzyl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.03
2-(4H-3,1-benzothiazin-2-yl)-1-benzyl-4-methyl-5-(tetrahydrofuran-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C
0.000458
2-(7-chloroquinolin-4-yl)-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000463
2-benzyl-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000326
2-[2-(4-chlorophenoxy)ethyl]-4-methyl-3-methylidene-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.00306
2-[4-(benzyloxy)phenyl]-4,5-dimethyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000293
3-(4,5-dimethyl-3,6-dioxo-1,3,5,6-tetrahydro-2H-pyrazolo[4,3-c]pyridin-2-yl)benzonitrile
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.001947
4,5-dimethyl-2-(4-phenyl-1,3-thiazol-2-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.001418
4,5-dimethyl-2-(5-[(4-methylpiperazin-1-yl)sulfonyl]pyridin-2-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000173
4-methyl-2-(2-methylphenyl)-5-(pyridine-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.005232
4-methyl-2-phenyl-5-(2-phenylethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000373
4-methyl-2-phenyl-5-(pyridin-3-ylmethyl)-1H-pyrazolo[4,3-c]-pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000334
4-methyl-3-methylidene-2-(2-phenylethyl)-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000445
4-methyl-3-methylidene-2-[2-(morpholin-4-yl)ethyl]-5-(pyridin-2-ylmethyl)-1,2,3,5-tetrahydro-6H-pyrazolo[4,3-c]pyridin-6-one
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.03
4-methyl-5-(3-phenoxybenzyl)-2-([1,2,4]triazolo[4,3-b]pyridazin-6-yl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C
0.000153
4-[(4-fluorophenoxy)methyl]-5-(2-methoxyethyl)-2-(2-morpholin-4-ylethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000095
4-[(benzyloxy)methyl]-2-(2-chlorophenyl)-5-(pyrazin-2-ylmethyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000082
4-[[(2-chlorobenzyl)oxy]methyl]-2-(2-chlorophenyl)-5-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.004222
4-[[2-(1,3-benzothiazol-2-yl)-4-methyl-3,6-dioxo-1,2,3,6-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl]methyl]benzoic acid
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000259
4-[[2-(2-chlorophenyl)-4-methyl-3,6-dioxo-1,2,3,6-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl]methyl]benzenesulfonamide
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000165
4-[[benzyl(methyl)amino]methyl]-2-(2-chloro-4-fluorophenyl)-5-(3-methoxypropyl)-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.00544
5-(1,3-benzodioxol-5-ylmethyl)-4-methyl-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.00949
5-(furan-2-ylmethyl)-4-methyl-2-phenyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000878
5-benzyl-2-(4-fluorophenyl)-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000218
N-[2-(2-chlorophenyl)-4-methyl-3,6-dioxo-1,2,3,6-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl]-2-(4-fluorophenoxy)acetamide
-
0.1 M phosphate buffer, pH 7.4, 37°C
0.000328
N-[3-(4,5-dimethyl-3,6-dioxo-1,3,5,6-tetrahydro-2H-pyrazolo[4,3-c]pyridin-2-yl)phenyl]acetamide
-
0.1 M phosphate buffer, pH 7.4, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00113
(3Z)-3-(3,4-dihydroxybenzylidene)-5-nitro-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00063
(3Z)-3-[4-hydroxy-3,5-di(propan-2-yl)benzylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00017
2,3,8,9-tetrahydroxy-5-(2-hydroxy-5-nitrobenzyl)phenanthridin-6(5H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
2,3,8,9-tetrahydroxy-5-(3-nitrobenzyl)phenanthridin-6(5H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00158
2,3,8,9-tetrahydroxy-5-(4-nitrobenzyl)phenanthridin-6(5H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00158
2,3,8,9-tetrahydroxy-5-[2-(phenylsulfonyl)benzyl]phenanthridin-6(5H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00074
2-(3,4-dihydroxyphenyl)-3,7-dihydroxy-6-methoxy-4H-chromen-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00085
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00102
2-(3,4-dihydroxyphenyl)-5-hydroxy-3,7-dimethoxy-4H-chromen-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00096
2-hydroxy-5-[(2-hydroxybenzyl)amino]benzoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00059
2-[(2,3,8,9-tetrahydroxy-6-oxophenanthridin-5(6H)-yl)methyl]benzonitrile
Homo sapiens
-
pH and temperature not specified in the publication
0.00102
2-[(2E)-2-(3,4-dihydroxybenzylidene)hydrazinyl]-N-(3-nitrophenyl)-2-oxoacetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00068
3,5,7-trihydroxy-2-(4-hydroxy-3-methylphenyl)-4H-chromen-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00079
3-(3,4-dihydroxycyclohexa-2,4-dien-1-yl)-2,7-dihydroxy-4H-chromen-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00113
5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00134
5-[(2,5-dihydroxybenzyl)amino]-2-hydroxybenzoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.004
ISNSESGPRGVHFIFNKENF
Homo sapiens
-
pH and temperature not specified in the publication
0.00127
methyl 2-hydroxy-5-[(2-hydroxybenzyl)amino]benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.00091
N'1,N'2-bis[(E)-(2,3-dihydroxyphenyl)methylidene]ethanedihydrazide
Homo sapiens
-
pH and temperature not specified in the publication
0.00116
N'1,N'2-bis[(E)-(3,4-dihydroxyphenyl)methylidene]ethanedihydrazide
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
N-(3-aminophenyl)-N'-[1-(4-hydroxy-3-methoxyphenyl)ethyl]ethanediamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
N-[(3Z)-3-(4-hydroxy-3-methoxybenzylidene)-2-oxo-2,3-dihydro-1H-indol-5-yl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00164
N-[1-(3,4-dihydroxyphenyl)ethyl]-N'-(3-nitrophenyl)ethanediamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00024
N4-(3-aminophenyl)[1]benzothieno[3,2-d]pyrimidine-4,8-diamine
Homo sapiens
-
pH and temperature not specified in the publication
0.00107
N4-(4-aminophenyl)[1]benzothieno[3,2-d]pyrimidine-4,8-diamine
Homo sapiens
-
pH and temperature not specified in the publication
0.00083
quercetin 3-O-alpha-D-glucopyranoside
Homo sapiens
-
pH and temperature not specified in the publication
0.034
VWYYRVYDIPPKFFYTRKLL
Homo sapiens
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.16
purified recombinant enzyme, with NADPH in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, pH 7.0, 30°C
0.38
purified recombinant enzyme, with NADH in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, pH 7.0, 30°C
additional information
-
voltage-clamp experiments, enzyme activity depends on both membrane potential and concentration of NADPH, the shape of the Ie-V curve is influenced by the concentration of NADPH in the submillimolar range
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the partially purified ReADH shows a preference for an alkaline pH range for the oxidation of (RS)-1-phenylethanol in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, the highest activity occurs at pH 12.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80 - 95
-
80°C: about 45% of maximal activity, 95°C: about 45% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
