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Information on EC 1.6.3.1 - NAD(P)H oxidase (H2O2-forming) and Organism(s) Sus scrofa and UniProt Accession Q8HZK2
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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.
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Word Map
- 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
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nad(p)h oxidase, p47phox, gp91phox, nadph-oxidase, p67phox, duox2, duox1, nadph oxidase 4, phagocyte nadph oxidase, nadph oxidase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dual oxidase
-
-
-
-
Duox
-
-
-
-
large NOX
-
-
-
-
LNOX
-
-
-
-
NADPH oxidase
-
-
-
-
p138 thyroid-oxidase
-
-
-
-
p138tox
-
-
-
-
ThOX
-
-
-
-
ThOX2
-
-
-
-
thyroid NADPH oxidase
-
-
-
-
thyroid oxidase
-
-
-
-
thyroid oxidase 2
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
9032-22-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
-
-
?
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
-
production of hydrogen peroxide in thyroid gland that is required for thyroid hormone synthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
Cd2+
Zn2+
additional information
Ca2+
-
regulates enzyme activity
Ca2+
-
a Ca2+/NADPH-dependent H2O2 generating system is associated with isoform Duox2 protein expression
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
Phenylarsine oxide
-
partial inactivation and desensitization of activity to Ca2+, effect is completely reversed by addition of 2,3-dimercaptopropanol
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
porcine coronary artery endothelial cell, PCAEC. Exposure of cells to hypoxia for 2 h followed by 1 h of reoxygenation significantly increases reactive oxygen species formation. Pretreatment with the NADPH oxidase inhibitors, diphenyleneiodonium and apocynin , significantly attenuates hypoxia/reoxygenation-induced reactive oxygen species formation. Exposure of PCAECs to hypoxia/reoxygenation causes a significant increase in serine-threonine kinase Akt and ERK1/2 activation. Exposure of PCAEC spheroids to hypoxia/reoxygenation significantly increases endothelial spheroid sprouting, whereas pharmacological inhibition of NADPH oxidase or genetic deletion of the NADPH oxidase subunit, p47phox (p47phox/), significantly suppresses these changes
additional information
-
expression of isoform Duox2 in all tissues of the digestive tract examined. Enzyme is located at the apical membrane of the enterocytes in the brush border
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DUOX2_PIG
1545
6
175284
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CHAPS is the best detergent for solubilization of enzyme, preserves native properties of enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
exposure of porcine coronary artery endothelial cells, PCAECs, to hypoxia for 2 h followed by 1 h of reoxygenation significantly increases reactive oxygen species formation. Pretreatment with the NADPH oxidase inhibitors, diphenyleneiodonium and apocynin, significantly attenuates hypoxia/reoxygenation-induced reactive oxygen species formation. Exposure of PCAECs to hypoxia/reoxygenation causes a significant increase in serine-threonine kinase Akt and ERK1/2 activation. Exposure of PCAEC spheroids to hypoxia/reoxygenation significantly increases endothelial spheroid sprouting and vessel outgrowth, whereas pharmacological inhibition of NADPH oxidase or genetic deletion of the NADPH oxidase subunit p47phox significantly suppresses these changes
medicine
-
in brain capillary endothelial cells, hypoxia/reoxygenation induces translocation of the NAD(P)H oxidase activator Rac-1 to the membrane. Inhibition of Rac-1 prevents the ischemia/reperfusion-induced blood-brain barrier disruption. Activation of NAD(P)H oxidase promotes cerebral reactive oxygen species formation, which then leads to Rho kinase-mediated endothelial cell contraction and disruption of the blood-brain barrier
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Umeki, S.
Mechanisms for the activation/electron transfer of neutrophil NADPH-oxidase complex and molecular pathology of chronic granulomatous disease
Ann. Hematol.
68
267-277
1994
Bos taurus, Cavia porcellus, Homo sapiens, Sus scrofa
De Deken, X.; Wang, D.; Many, M.C.; Costagliola, S.; Libert, F.; Vassart, G.; Dumont, J.E.; Miot, F.
Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family
J. Biol. Chem.
275
23227-23233
2000
Canis lupus familiaris, Sus scrofa, Caenorhabditis elegans (O61213), Caenorhabditis elegans, Homo sapiens (Q9NRD8), Homo sapiens
Dupuy, C.; Ohayon, R.; Valent, A.; Noel-Hudson, M.S.; Deme, D.; Virion, A.
Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs
J. Biol. Chem.
274
37265-37269
1999
Caenorhabditis elegans (O61213), Sus scrofa (Q8HZK2), Sus scrofa, Homo sapiens (Q9NRD8), Homo sapiens
Leseney, A.M.; Deme, D.; Legue, O.; Ohayon, R.; Chanson, P.; Sales, J.P.; Pires de Carvalho, D.; Dupuy, C.; Virion, A.
Biochemical characterization of a Ca2+/NAD(P)H-dependent H2O2 generator in human thyroid tissue
Biochimie
81
373-380
1999
Homo sapiens, Sus scrofa
Dupuy, C.; Virion, A.; Ohayon, R.; Kaniewski, J.; Deme, D.; Pommier, J.
Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase in thyroid plasma membrane
J. Biol. Chem.
266
3739-3743
1991
Sus scrofa
Dupuy, C.; Virion, A.; Hammou, N.A.; Kaniewski, J.; Deme, D.; Pommier, J.
Solubilization and characteristics of the thyroid NADPH-dependent hydrogen peroxide generating system
Biochem. Biophys. Res. Commun.
141
839-846
1986
Sus scrofa
Nakamura, Y.; Ogihara, S.; Ohtaki, S.
Activation by ATP of calcium-dependent NADPH-oxidase generating hydrogen peroxide in thyroid plasma membranes
J. Biochem.
102
1121-1132
1987
Sus scrofa
Ohayon, R.; Boeynaems, J.M.; Braekman, J.C.; Van den Bergen, H.; Gorin, Y.; Virion, A.
Inhibition of thyroid NADPH-oxidase by 2-iodohexadecanal in a cell-free system
Mol. Cell. Endocrinol.
99
133-141
1994
Sus scrofa
Carvalho, D.P.; Dupuy, C.; Gorin, Y.; Legue, O.; Pommier, J.; Haye, B.; Virion, A.
The Ca2+- and reduced nicotinamide adenine dinucleotide phosphate-dependent hydrogen peroxide generating system is induced by thyrotropin in porcine thyroid cells
Endocrinology
137
1007-1012
1996
Sus scrofa
Gorin, Y.; Leseney, A.M.; Ohayon, R.; Dupuy, C.; Pommier, J.; Virion, A.; Deme, D.
Regulation of the thyroid NADPH-dependent H2O2 generator by Ca2+: studies with phenylarsine oxide in thyroid plasma membrane
Biochem. J.
321
383-388
1997
Sus scrofa
-
El Hassani, R.A.; Benfares, N.; Caillou, B.; Talbot, M.; Sabourin, J.; Belotte, V.; Morand, S.; Gnidehou, S.; Agnandji, D.; Ohayon, R.; Kaniewski, J.; Noel-Hudson, M.; Bidart, J.; Schlumberger, M.; Virion, A.; Dupuy, C.
Dual oxidase2 is expressed all along the digestive tract
Am. J. Physiol.
288
G933-G942
2005
Homo sapiens, Sus scrofa
Ameziane-El-Hassani, R.; Morand, S.; Boucher, J.L.; Frapart, Y.M.; Apostolou, D.; Agnandji, D.; Gnidehou, S.; Ohayon, R.; Noel-Hudson, M.S.; Francon, J.; Lalaoui, K.; Virion, A.; Dupuy, C.
Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity
J. Biol. Chem.
280
30046-30054
2005
Homo sapiens, Sus scrofa
Chen, J.X.; Zeng, H.; Tuo, Q.H.; Yu, H.; Meyrick, B.; Aschner, J.L.
NADPH oxidase modulates myocardial Akt, ERK1/2 activation, and angiogenesis after hypoxia-reoxygenation
Am. J. Physiol. Heart Circ. Physiol.
292
H1664-H1674
2007
Mus musculus, Sus scrofa
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