Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.6.3.1 - NAD(P)H oxidase (H2O2-forming) and Organism(s) Caenorhabditis elegans and UniProt Accession O61213

for references in articles please use BRENDA:EC1.6.3.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Caenorhabditis elegans
UNIPROT: O61213
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BLI-3
-
the dual oxidase enzyme has a NADPH oxidase domain
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 hide
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 hide
9032-22-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
show the reaction diagram
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
-
-
-
-
?
NADPH + H+ + O2
NADP+ + H2O2
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD(P)H + H+ + O2
NAD(P)+ + H2O2
show the reaction diagram
-
-
-
?
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
-
-
-
-
?
NADPH + H+ + O2
NADP+ + H2O2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
high sequence similarities to mammalian proteins
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
a lesion in BLI-3's NADPH oxidase domain increases sensitivity to pathogen and diminishes lifespan
physiological function
-
the enzyme BLI-3 has roles in both cuticle development and in protection against infection with Enterococcus faecalis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DUOX1_CAEEL
1497
7
170416
Swiss-Prot
Secretory Pathway (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
van der Hoeven, R.; Cruz, M.R.; Chavez, V.; Garsin, D.A.
Localization of the dual oxidase BLI-3 and characterization of its NADPH oxidase domain during infection of Caenorhabditis elegans
PLoS ONE
10
e0124091
2015
Caenorhabditis elegans
Manually annotated by BRENDA team