Literature summary for 1.6.3.1 extracted from

Luxen, S.; Noack, D.; Frausto, M.; Davanture, S.; Torbett, B.E.; Knaus, U.G.
Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells (2009), J. Cell Sci., 122, 1238-1247.

Search for more literature for 1.6.3.1

Application

Application	Comment	Organism
medicine	inactivating mutations of Duox2 are linked to congenital hypothyroidism, and epigenetic silencing of Duox is frequently observed in lung cancer	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
medicine	epigenetic silencing of Duox is frequently observed in lung cancer	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9NRD8	-	-
Homo sapiens	Q9NRD9	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
lung epithelial cell	Duox1 and Duox2 localize distinctly in lung epithelial cells as well as in ex-vivo differentiated lung epithelia. The localization of functional Duox-DuoxA heterodimers seems to be controlled by the associated DuoxA subunit	Homo sapiens	-
lung epithelial cell	Duox1 and Duox2 localize distinctly in lung epithelial cells as well as in ex-vivo differentiated lung epithelia. The localization of functional Duox-DuoxA heterodimers seems to be controlled by the associated DuoxA subunit, including Duox2 expression in ciliated cells in an ex vivo differentiated lung epithelium	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	Duox proteins form functional heterodimers with their respective DuoxA subunits, in close analogy to the phagocyte NADPH oxidase. Characterization of novel DuoxA1 isoforms and mispaired Duox-DuoxA complexes reveals that heterodimerization is a prerequisite for reactive oxygen species production. Functional Duox1 and Duox2 localize to the leading edge of migrating cells, augmenting motility and wound healing. DuoxA subunits are responsible for targeting functional oxidases to distinct cellular compartments in lung epithelial cells	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Duox-DuoxA NADPH oxidase	-	Homo sapiens
Duox1	-	Homo sapiens
Duox2	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)