Literature summary for 1.6.3.2 extracted from

Jia, B.; Lee, S.; Pham, B.P.; Cho, Y.S.; Yang, J.K.; Byeon, H.S.; Kim, J.C.; Cheong, G.W.
An archaeal NADH oxidase causes damage to both proteins and nucleic acids under oxidative stress (2010), Mol. Cells, 29, 363-371.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermococcus profundus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
50000	-	2 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE	Thermococcus profundus
50000	-	6 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE	Thermococcus profundus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 NADH + H+ + O2	Thermococcus profundus	reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2) to detoxify O2. Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability	NAD+ + 2 H2O	-	?
2 NADPH + 2 H+ + O2	Thermococcus profundus	reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2) to detoxify O2. Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability	2 NADP+ + 2 H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermococcus profundus	B2G3S1	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 NADH + H+ + O2	reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2) to detoxify O2. Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability	Thermococcus profundus	NAD+ + 2 H2O	-	?
2 NADH + H+ + O2	reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2). Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability	Thermococcus profundus	NAD+ + 2 H2O	-	?
2 NADPH + 2 H+ + O2	reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2) to detoxify O2. Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability	Thermococcus profundus	2 NADP+ + 2 H2O	-	?
2 NADPH + 2 H+ + O2	reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2). Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability	Thermococcus profundus	2 NADP+ + 2 H2O	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE	Thermococcus profundus
hexamer	6 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE	Thermococcus profundus

Synonyms

Synonyms	Comment	Organism
NOXtp	-	Thermococcus profundus

General Information

General Information	Comment	Organism
physiological function	NAD(P)H oxidase reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2) to detoxify O2. Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability	Thermococcus profundus

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Release 2023.1 (January 2023)