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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.3.2 expression in Escherichia coli Thermococcus profundus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.3.2 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
1.6.3.2 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.3.2 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
-
 ?
1.6.3.2 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

EC Number Organism UniProt Comment Textmining
1.6.3.2 Thermococcus profundus B2G3S1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.3.2 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
-
 ?
1.6.3.2 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
-
 ?
1.6.3.2 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
-
 ?
1.6.3.2 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

EC Number Subunits Comment Organism
1.6.3.2 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
1.6.3.2 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

EC Number Synonyms Comment Organism
1.6.3.2 NOXtp
-
 Thermococcus profundus

General Information

EC Number General Information Comment Organism
1.6.3.2 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