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Information on EC 1.6.3.1 - NAD(P)H oxidase (H2O2-forming) and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JGP4

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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.
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This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JGP4
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Word Map
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
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
dual oxidase
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-
-
-
Duox
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-
-
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large NOX
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-
-
-
LNOX
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-
-
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NADPH oxidase
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-
-
-
p138 thyroid-oxidase
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-
-
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p138tox
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-
-
-
ThOX
-
-
-
-
ThOX2
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-
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thyroid NADPH oxidase
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-
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thyroid oxidase
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-
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thyroid oxidase 2
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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-
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reduction
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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
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
activity with NADPH is much lower than with NADH
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-
?
NADPH + H+ + O2
NADP+ + H2O2
show the reaction diagram
activity with NADPH is much lower than with NADH
-
-
?
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
NADPH + H+ + O2
NADP+ + H2O2
show the reaction diagram
additional information
?
-
KOD1 (TkNOX) catalyzes oxidation of NADH and NADPH with oxygen from atmospheric air as an electron acceptor
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-
?
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
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
-
-
-
?
NADPH + H+ + O2
NADP+ + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
KOD1 (TkNOX) catalyzes oxidation of NADH and NADPH with oxygen from atmospheric air as an electron acceptor
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
preference to NADPH versus NADH as an electron donor during oxygen reduction
NADPH
preference to NADPH versus NADH as an electron donor during oxygen reduction
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not
CoA
NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.16
purified recombinant enzyme, with NADPH in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, pH 7.0, 30°C
0.38
purified recombinant enzyme, with NADH in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the partially purified ReADH shows a preference for an alkaline pH range for the oxidation of (RS)-1-phenylethanol in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, the highest activity occurs at pH 12.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
and above, activity range, profile overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
6 * 50000, SDS-PAGE
homodimer
homotetramer
4 * 49000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
the enzyme shows a 25% loss of activity after incubation at 65°C for 1 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL partially by heat treatment at 65°C for 15 min
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
gene tk0304, functional expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
usage of the enzyme for regeneration of both NADP+ and NAD+ in alcohol dehydrogenase-catalyzed enantioselective oxidation of racemic 1-phenylethanol. NADP+ regeneration at 30°C by TkNOX coupled with (R)-specific ADH from Lactobacillus kefir results in successful acquisition of optically pure (S)-1-phenylethanol, or at 45-60°C with moderately thermostable (S)-specific ADH from Rhodococcus erythropolis in optically pure (R)-1-phenylethanol, giving the possibility to operate the enantioselective bioconversion accompanying NAD+ regeneration at high temperatures, advantage of the combination of thermostable enzymes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, X.; Kobori, H.; Orita, I.; Zhang, C.; Imanaka, T.; Xing, X.H.; Fukui, T.
Application of a novel thermostable NAD(P)H oxidase from hyperthermophilic archaeon for the regeneration of both NAD+ and NADP+
Biotechnol. Bioeng.
109
53-62
2012
Thermococcus kodakarensis (Q5JFZ8)
Manually annotated by BRENDA team
Harnvoravongchai, P.; Kobori, H.; Orita, I.; Nakamura, S.; Imanaka, T.; Fukui, T.
Characterization and gene deletion analysis of four homologues of group 3 pyridine nucleotide disulfide oxidoreductases from Thermococcus kodakarensis
Extremophiles
18
603-616
2014
Thermococcus kodakarensis (Q5JFZ8), Thermococcus kodakarensis (Q5JGF8), Thermococcus kodakarensis (Q5JGP4), Thermococcus kodakarensis (Q5JHY2), Thermococcus kodakarensis (Q5JJB9), Thermococcus kodakarensis
Manually annotated by BRENDA team