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Information on EC 1.6.3.2 - NAD(P)H oxidase (H2O-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
                1.6.3.2 NAD(P)H oxidase (H2O-forming)
IUBMB Comments
A flavoprotein (FAD). NADPH is a better substrate than NADH [1,3]. By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida.
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This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JGP4
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The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
2
+
+
=
2
+
2
Synonyms
noxtp, more
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:oxygen oxidoreductase (H2O-forming)
A flavoprotein (FAD). NADPH is a better substrate than NADH [1,3]. By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 NADH + 3 H+ + 2 O2
3 NAD+ + H2O
show the reaction diagram
approximately 75% H2O and 25% H2O is produced. Km value of the enzyme towards NADH and NADPH is almost the same whereas specific activity is higher with NADPH compared to NADH
-
-
?
3 NADPH + 3 H+ + 2 O2
3 NADP+ + H2O
show the reaction diagram
approximately 87% H2O and 13% H2O2 is produced. Km value of the enzyme towards NADH and NADPH is almost the same whereas specific activity is higher with NADPH compared to NADH
-
-
?
NADH + H+ + O2
NAD+ + H2O
show the reaction diagram
-
-
-
?
NADPH + H+ + O2
NADP+ + H2O
show the reaction diagram
the enzyme prefers NADPH over NADH
-
-
?
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+ + H2O
show the reaction diagram
-
-
-
?
NADPH + H+ + O2
NADP+ + H2O
show the reaction diagram
the enzyme prefers NADPH over NADH
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24
NADH
pH 7.8, 75°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
68
NADH
pH 7.8, 75°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
pH 7.5: about 70% of maximal activity, pH 8.5: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 80
70°C: about 60% of maximal activity, 80°C: about 70% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
300000
gel filtration
330000
gel filtration
48610
6 * 48610, sequence calculation
49375
6 * 49375, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homohexamer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
150 min, less than 5% loss of activity
120
secondary structure of the enzyme is not stable at this temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nisar, M.A.; Rashid, N.; Bashir, Q.; Gardner, Q.T.; Shafiq, M.H.; Akhtar, M.
TK1299, a highly thermostable NAD(P)H oxidase from Thermococcus kodakaraensis exhibiting higher enzymatic activity with NADPH
J. Biosci. Bioeng.
116
39-44
2013
Thermococcus kodakarensis (Q5JGP4)
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 (Q5JGP4)
Manually annotated by BRENDA team