BRENDA - Enzyme Database show
show all sequences of 1.6.3.2

TK1299, a highly thermostable NAD(P)H oxidase from Thermococcus kodakaraensis exhibiting higher enzymatic activity with NADPH

Nisar, M.A.; Rashid, N.; Bashir, Q.; Gardner, Q.T.; Shafiq, M.H.; Akhtar, M.; J. Biosci. Bioeng. 116, 39-44 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Thermococcus kodakarensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.24
-
NADH
pH 7.8, 75°C
Thermococcus kodakarensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
48610
-
6 * 48610, sequence calculation
Thermococcus kodakarensis
49375
-
6 * 49375, mass spectrometry
Thermococcus kodakarensis
300000
-
gel filtration
Thermococcus kodakarensis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermococcus kodakarensis
Q5JGP4
-
-
Purification (Commentary)
Commentary
Organism
-
Thermococcus kodakarensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3 NADH + 3 H+ + 2 O2
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
725576
Thermococcus kodakarensis
3 NAD+ + H2O
-
-
-
?
3 NADPH + 3 H+ + 2 O2
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
725576
Thermococcus kodakarensis
3 NADP+ + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
hexamer
6 * 48610, sequence calculation; 6 * 49375, mass spectrometry
Thermococcus kodakarensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
75
-
-
Thermococcus kodakarensis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
70
80
70°C: about 60% of maximal activity, 80°C: about 70% of maximal activity
Thermococcus kodakarensis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
150 min, less than 5% loss of activity
Thermococcus kodakarensis
120
-
secondary structure of the enzyme is not stable at this temperature
Thermococcus kodakarensis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
68
-
NADH
pH 7.8, 75°C
Thermococcus kodakarensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Thermococcus kodakarensis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.5
8.5
pH 7.5: about 70% of maximal activity, pH 8.5: about 70% of maximal activity
Thermococcus kodakarensis
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
tightly bound, 0.5 FAD attached per subunit
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Thermococcus kodakarensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
tightly bound, 0.5 FAD attached per subunit
Thermococcus kodakarensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.24
-
NADH
pH 7.8, 75°C
Thermococcus kodakarensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
48610
-
6 * 48610, sequence calculation
Thermococcus kodakarensis
49375
-
6 * 49375, mass spectrometry
Thermococcus kodakarensis
300000
-
gel filtration
Thermococcus kodakarensis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3 NADH + 3 H+ + 2 O2
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
725576
Thermococcus kodakarensis
3 NAD+ + H2O
-
-
-
?
3 NADPH + 3 H+ + 2 O2
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
725576
Thermococcus kodakarensis
3 NADP+ + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
hexamer
6 * 48610, sequence calculation; 6 * 49375, mass spectrometry
Thermococcus kodakarensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
75
-
-
Thermococcus kodakarensis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
70
80
70°C: about 60% of maximal activity, 80°C: about 70% of maximal activity
Thermococcus kodakarensis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
150 min, less than 5% loss of activity
Thermococcus kodakarensis
120
-
secondary structure of the enzyme is not stable at this temperature
Thermococcus kodakarensis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
68
-
NADH
pH 7.8, 75°C
Thermococcus kodakarensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Thermococcus kodakarensis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.5
8.5
pH 7.5: about 70% of maximal activity, pH 8.5: about 70% of maximal activity
Thermococcus kodakarensis
Other publictions for EC 1.6.3.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743751
Castillo-Villanueva
Cloning, expression and chara ...
Giardia intestinalis
Protein J.
35
24-33
2016
1
-
1
-
-
-
5
2
-
-
1
2
-
1
-
-
1
-
-
-
-
1
2
1
-
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
-
-
-
5
-
2
-
-
1
2
-
-
-
1
-
-
-
1
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
742466
Harnvoravongchai
Characterization and gene del ...
Thermococcus kodakarensis
Extremophiles
18
603-616
2014
-
-
-
-
-
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725576
Nisar
TK1299, a highly thermostable ...
Thermococcus kodakarensis
J. Biosci. Bioeng.
116
39-44
2013
-
-
1
-
-
-
-
1
-
-
3
-
-
1
-
-
1
-
-
-
-
-
2
1
1
1
2
1
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
3
-
-
-
-
1
-
-
-
-
2
1
1
1
2
1
1
1
-
-
-
-
-
-
-
-
723187
Jia
An archaeal NADH oxidase cause ...
Thermococcus profundus
Mol. Cells
29
363-371
2010
-
-
1
-
-
-
-
-
-
-
1
2
-
3
-
-
-
-
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
722229
Jia
Hexameric ring structure of a ...
Thermococcus profundus
FEBS J.
275
5355-5366
2008
-
-
1
-
3
-
-
2
-
-
2
1
-
4
-
-
1
-
-
-
-
-
3
1
1
1
-
2
1
1
-
3
-
-
-
-
-
1
3
-
3
-
-
-
-
2
-
-
2
1
-
-
-
1
-
-
-
-
3
1
1
1
-
2
1
1
-
-
-
1
1
-
2
2
723205
Li
A likely molecular basis of th ...
Giardia intestinalis
Mol. Microbiol.
59
202-211
2006
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
722165
Brown
A H2O-producing NADH oxidase f ...
Giardia intestinalis, Giardia intestinalis BRIS/83/HEPU/106
Eur. J. Biochem.
241
155-161
1996
-
-
-
-
-
-
8
2
-
1
2
2
-
2
-
-
1
-
-
1
-
-
8
1
-
-
-
-
1
1
-
3
-
-
-
-
-
-
3
-
-
-
-
8
-
2
-
1
2
2
-
-
-
1
-
1
-
-
8
1
-
-
-
-
1
1
-
-
-
1
1
-
-
-