BRENDA - Enzyme Database show
show all sequences of 1.6.99.3

Purification and characterization of NADH dehydrogenase from Bacillus megaterium

Thiagalingam, S.; Yang, T.; Can. J. Microbiol. 39, 826-833 (1993)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
AMP
; 10 mM, 41% inhibition
Bacillus megaterium
ATP
10 mM, 17% inhibition
Bacillus megaterium
EDTA
10 mM, 21% inhibition
Bacillus megaterium
HgCl2
10 mM, complete inhibition
Bacillus megaterium
KCN
10 mM, 36% inhibition
Bacillus megaterium
additional information
no inhibition by rotenone
Bacillus megaterium
NAD+
competitive
Bacillus megaterium
PCMB
10 mM, 90% inhibition
Bacillus megaterium
sodium arsenite
10 mM, 44% inhibition
Bacillus megaterium
Sodium azide
10 mM, 24% inhibition
Bacillus megaterium
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0157
-
NADH
reaction with 2,6-dichlorophenolindophenol
Bacillus megaterium
0.0348
-
NADH
reaction with ferricyanide
Bacillus megaterium
0.0692
-
NADH
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
Bacillus megaterium
1.035
-
NADPH
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
Bacillus megaterium
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
can be solubilized by sonication
Bacillus megaterium
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
x * 42000, SDS-PAGE
Bacillus megaterium
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus megaterium
the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus megaterium
-
-
-
Purification (Commentary)
Commentary
Organism
-
Bacillus megaterium
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.725
-
-
Bacillus megaterium
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferricyanide + NADH
-
392825
Bacillus megaterium
2 ferrocyanide + NAD+ + H+
-
-
-
?
additional information
the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
392825
Bacillus megaterium
?
-
-
-
-
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
-
392825
Bacillus megaterium
NAD+ + ?
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
392825
Bacillus megaterium
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
rate of oxidation is less than 5% of the reaction with NADH
392825
Bacillus megaterium
NADP+ + ?
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 42000, SDS-PAGE
Bacillus megaterium
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
7.8
-
Bacillus megaterium
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Bacillus megaterium
NADH
specific for NADH
Bacillus megaterium
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.037
-
NAD+
-
Bacillus megaterium
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Bacillus megaterium
NADH
specific for NADH
Bacillus megaterium
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
AMP
; 10 mM, 41% inhibition
Bacillus megaterium
ATP
10 mM, 17% inhibition
Bacillus megaterium
EDTA
10 mM, 21% inhibition
Bacillus megaterium
HgCl2
10 mM, complete inhibition
Bacillus megaterium
KCN
10 mM, 36% inhibition
Bacillus megaterium
additional information
no inhibition by rotenone
Bacillus megaterium
NAD+
competitive
Bacillus megaterium
PCMB
10 mM, 90% inhibition
Bacillus megaterium
sodium arsenite
10 mM, 44% inhibition
Bacillus megaterium
Sodium azide
10 mM, 24% inhibition
Bacillus megaterium
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.037
-
NAD+
-
Bacillus megaterium
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0157
-
NADH
reaction with 2,6-dichlorophenolindophenol
Bacillus megaterium
0.0348
-
NADH
reaction with ferricyanide
Bacillus megaterium
0.0692
-
NADH
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
Bacillus megaterium
1.035
-
NADPH
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
Bacillus megaterium
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
can be solubilized by sonication
Bacillus megaterium
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
x * 42000, SDS-PAGE
Bacillus megaterium
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus megaterium
the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus megaterium
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.725
-
-
Bacillus megaterium
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferricyanide + NADH
-
392825
Bacillus megaterium
2 ferrocyanide + NAD+ + H+
-
-
-
?
additional information
the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
392825
Bacillus megaterium
?
-
-
-
-
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
-
392825
Bacillus megaterium
NAD+ + ?
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
392825
Bacillus megaterium
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
rate of oxidation is less than 5% of the reaction with NADH
392825
Bacillus megaterium
NADP+ + ?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 42000, SDS-PAGE
Bacillus megaterium
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
7.8
-
Bacillus megaterium
Other publictions for EC 1.6.99.3
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)
741964
Villegas
FAD binding properties of a c ...
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Biochim. Biophys. Acta
1844
576-584
2014
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724488
Villegas
Maintenance and thermal stabil ...
Arabidopsis thaliana, Marchantia polymorpha, Nicotiana tabacum, Synechocystis sp., Zea mays
Biochimie
95
382-387
2013
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8
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5
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14
14
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746936
Lakhal
Oxygen uptake rates in the hy ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Arch. Microbiol.
193
429-438
2011
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701758
Do
Engineering Escherichia coli f ...
Trichomonas vaginalis
Appl. Biochem. Biotechnol.
153
21-33
2009
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1
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6
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3
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7
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-
4
1
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3
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685693
Chakraborty
Two proteins with diaphorase a ...
Moorella thermoacetica
Biosci. Biotechnol. Biochem.
72
877-879
2008
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1
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2
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1
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692853
Platt
Proteomic, microarray, and sig ...
Pseudomonas aeruginosa
J. Bacteriol.
190
2739-2758
2008
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1
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1
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4
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677088
Kitazume
Involvement of Lys-308 in the ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) YN-1
Res. Microbiol.
157
956-959
2006
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2
-
1
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3
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658494
Shiraki
Involvement of glycine and asp ...
Bacillus sp. YN-1
Curr. Microbiol.
46
432-434
2003
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1
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5
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2
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392824
Marques
Activation of a NADH dehydroge ...
Homo sapiens
Biol. Signals
6
52-61
1997
1
-
-
-
-
-
-
-
1
-
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2
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392825
Thiagalingam
-
Purification and characterizat ...
Bacillus megaterium
Can. J. Microbiol.
39
826-833
1993
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10
4
1
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1
1
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5
1
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1
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10
1
4
1
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5
1
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392819
Nisimoto
NADH dehydrogenase from bovine ...
Bos taurus
J. Biol. Chem.
261
285-290
1986
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3
2
2
-
2
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3
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1
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1
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1
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1
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4
1
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392812
Borneleit
-
Purification and properties of ...
Acinetobacter calcoaceticus
Biochim. Biophys. Acta
722
94-101
1983
1
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392820
Bergsma
Purification and characterizat ...
Bacillus subtilis, Bacillus subtilis W23
Eur. J. Biochem.
128
151-157
1982
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3
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1
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392811
Kitajima
Purification and properties of ...
Homo sapiens
Arch. Biochem. Biophys.
210
330-339
1981
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7
2
1
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2
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1
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1
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1
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6
1
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1
2
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3
1
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3
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7
1
2
1
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2
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1
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1
1
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6
1
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1
2
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392810
Wang
Human erythrocyte NADH: (accep ...
Homo sapiens
Biochim. Biophys. Acta
616
22-29
1980
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3
2
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392805
Adachi
Study on the reduced pyridine ...
Bos taurus
Biochim. Biophys. Acta
268
629-637
1972
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1
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1
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392821
Ramanarayanan
Purification & properties of a ...
Agrobacterium tumefaciens
Indian J. Biochem. Biophys.
8
214-218
1971
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1
1
1
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1
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392807
Kaniuga
The Transformation of mitochon ...
Sus scrofa
Biochim. Biophys. Acta
73
550-564
1963
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