BRENDA - Enzyme Database show
show all sequences of 1.6.99.3

Involvement of glycine and aspartate residues in the binding capacity of FAD in the NADH dehydrogenase from an alkaliphilic Bacillus

Shiraki, M.; Koyama, N.; Curr. Microbiol. 46, 432-434 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Bacillus sp. YN-1
Engineering
Amino acid exchange
Commentary
Organism
A476S
82% of the wild-type NADH dehydrogenase activity
Bacillus sp. YN-1
D479A
no NADH dehydrogenase activity and NADH oxidase activity
Bacillus sp. YN-1
D479K
no NADH dehydrogenase activity and NADH oxidase activity
Bacillus sp. YN-1
G478A
no NADH dehydrogenase activity and NADH oxidase activity which appears to result from
Bacillus sp. YN-1
T469A
129% of the wild-type NADH dehydrogenase activity
Bacillus sp. YN-1
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus sp. YN-1
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme also shows NADH oxidase activity
658494
Bacillus sp. YN-1
?
-
-
-
-
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
658494
Bacillus sp. YN-1
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Bacillus sp. YN-1
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Bacillus sp. YN-1
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Bacillus sp. YN-1
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A476S
82% of the wild-type NADH dehydrogenase activity
Bacillus sp. YN-1
D479A
no NADH dehydrogenase activity and NADH oxidase activity
Bacillus sp. YN-1
D479K
no NADH dehydrogenase activity and NADH oxidase activity
Bacillus sp. YN-1
G478A
no NADH dehydrogenase activity and NADH oxidase activity which appears to result from
Bacillus sp. YN-1
T469A
129% of the wild-type NADH dehydrogenase activity
Bacillus sp. YN-1
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme also shows NADH oxidase activity
658494
Bacillus sp. YN-1
?
-
-
-
-
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
658494
Bacillus sp. YN-1
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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 ...
Escherichia coli
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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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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1
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1
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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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-
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-
6
-
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3
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7
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1
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4
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4
1
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3
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1
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6
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3
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1
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4
-
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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1
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1
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1
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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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1
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4
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1
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1
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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
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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
-
5
-
-
-
-
-
-
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-
2
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2
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1
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1
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
-
-
-
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-
-
-
1
-
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1
-
2
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2
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2
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2
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1
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2
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1
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1
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2
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2
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-
392825
Thiagalingam
-
Purification and characterizat ...
Bacillus megaterium
Can. J. Microbiol.
39
826-833
1993
-
-
-
-
-
-
10
4
1
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1
1
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1
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1
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1
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5
1
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1
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2
1
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2
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10
1
4
1
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1
1
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1
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5
1
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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
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2
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3
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1
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1
1
1
4
1
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3
1
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3
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1
2
2
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2
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1
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1
1
1
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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1
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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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4
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1
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8
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1
1
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1
1
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3
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3
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3
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4
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1
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1
1
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4
1
1
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1
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392811
Kitajima
Purification and properties of ...
Homo sapiens
Arch. Biochem. Biophys.
210
330-339
1981
-
-
-
-
-
-
7
2
1
-
2
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1
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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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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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1
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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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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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2
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