BRENDA - Enzyme Database show
show all sequences of 1.14.13.208

Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii

Mohamed, M.E.; Zaar, A.; Ebenau-Jehle, C.; Fuchs, G.; J. Bacteriol. 183, 1899-1908 (2001)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
boxA gene
Azoarcus evansii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
the reductase componment BoxA contains 10.4 to 18.4 mol of Fe, and 13.3 to 17.9 mol of acid-labile sulfur per mol of native protein, depending on the method of protein determination
Azoarcus evansii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45883
-
2 * 45883, component BoxA, calculated from sequence
Azoarcus evansii
50000
-
2 * 50000, component BoxA, SDS-PAGE
Azoarcus evansii
98000
-
BoxA, gel filtration
Azoarcus evansii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
benzoyl-CoA + NADPH + H+ + O2
Azoarcus evansii
second step in aerobic benzoate metabolism, enzyme is induced by benzoate
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azoarcus evansii
-
-
-
Purification (Commentary)
Commentary
Organism
BoxA
Azoarcus evansii
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:benzoate-grown cell
-
Azoarcus evansii
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
benzoyl-CoA + NADPH + H+ + O2
second step in aerobic benzoate metabolism, enzyme is induced by benzoate
651677
Azoarcus evansii
?
-
-
-
?
additional information
purified reductase component BoxA catalyses, in the absence of BoxB, the electron transfer from NADPH to free FAD with a rate of 17 mmol/min*mg protein. This activity is very high compared to the benzoyl-CoA conversion rate with purified BoxAB (0.29 mmol/min*mg BoxA). The reductase component BoxA oxidizes NADPH to transfer electrons, mediated by enzyme-bound FAD, to one or two of the [4Fe-4S] centres of the protein. The flow of electrons from NADPH to the artificial electron acceptor, free FAD, is greatly (10-fold) stimulated by binding of benzoyl-CoA to BoxA
651677
Azoarcus evansii
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
2 * 45883, component BoxA, calculated from sequence; 2 * 50000, component BoxA, SDS-PAGE
Azoarcus evansii
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
the reductase componment BoxA contains 0.72 mol flavin adenine dinucleotide. BoxA oxidizes NADPH to transfer electrons, mediated by enzyme-bound FAD, to one or two of the [4Fe-4S] centres of the protein. The flow of electrons from NADPH to the artificial electron acceptor, free FAD, is greatly (10-fold) stimulated by binding of benzoyl-CoA to BoxA
Azoarcus evansii
NADPH
the reductase component BoxA oxidizes NADPH to transfer electrons, mediated by enzyme-bound FAD, to one or two of the [4Fe-4S] centres of the protein. The flow of electrons from NADPH to the artificial electron acceptor, free FAD, is greatly (10-fold) stimulated by binding of benzoyl-CoA to BoxA. No oxidation of NADH
Azoarcus evansii
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Azoarcus evansii
component BoxA, calculated from sequence
-
5.6
Cloned(Commentary) (protein specific)
Commentary
Organism
boxA gene
Azoarcus evansii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
the reductase componment BoxA contains 0.72 mol flavin adenine dinucleotide. BoxA oxidizes NADPH to transfer electrons, mediated by enzyme-bound FAD, to one or two of the [4Fe-4S] centres of the protein. The flow of electrons from NADPH to the artificial electron acceptor, free FAD, is greatly (10-fold) stimulated by binding of benzoyl-CoA to BoxA
Azoarcus evansii
NADPH
the reductase component BoxA oxidizes NADPH to transfer electrons, mediated by enzyme-bound FAD, to one or two of the [4Fe-4S] centres of the protein. The flow of electrons from NADPH to the artificial electron acceptor, free FAD, is greatly (10-fold) stimulated by binding of benzoyl-CoA to BoxA. No oxidation of NADH
Azoarcus evansii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
the reductase componment BoxA contains 10.4 to 18.4 mol of Fe, and 13.3 to 17.9 mol of acid-labile sulfur per mol of native protein, depending on the method of protein determination
Azoarcus evansii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45883
-
2 * 45883, component BoxA, calculated from sequence
Azoarcus evansii
50000
-
2 * 50000, component BoxA, SDS-PAGE
Azoarcus evansii
98000
-
BoxA, gel filtration
Azoarcus evansii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
benzoyl-CoA + NADPH + H+ + O2
Azoarcus evansii
second step in aerobic benzoate metabolism, enzyme is induced by benzoate
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
BoxA
Azoarcus evansii
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:benzoate-grown cell
-
Azoarcus evansii
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
benzoyl-CoA + NADPH + H+ + O2
second step in aerobic benzoate metabolism, enzyme is induced by benzoate
651677
Azoarcus evansii
?
-
-
-
?
additional information
purified reductase component BoxA catalyses, in the absence of BoxB, the electron transfer from NADPH to free FAD with a rate of 17 mmol/min*mg protein. This activity is very high compared to the benzoyl-CoA conversion rate with purified BoxAB (0.29 mmol/min*mg BoxA). The reductase component BoxA oxidizes NADPH to transfer electrons, mediated by enzyme-bound FAD, to one or two of the [4Fe-4S] centres of the protein. The flow of electrons from NADPH to the artificial electron acceptor, free FAD, is greatly (10-fold) stimulated by binding of benzoyl-CoA to BoxA
651677
Azoarcus evansii
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
2 * 45883, component BoxA, calculated from sequence; 2 * 50000, component BoxA, SDS-PAGE
Azoarcus evansii
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Azoarcus evansii
component BoxA, calculated from sequence
-
5.6
Other publictions for EC 1.14.13.208
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)
745167
Rokob
Pathways for arene oxidation ...
Azoarcus evansii, Azoarcus evansii KB 740
J. Am. Chem. Soc.
138
14623-14638
2016
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1
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4
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3
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1
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4
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1
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4
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4
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1
1
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744692
Liao
Mechanism and selectivity of ...
Azoarcus evansii
Chem. Sci.
6
2754-2764
2015
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1
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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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1
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2
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2
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1
1
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733379
Rather
The reducing component BoxA of ...
Azoarcus evansii
Biochim. Biophys. Acta
1814
1609-1615
2011
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1
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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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734168
Rather
Structure and mechanism of the ...
Azoarcus evansii
J. Biol. Chem.
286
29241-29248
2011
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1
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1
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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
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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712441
Rather
Coenzyme A-dependent aerobic m ...
Azoarcus evansii, Azoarcus evansii KB740
J. Biol. Chem.
285
20615-20624
2010
1
-
1
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-
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1
1
2
-
5
-
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1
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2
1
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3
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1
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1
3
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1
1
2
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1
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2
1
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700258
Zaar
New enzymes involved in aerobi ...
Azoarcus evansii, Azoarcus evansii KB740
Mol. Microbiol.
54
223-238
2004
1
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1
1
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1
1
2
-
5
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1
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10
1
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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1
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1
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1
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1
1
2
-
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1
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10
1
1
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1
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1
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-
698566
Gescher
Genes coding for a new pathway ...
Azoarcus evansii
J. Bacteriol.
184
6301-6315
2002
-
-
1
-
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1
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1
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3
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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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1
1
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2
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-
651677
Mohamed
Reinvestigation of a new type ...
Azoarcus evansii
J. Bacteriol.
183
1899-1908
2001
-
-
1
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-
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1
3
1
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4
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1
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1
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2
1
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2
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1
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1
2
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1
3
1
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1
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1
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2
1
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1
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