BRENDA - Enzyme Database show
show all sequences of 1.14.13.208

New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii

Zaar, A.; Gescher, J.; Eisenreich, W.; Bacher, A.; Fuchs, G.; Mol. Microbiol. 54, 223-238 (2004)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
BoxC
addition of the putative ring cleaving enzyme BoxC leads to a several-fold acceleration of the initial rate and completes conversion of benzoyl-CoA. BoxC might facilitate the binding of BoxA to BoxB and thus lead to the observed rate increase
Azoarcus evansii
Inhibitors
Inhibitors
Commentary
Organism
Structure
KCl
higher salt concentration (500 mM KCl) results in sixfold lower activity suggesting that the interaction of the protein components is affected by high salt concentration
Azoarcus evansii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.03
-
benzoyl-CoA
pH 8, 22°C, addition of the putative ring cleaving enzyme BoxC leads to a several-fold acceleration of the initial rate and completes conversion of benzoyl-CoA. Because of this complex behaviour of the oxygenase system, the apparent Km value for benzoyl-CoA can only be estimated from the time curve of benzoyl-CoA concentration in an assay mixture that contains BoxAB and the putative ring-cleaving enzyme BoxC. This curve shows a half-maximal rate at a benzoyl-CoA concentration of 0.03 mM
Azoarcus evansii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein, which acts as reductase. BoxB is a monomeric iron-protein. Subunit BoxB contains 1.6 mol of iron per mol of protein, addition of 1 mM Fe2+ to the assays has no stimulatory or inhibitory effect on the catalytic turnover
Azoarcus evansii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
2 * 46000 (BoxA) + 50000 (BoxB), boxA/boxB system, BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein, which acts as reductase. BoxB is a monomeric iron-protein (50000-60000 Da, gel filtration. 50000 Da, SDS-PAGE)
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
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
?
benzoyl-CoA + NADPH + H+ + O2
Azoarcus evansii KB740
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azoarcus evansii
Q9AIX6 and Q9AIX7
Q9AIX6: subunit A, Q9AIX7: subunit B
-
Azoarcus evansii KB740
Q9AIX6 and Q9AIX7
Q9AIX6: subunit A, Q9AIX7: subunit B
-
Purification (Commentary)
Commentary
Organism
His6-tagged component B of benzoyl-CoA oxygenase, component A of benzoyl-CoA oxygenase
Azoarcus evansii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-fluorobenzoyl-CoA + NADPH + H+ + O2
83% of the activity with benzoyl-CoA
700258
Azoarcus evansii
?
-
-
-
?
2-fluorobenzoyl-CoA + NADPH + H+ + O2
83% of the activity with benzoyl-CoA
700258
Azoarcus evansii KB740
?
-
-
-
?
4-fluorobenzoyl-CoA + NADPH + H+ + O2
30% of the activity with benzoyl-CoA
700258
Azoarcus evansii
?
-
-
-
?
4-fluorobenzoyl-CoA + NADPH + H+ + O2
30% of the activity with benzoyl-CoA
700258
Azoarcus evansii KB740
?
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
700258
Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
no activity with NADH as electron donor
700258
Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
700258
Azoarcus evansii KB740
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
no activity with NADH as electron donor
700258
Azoarcus evansii KB740
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
additional information
no activity with benzoate or phenylacetyl-CoA
700258
Azoarcus evansii
?
-
-
-
-
additional information
no activity with benzoate or phenylacetyl-CoA
700258
Azoarcus evansii KB740
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
2 * 46000 (BoxA) + 50000 (BoxB), boxA/boxB system, BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein, which acts as reductase. BoxB is a monomeric iron-protein (50000-60000 Da, gel filtration. 50000 Da, SDS-PAGE)
Azoarcus evansii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Azoarcus evansii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Azoarcus evansii
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
no activity with NADH
Azoarcus evansii
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Azoarcus evansii
calculated from sequence
-
5.6
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
BoxC
addition of the putative ring cleaving enzyme BoxC leads to a several-fold acceleration of the initial rate and completes conversion of benzoyl-CoA. BoxC might facilitate the binding of BoxA to BoxB and thus lead to the observed rate increase
Azoarcus evansii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
no activity with NADH
Azoarcus evansii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
KCl
higher salt concentration (500 mM KCl) results in sixfold lower activity suggesting that the interaction of the protein components is affected by high salt concentration
Azoarcus evansii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.03
-
benzoyl-CoA
pH 8, 22°C, addition of the putative ring cleaving enzyme BoxC leads to a several-fold acceleration of the initial rate and completes conversion of benzoyl-CoA. Because of this complex behaviour of the oxygenase system, the apparent Km value for benzoyl-CoA can only be estimated from the time curve of benzoyl-CoA concentration in an assay mixture that contains BoxAB and the putative ring-cleaving enzyme BoxC. This curve shows a half-maximal rate at a benzoyl-CoA concentration of 0.03 mM
Azoarcus evansii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein, which acts as reductase. BoxB is a monomeric iron-protein. Subunit BoxB contains 1.6 mol of iron per mol of protein, addition of 1 mM Fe2+ to the assays has no stimulatory or inhibitory effect on the catalytic turnover
Azoarcus evansii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
2 * 46000 (BoxA) + 50000 (BoxB), boxA/boxB system, BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein, which acts as reductase. BoxB is a monomeric iron-protein (50000-60000 Da, gel filtration. 50000 Da, SDS-PAGE)
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
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
?
benzoyl-CoA + NADPH + H+ + O2
Azoarcus evansii KB740
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
His6-tagged component B of benzoyl-CoA oxygenase, component A of benzoyl-CoA oxygenase
Azoarcus evansii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-fluorobenzoyl-CoA + NADPH + H+ + O2
83% of the activity with benzoyl-CoA
700258
Azoarcus evansii
?
-
-
-
?
2-fluorobenzoyl-CoA + NADPH + H+ + O2
83% of the activity with benzoyl-CoA
700258
Azoarcus evansii KB740
?
-
-
-
?
4-fluorobenzoyl-CoA + NADPH + H+ + O2
30% of the activity with benzoyl-CoA
700258
Azoarcus evansii
?
-
-
-
?
4-fluorobenzoyl-CoA + NADPH + H+ + O2
30% of the activity with benzoyl-CoA
700258
Azoarcus evansii KB740
?
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
700258
Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
no activity with NADH as electron donor
700258
Azoarcus evansii
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
the enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii
700258
Azoarcus evansii KB740
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
benzoyl-CoA + NADPH + H+ + O2
no activity with NADH as electron donor
700258
Azoarcus evansii KB740
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
-
-
-
?
additional information
no activity with benzoate or phenylacetyl-CoA
700258
Azoarcus evansii
?
-
-
-
-
additional information
no activity with benzoate or phenylacetyl-CoA
700258
Azoarcus evansii KB740
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
2 * 46000 (BoxA) + 50000 (BoxB), boxA/boxB system, BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein, which acts as reductase. BoxB is a monomeric iron-protein (50000-60000 Da, gel filtration. 50000 Da, SDS-PAGE)
Azoarcus evansii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Azoarcus evansii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Azoarcus evansii
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Azoarcus evansii
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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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
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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734168
Rather
Structure and mechanism of the ...
Azoarcus evansii
J. Biol. Chem.
286
29241-29248
2011
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712441
Rather
Coenzyme A-dependent aerobic m ...
Azoarcus evansii, Azoarcus evansii KB740
J. Biol. Chem.
285
20615-20624
2010
1
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1
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1
1
2
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5
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1
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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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-
-
-
-
-
-
-
-
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-
700258
Zaar
New enzymes involved in aerobi ...
Azoarcus evansii, Azoarcus evansii KB740
Mol. Microbiol.
54
223-238
2004
1
-
-
-
-
-
1
1
-
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
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-
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
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
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1
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1
3
1
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4
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1
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1
3
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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