Information on EC 1.14.13.208 - benzoyl-CoA 2,3-epoxidase

Word Map on EC 1.14.13.208
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Azoarcus evansii

EC NUMBER
COMMENTARY hide
1.14.13.208
-
RECOMMENDED NAME
GeneOntology No.
benzoyl-CoA 2,3-epoxidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + NADPH + H+ + O2 = 2,3-epoxy-2,3-dihydrobenzoyl-CoA + NADP+ + H2O
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
benzoyl-CoA degradation I (aerobic)
-
-
SYSTEMATIC NAME
IUBMB Comments
benzoyl-CoA,NADPH:oxygen oxidoreductase (2,3-epoxydizing)
The enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii. BoxB functions as the oxygenase part of benzoyl-CoA oxygenase in conjunction with BoxA, the reductase component, which upon binding of benzoyl-CoA, transfers two electrons to the ring in the course of monooxygenation. BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein (FAD), BoxB is a monomeric iron-protein [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-fluorobenzoyl-CoA + NADPH + H+ + O2
?
show the reaction diagram
4-fluorobenzoyl-CoA + NADPH + H+ + O2
?
show the reaction diagram
benzoyl-CoA + NADPH + H+ + O2
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
show the reaction diagram
benzoyl-CoA + NADPH + H+ + O2
2,3-epoxy-2,3-dihydrobenzoyl-CoA + NADP+ + H2O
show the reaction diagram
benzoyl-CoA + NADPH + H+ + O2
?
show the reaction diagram
-
second step in aerobic benzoate metabolism, enzyme is induced by benzoate
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
benzoyl-CoA + NADPH + H+ + O2
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
show the reaction diagram
benzoyl-CoA + NADPH + H+ + O2
2,3-epoxy-2,3-dihydrobenzoyl-CoA + NADP+ + H2O
show the reaction diagram
benzoyl-CoA + NADPH + H+ + O2
?
show the reaction diagram
-
second step in aerobic benzoate metabolism, enzyme is induced by benzoate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe-S center
-
-
NADPH
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
Q9AIX6 and Q9AIX7
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BoxC
Q9AIX6 and Q9AIX7
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
-
BoxC protein
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
benzoyl-CoA
Q9AIX6 and Q9AIX7
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
Q9AIX6 and Q9AIX7
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
Q9AIX6 and Q9AIX7
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.59
Q9AIX6 and Q9AIX7
benzoyl-CoA oxygenase component A, calculated from sequence
5.62
Q9AIX6 and Q9AIX7
benzoyl-CoA oxygenase component B, calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Q9AIX6 and Q9AIX7
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
98000
-
BoxA, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.1 M NaH2PO4 and 0.2 M K2HPO4 as precipitant
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged component B of benzoyl-CoA oxygenase, component A of benzoyl-CoA oxygenase
Q9AIX6 and Q9AIX7
Strep-Tactin Superflow column chromatography
-
Streptavidin affinity column chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q9AIX6 and Q9AIX7
boxA gene
-
expressed in Escherichia coli DH5alpha cells
-