Information on EC 4.1.2.44 - 2,3-epoxybenzoyl-CoA dihydrolase

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The expected taxonomic range for this enzyme is: Azoarcus evansii

EC NUMBER
COMMENTARY hide
4.1.2.44
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RECOMMENDED NAME
GeneOntology No.
2,3-epoxybenzoyl-CoA dihydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,3-epoxy-2,3-dihydrobenzoyl-CoA + 2 H2O = (3Z)-6-oxohex-3-enoyl-CoA + formate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
benzoyl-CoA degradation I (aerobic)
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SYSTEMATIC NAME
IUBMB Comments
2,3-epoxy-2,3-dihydrobenzoyl-CoA (3Z)-6-oxohex-3-enoyl-CoA-lyase (formate-forming)
The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway of the bacterium Azoarcus evansii. The enzyme converts 2,3-epoxy-2,3-dihydrobenzoyl-CoA to its oxepin form prior to the ring-opening and the formation of a dialdehyde intermediate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Azoarcus evansii KB740 (DSMZ6869)
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SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
3,4-dehydroadipyl-CoA semialdehyde + formate
show the reaction diagram
additional information
?
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no activity with crotonyl-CoA
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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
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
3,4-dehydroadipyl-CoA semialdehyde + formate
show the reaction diagram
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the enzyme is involved in the aerobic benzoyl-CoA catabolic pathway. Benzoyl-CoA is oxidized to 2,3-dihydro-2,3-dihydroxybenzoyl-CoA (benzoyl-CoA dihydrodiol) by benzoyl-CoA oxygenase/reductase BoxBA in the presence of molecular oxygen. The next, ring cleaving step is catalysed by BoxC
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the purified protein does not require divalent metals or any cosubstrates or coenzymes for activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the purified protein does not require divalent metals or any cosubstrates or coenzymes for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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acetoacetyl-CoA (0.2 mM), a potential inhibitor of enoyl-CoA hydratase, has no impact on enzyme activity of BoxCmal. Crotonyl-CoA (0.2 mM), a potential substrate of enoyl-CoA hydratase (crotonase), is neither converted to 3-hydroxybutyryl-CoA nor does it inhibit the standard assay
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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addition of 1 mM thiamine diphosphate to the standard assay causes only a minimal stimulation (8%)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
2,3-dihydro-2,3-dihydroxybenzoyl-CoA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
2,3-dihydro-2,3-dihydroxybenzoyl-CoA
Azoarcus evansii
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
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half maximal activity at pH 7 and pH 11
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.44
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calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 61000, calculated from sequence
homodimer
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2 * 60000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, the protein can be stored without appreciable loss of activity for months in the presence of 10% (v/v) glycerol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild type and recombinant proteins
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the boxC gene is expressed in a recombinant Escherichia coli strain as a fusion protein with maltose binding protein (BoxCmal)
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