Information on EC 4.1.2.44 - benzoyl-CoA-dihydrodiol lyase

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The expected taxonomic range for this enzyme is: Azoarcus evansii

EC NUMBER
COMMENTARY
4.1.2.44
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RECOMMENDED NAME
GeneOntology No.
benzoyl-CoA-dihydrodiol lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O = 3,4-didehydroadipyl-CoA semialdehyde + 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-dihydro-2,3-dihydroxybenzoyl-CoA lyase/hydrolase (deformylating)
The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway of the bacterium Azoarcus evansii.
ORGANISM
COMMENTARY
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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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, NADPH and semicarbazide are analysed directly by NMR spectroscopy and mass spectrometry. The purified protein does not require molecular oxygen for activity
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-
?
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
3,4-dehydroadipyl-CoA semialdehyde + formate
show the reaction diagram
Azoarcus evansii, Azoarcus evansii KB740
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2,3-dihydro-2,3-dihydroxybenzoyl-CoA is also named 2,3-epoxybenzoyl-CoA
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?
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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
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
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
LITERATURE
additional information
-
the purified protein does not require divalent metals or any cosubstrates or coenzymes for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
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
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
LITERATURE
IMAGE
0.017
2,3-dihydro-2,3-dihydroxybenzoyl-CoA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20
2,3-dihydro-2,3-dihydroxybenzoyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 11
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half maximal activity at pH 7 and pH 11
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.44
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calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
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gel filtration
700259
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
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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