Information on EC 1.13.11.41 - 2,4'-dihydroxyacetophenone dioxygenase

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The expected taxonomic range for this enzyme is: Burkholderiales

EC NUMBER
COMMENTARY
1.13.11.41
-
RECOMMENDED NAME
GeneOntology No.
2,4'-dihydroxyacetophenone dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2,4'-dihydroxyacetophenone + O2 = 4-hydroxybenzoate + formate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Bisphenol degradation
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(4-hydroxybenzoyl)methanol oxygenase
-
-
-
-
DAD
F7J5X4
-
DAD
F7J5X4
-
-
DHAP dioxygenase
F7J5X4
-
DHAP dioxygenase
F7J5X4
-
-
CAS REGISTRY NUMBER
COMMENTARY
105503-64-8
-
257617-97-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 4HAP
SwissProt
Manually annotated by BRENDA team
Alcaligenes sp. 4HAP
strain 4HAP
SwissProt
Manually annotated by BRENDA team
isolated from a soil ssampple in Gifu, Japan, gene dad
UniProt
Manually annotated by BRENDA team
isolated from a soil ssampple in Gifu, Japan, gene dad
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
F7J5X4
the enzyme is involved in degradation of bisphenol A
metabolism
-
the enzyme is involved in degradation of bisphenol A
-
physiological function
F7J5X4
the enzyme is involved in degradation of bisphenol A
physiological function
-
the enzyme is involved in degradation of bisphenol A
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4-hydroxybenzoyl)methanol + O2
4-hydroxybenzoic acid + formic acid
show the reaction diagram
Q9REI7
-
-
?
2,4'-dihydroxyacetophenone + O2
4-hydroxybenzoate + formate
show the reaction diagram
Q9REI7
-
-
?
2,4'-dihydroxyacetophenone + O2
4-hydroxybenzoate + formate
show the reaction diagram
F7J5X4
-, anaerobic conditions
-
-
?
2,4'-dihydroxyacetophenone + O2
4-hydroxybenzoate + formate
show the reaction diagram
F7J5X4
-, anaerobic conditions
-
-
?
additional information
?
-
F7J5X4
2-hydroxyacetophenone is a poor substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(4-hydroxybenzoyl)methanol + O2
4-hydroxybenzoic acid + formic acid
show the reaction diagram
Q9REI7
-
-
?
2,4'-dihydroxyacetophenone + O2
4-hydroxybenzoate + formate
show the reaction diagram
F7J5X4
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
Q9REI7
contains one atom of iron per molecule of enzyme
Fe2+
F7J5X4
the enzyme contains 1.69 mol of non-heme iron per mol of enzyme, His77, His79, His115, and Glu96 in the cupin fold are putative metal ligands, Fe2+ weakly activates the enzyme
additional information
F7J5X4
poor or no effects by Fe3+, Ca2+ and Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
F7J5X4
-
2,2'-Dipyridine
F7J5X4
-
4-chloromercuribenzoate
F7J5X4
-
8-hydroxyquinoline
F7J5X4
-
Cu2+
F7J5X4
strong inhibition
diethyldicarbonate
F7J5X4
-
Hg2+
F7J5X4
strong inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
F7J5X4
slight activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0016
-
2,4'-dihydroxyacetophenone
F7J5X4
pH 7.0, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.042
-
F7J5X4
crude enzyme extract of strain AZ11, pH 7.0, 25C
0.33
-
F7J5X4
crude enzyme extract of recombinant Escherichia coli strain JM109 expressing gene dad, pH 7.0, 25C
2.85
-
Q9REI7
-
3.4
-
Q9REI7
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7
F7J5X4
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
F7J5X4
assay at
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
81600
87000
Q9REI7
gel filtration
83000
-
Q9REI7
gel filtration, BioSil TSK-125 column
87000
-
Q9REI7
Sephacryl S200
90000
-
F7J5X4
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homotetramer
F7J5X4
4 * 23000, recombinant enzyme, SDS-PAGE
homotetramer
-
4 * 23000, recombinant enzyme, SDS-PAGE
-
tetramer
Q9REI7
4 * 20364, amino acid sequence; 4 * 20379, electrospray MS; 4 * 21000, SDS-PAGE
tetramer
Alcaligenes sp. 4HAP
-
4 * 20364, amino acid sequence; 4 * 20379, electrospray MS; 4 * 21000, SDS-PAGE
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
F7J5X4
purified enzyme, 20 min, over 80% activity remaining
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C
Q9REI7
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partially
Q9REI7
recombinant enzyme 39fold from Escherichia coli strain JM109 by heat treatment, ammonium sulfate fractionation, gel filtration, and anion exchange chromatography, native enzyme 17fold from strain AZ11 by gel filtration, anion exchange and hydrophobic interaction chromatography
F7J5X4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene cloned, sequenced and expressed in Escherichia coli N-4830, nucleotide sequence of the gene dad deposited in the GenBank (r)/EMBL/DDBJ nucleotide sequence databases
Q9REI7
gene dad, DNA and amino acid sequence determination and analysis, sequence comparisons, overexpression in Escherichia coli strain JM109
F7J5X4