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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.41
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RECOMMENDED NAME
GeneOntology No.
2,4'-dihydroxyacetophenone dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,4'-dihydroxyacetophenone + O2 = 4-hydroxybenzoate + formate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bisphenol degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving)
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CAS REGISTRY NUMBER
COMMENTARY hide
105503-64-8
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257617-97-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4-hydroxybenzoyl)methanol + O2
4-hydroxybenzoic acid + formic acid
show the reaction diagram
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-
?
2,4'-dihydroxyacetophenone + O2
4-hydroxybenzoate + formate
show the reaction diagram
additional information
?
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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
(4-hydroxybenzoyl)methanol + O2
4-hydroxybenzoic acid + formic acid
show the reaction diagram
Q9REI7
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-
?
2,4'-dihydroxyacetophenone + O2
4-hydroxybenzoate + formate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
poor or no effects by Fe3+, Ca2+ and Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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2,2'-dipyridine
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4-chloromercuribenzoate
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8-hydroxyquinoline
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Cu2+
strong inhibition
diethyldicarbonate
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Hg2+
strong inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
2,4'-dihydroxyacetophenone
pH 7.0, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.042
crude enzyme extract of strain AZ11, pH 7.0, 25C
0.33
crude enzyme extract of recombinant Escherichia coli strain JM109 expressing gene dad, pH 7.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20364
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4 * 20364, amino acid sequence
20379
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4 * 20379, electrospray MS
21000
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4 * 21000, SDS-PAGE
23000
4 * 23000, recombinant enzyme, SDS-PAGE
40000
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recombinant chymotrypsinolysed enzyme, gel filtration and analytical ultracentrifugation
80000
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recombinant wild-type enzyme, gel filtration and analytical ultracentrifugation
81600 - 87000
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gel filtration
83000
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gel filtration, BioSil TSK-125 column
87000
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Sephacryl S200
90000
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, mixing of 5 mg/ml protein in 50 mM Tris, pH 7.3, 100 mM NaCl, and mM 4-hydroxybenzoic acid or 0.1 mM 4-aminobenzamidine, with reservoir solution containing 0.1 M sodium cacodylate pH 5.9-6.8 and 1.1-1.6 M sodium acetate, method optimization, X-ray diffraction structure determination and analysis at 1.88 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein
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purified recombinant detagged chymotrypsinolysed enzyme, 5 mg/ml protein in 50 mM Tris, pH 7.5, 100 mM NaCl, 1 mM 2-mercaptoethanol is mixed with a solution containing 10% w/v PEG 1000 and 10% PEG 8000, X-ray diffraction structure determination and analysis at 2.2 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein
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purified recombinant His-tagged chymotrypsinolysed enzyme, 5 mg/ml protein in 50 mM Tris, pH 7.5, 100 mM NaCl, 1 mM 2-mercaptoethanol is mixed with a solution containing 10% w/v PEG 1000 and 10% PEG 8000, X-ray diffraction structure determination and analysis at 2.2 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
purified enzyme, 20 min, over 80% activity remaining
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially
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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
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, removal of the His-tag by thrombin cleavage
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Cloned/COMMENTARY
ORGANISM
UNIPROT
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
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gene dad, DNA and amino acid sequence determination and analysis, sequence comparisons, overexpression in Escherichia coli strain JM109
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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