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 hide
1.13.11.41
-
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
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bisphenol degradation
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving)
-
CAS REGISTRY NUMBER
COMMENTARY hide
105503-64-8
-
257617-97-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
COMMENTARY hide
LITERATURE
metabolism
physiological function
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
-
-
?
2,4'-dihydroxyacetophenone + O2
4-hydroxybenzoate + formate
show the reaction diagram
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
(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
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
-
2,2'-dipyridine
-
4-chloromercuribenzoate
-
8-hydroxyquinoline
-
Cu2+
strong inhibition
diethyldicarbonate
-
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
81600 - 87000
gel filtration
83000
gel filtration, BioSil TSK-125 column
87000
Sephacryl S200
90000
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
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
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
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
gene dad, DNA and amino acid sequence determination and analysis, sequence comparisons, overexpression in Escherichia coli strain JM109