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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
LITERATURE
2,4'-dihydroxyacetophenone + O2 = 4-hydroxybenzoate + formate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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)
-
SYNONYMS
ORGANISM
UNIPROT
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
UNIPROT
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
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
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
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
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
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
F7J5X4
-
2,2'-Dipyridine
F7J5X4
-
4-chloromercuribenzoate
F7J5X4
-
8-hydroxyquinoline
F7J5X4
-
Co2+
F7J5X4
-
Cu2+
F7J5X4
strong inhibition
diethyldicarbonate
F7J5X4
-
Hg2+
F7J5X4
strong inhibition
Ni2+
F7J5X4
-
Tiron
F7J5X4
-
Zn2+
F7J5X4
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
F7J5X4
slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
2,4'-dihydroxyacetophenone
F7J5X4
pH 7.0, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
F7J5X4
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
F7J5X4
assay at
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
81600 - 87000
Q9REI7
gel filtration
439395
83000
Q9REI7
gel filtration, BioSil TSK-125 column
439395
87000
Q9REI7
Sephacryl S200
439395
90000
F7J5X4
recombinant enzyme, gel filtration
724599
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
F7J5X4
4 * 23000, recombinant enzyme, SDS-PAGE
homotetramer
-
4 * 23000, recombinant enzyme, SDS-PAGE
-
tetramer
Q9REI7
4 * 21000, SDS-PAGE, 4 * 20364, amino acid sequence, 4 * 20379, electrospray MS
tetramer
Alcaligenes sp. 4HAP
-
4 * 21000, SDS-PAGE, 4 * 20364, amino acid sequence, 4 * 20379, electrospray MS
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
F7J5X4
purified enzyme, 20 min, over 80% activity remaining
724599
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C
Q9REI7
Purification/COMMENTARY
ORGANISM
UNIPROT
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
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