Information on EC 1.14.12.7 - phthalate 4,5-dioxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.12.7
-
RECOMMENDED NAME
GeneOntology No.
phthalate 4,5-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phthalate + NADH + H+ + O2 = cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Microbial metabolism in diverse environments
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Polycyclic aromatic hydrocarbon degradation
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-
SYSTEMATIC NAME
IUBMB Comments
phthalate,NADH:oxygen oxidoreductase (4,5-hydroxylating)
A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin. Requires Fe2+.
CAS REGISTRY NUMBER
COMMENTARY hide
63626-44-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
firefly
-
-
Manually annotated by BRENDA team
isolated from sewage sludge
UniProt
Manually annotated by BRENDA team
isolated from sewage sludge
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dicarboxypyridine + NADH + O2
5,6-dihydroxy-5,6-dihydropyridine-2,3-dicarboxylate + NAD+ + H2O
show the reaction diagram
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69% of the activity with o-phthalate
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-
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4-chloro-o-phthalate + NADH + O2
4-chloro-cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+ + H2O
show the reaction diagram
-
79% of the activity with o-phthalate
-
-
-
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
phthalate + NADH + H+ + O2
cis-4,5-dihydro-4,5-dihydroxyphthalate + NAD+
show the reaction diagram
phthalate + NADH + H+ + O2
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+
show the reaction diagram
phthalate + NADH + O2
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+ + H2O
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
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
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enzyme contains FMN
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
-
stimulates
additional information
-
optimal activity at ionic strength of 80 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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-
azide
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weak, binds to the six-coordinate resting enzyme to form a new six-coordinate Fe2+ species
diethylether
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Halothane
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Methoxyflurane
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n-butanol
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n-Heptanol
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n-Hexanol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002 - 0.5
Phthalate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
di-n-butyl phthalate degradation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
di-n-butyl phthalate degradation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
217000
-
gel filtration
250000
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gel filtration
290000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homohexamer
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
room temperature, 12 h, stable
439047
8
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room temperature, 12 h, stable
439047
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
-
pH 6.8 or pH 8.0, 12 h stable
25
-
stable below
42
-
1 h, stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, pH 8.0, 100 mM HEPES buffer, 20% v/v glycerol, stable for 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli 41 (DE3)
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expressed in Escherichia coli C41(DE3) cells
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expressed in Escherichia coli strain C41(DE3)
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gene from strain JDC-11, DNA and amino acid sequence determination and analysis, phylogenetic tree
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H120A
-
putative participation in phthalate dioxygenase reductase binding
K117A
-
putative participation in phthalate dioxygenase reductase binding
K117A/K119A/H120A/K121A/Y123A
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putative participation in phthalate dioxygenase reductase binding
K119A
-
putative participation in phthalate dioxygenase reductase binding
K121A
-
putative participation in phthalate dioxygenase reductase binding
W94A
-
adjacent to the Rieske center
W94F
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adjacent to the Rieske center
W94Y
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adjacent to the Rieske center
Y123A
-
putative participation in phthalate dioxygenase reductase binding
D178A
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mutation affects protonation of the Rieske center histidine and conformation of subunits within the PDO multimer to create a more open structure with more solvent-accessible Rieske centers; the rates of oxidation of the reduced Rieske centers are decreased by more than 10000fold, 16% of wild type activity
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D178N
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mutation affects protonation of the Rieske center histidine and conformation of subunits within the PDO multimer to create a more open structure with more solvent-accessible Rieske centers; the rates of oxidation of the reduced Rieske centers are decreased by more than 10000fold, 7% of wild type activity
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H120A
-
putative participation in phthalate dioxygenase reductase binding
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K117A
-
putative participation in phthalate dioxygenase reductase binding
-
K119A
-
putative participation in phthalate dioxygenase reductase binding
-
K121A
-
putative participation in phthalate dioxygenase reductase binding
-
Y123A
-
putative participation in phthalate dioxygenase reductase binding
-
Show AA Sequence (233 entries)
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