Information on EC 1.14.13.6 - orcinol 2-monooxygenase

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

EC NUMBER
COMMENTARY hide
1.14.13.6
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RECOMMENDED NAME
GeneOntology No.
orcinol 2-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
orcinol + NADH + H+ + O2 = 2,3,5-trihydroxytoluene + NAD+ + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
orcinol degradation
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SYSTEMATIC NAME
IUBMB Comments
orcinol,NADH:oxygen oxidoreductase (2-hydroxylating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
37217-34-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-chlorophenol + NADH + O2
?
show the reaction diagram
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33% of activity with orcinol
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?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
show the reaction diagram
3-ethylphenol + NADH + O2
?
show the reaction diagram
3-trifluoromethylphenol + NADH + O2
?
show the reaction diagram
4-bromoresorcinol + NADH + O2
?
show the reaction diagram
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-
-
-
?
4-methylresorcinol + NADH + O2
?
show the reaction diagram
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-
-
-
?
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
show the reaction diagram
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Acetyl pyridine nucleotide
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-Dimethoxybenzene
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45% inhibition at 1.7 mM
2-Hydroxy-4-methoxybenzoate
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68% inhibition at 1.7 mM
2-Methylresorcinol
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27% inhibition at 1.7 mM
2-Nitroorcinol
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64% inhibition at 1.7 mM
3,4-dimethylphenol
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54% inhibition at 1.7 mM
3,5-Dihydroxybenzoate
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59% inhibition at 1.7 mM
3,5-Dimethylphenol
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68% inhibition at 1.7 mM
3-Hydroxybenzaldehyde
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23% inhibition at 1.7 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
m-cresol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
3-acetylpyridine NADH
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substrate: orcinol
0.17
3-cresol
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0.13 - 2.5
NADH
0.026 - 0.085
orcinol
0.19 - 0.22
resorcinol
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
orcinol
Pseudomonas putida
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crystalline enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8
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apoenzyme without flavin addition
3.5
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apoenzyme with addition of FMN
14.7
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apoenzyme with addition of FAD
18
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holoenzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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difficult to evaluate, because the values do not take into account the nonenzymic oxidation rate of the product of the reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000 - 70000
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gel filtration
63000
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gel filtration
65000
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sedimentation equilibrium
68000
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gel filtration
70000
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ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in 2-3 days by addition of ammonium sulfate until turbidity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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highest stability
438809
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
thiol reagents, e.g. 2-mercaptoethanol, stabilize
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stabilized by thiol reagents, e.g. 2-mercaptoethanol, some days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ORC, using protamine sulfate treatment, column chromatography on DEAE-cellulose, Sephadex G-100, Sephadex G-75 and a second DEAE-cellulose column chromatography
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using protamine sulfate treatment, column chromatography on DEAE-cellulose, Sephadex G-100, Sephadex G-75, a second DEAE-cellulose column chromatography and crystallization
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using protamine sulfate treatment, DEAE-cellulose column chromatography, ammonium sulfate treatment and column chromatography on Sephadex G-100 followed by ammonium sulfate treatment and column chromatography on hydroxylapatite
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
most of the activity of the apoenzyme is reconstituted by the addition of FAD, FMN is a poor substitute for FAD
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