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Information on EC 1.14.13.6 - orcinol 2-monooxygenase
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1.14.13.6 orcinol 2-monooxygenaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.14.13.6
- resorcinol
- putida
-
resorcinylic
- fad
- m-cresol
- flavoproteins
-
tritium
-
1,2-oxygenase
- deuterium
- quinone
-
mono-oxygenase
- flavin
- hydroxyquinol
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nonenzymic
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
orcinol hydroxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
orcinol hydroxylase
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oxygenase, orcinol 2-mono
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
orcinol + NADH + H+ + O2 = 2,3,5-trihydroxytoluene + NAD+ + H2O
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
orcinol,NADH:oxygen oxidoreductase (2-hydroxylating)
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
37217-34-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
orcinol + 3-acetylpyridine-NADH + H+ + O2
2,3,5-trihydroxytoluene + 3-acetylpyridine-NAD+ + H2O
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-
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r
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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nonsubstrate effector, which increases NADH oxidase activity without being hydroxylated
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-
?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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nonsubstrate effector, which increases NADH oxidase activity without being hydroxylated
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-
?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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11-14% of the activity with orcinol
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?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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20 to 70% coupled in various assays
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?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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nonsubstrate effector, which increases NADH oxidase activity without being hydroxylated
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-
?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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20 to 70% coupled in various assays
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?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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nonsubstrate effector, which increases NADH oxidase activity without being hydroxylated
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-
?
3-cresol + NADH + O2
3-methylcatechol + NAD+ + H2O
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11-14% of the activity with orcinol
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?
3-ethylphenol + NADH + O2
?
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no substrate, mimic orcinol as effector
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?
3-ethylphenol + NADH + O2
?
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no substrate, mimic orcinol as effector
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?
3-trifluoromethylphenol + NADH + O2
?
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94% of activity with orcinol
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?
3-trifluoromethylphenol + NADH + O2
?
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94% of activity with orcinol
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?
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
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highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol
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?
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
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highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol
-
?
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
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highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol
-
?
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
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highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol
-
?
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
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highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol
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?
orcinol + NADH + O2
2,3,5-trihydroxytoluene + NAD+ + H2O
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?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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hydroxylated to a limited extent
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?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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behaves both as a substrate and a nonsubstrate effector
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?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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hydroxylated to a limited extent
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?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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hydroxylated to a limited extent
-
?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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23% of activity with orcinol
-
?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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the enzyme processes resorcinol to hydroxylated product 66% of the time
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?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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hydroxylated to a limited extent
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?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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the enzyme processes resorcinol to hydroxylated product 66% of the time
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?
resorcinol + NADH + O2
hydroxyquinol + NAD+ + H2O
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23% of activity with orcinol
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?
additional information
?
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reduced orcinol hydroxylase is able to transfer reducing equivalents to a variety of electron acceptors, other than oxygen. These include free FAD, ferricyanide, cytochrome c, acetylpyridine-NAD and tetrazolium salts
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?
additional information
?
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reduced orcinol hydroxylase is able to transfer reducing equivalents to a variety of electron acceptors, other than oxygen. These include free FAD, ferricyanide, cytochrome c, acetylpyridine-NAD and tetrazolium salts
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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4R stereospecificity for the transfer of hydride, substrate: orcinol
NADH
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mixed type 4R,4S stereospecificity with respect to dihydronicotinamide oxidation with the substrates m-cresol and resorcinol, 4R chirality with orcinol
NADH
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4R stereospecificity with respect to dihydronicotinamide oxidation with the substrates: orcinol, resorcinol and m-cresol
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
difficult to evaluate, because the values do not take into account the nonenzymic oxidation rate of the product of the reaction
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flashner, M.S.; Massey, V.
Flavoprotein oxygenases
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
245-283
1974
Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas putida 1
-
brenda
Sahasrabudhe, S.R.; Lala, D.; Modi, V.V.
Degradation of orcinol by Aspergillus niger
Can. J. Microbiol.
32
535-538
1986
Aspergillus niger
brenda
Otha, Y.; Ribbons, D.W.
Crystallization of orcinol hydroxylase from Pseudomonas putida
FEBS Lett.
11
189-192
1970
Pseudomonas putida, Pseudomonas putida 1
brenda
Ribbons, D.W.; Ohta, Y.; Higgins, I.J.
Specificity of a catabolic pathway--a lesson learned from indirect assays
J. Bacteriol.
106
702-703
1971
Pseudomonas putida, Pseudomonas putida 1
brenda
Ryerson, C.C.; Walsh, C.
The stereochemistry of NADH utilization by the flavoenzyme monooxygenase orcinol hydroxylase
J. Biol. Chem.
254
4349-4351
1979
Pseudomonas putida, Pseudomonas putida 1
brenda
Ribbons, D.W.; Ohta, Y.; Higgins, I.J.
Electron transport in a flavoprotein, orcinol hydroxylase
Mol. Basis of Electron Transp. (Proc. Miami Winter Symp. , Schultz, J. , Cameron, B. F. , eds. )
4
251-274
1972
Pseudomonas putida, Pseudomonas putida 1
-
brenda
Ohta, Y.; Ribbons, D.W.
Bacterial metabolism of resorcinylic compounds: purification and properties of orcinol hydroxylase and resorcinol hydroxylase from Pseudomonas putida ORC
Eur. J. Biochem.
61
259-269
1976
Pseudomonas putida, Pseudomonas putida ORC
brenda
Ohta, Y.; Higgins, I.J.; Ribbons, D.W.
Metabolism of resorcinylic compounds by bacteria. Purification and properties of orcinol hydroxylase from Pseudomonas putida 01
J. Biol. Chem.
250
3814-3825
1975
Pseudomonas putida, Pseudomonas putida 1
brenda
Higgins, I.J.; Ribbons, D.W.
Stereospecificity of hydride transfer in the flavin mono-oxygenase orcinol hydroxylase
Biochem. J.
127
65P
1972
Pseudomonas putida
brenda
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