Information on EC 1.14.14.27 - resorcinol 4-hydroxylase (FADH2)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.27
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RECOMMENDED NAME
GeneOntology No.
resorcinol 4-hydroxylase (FADH2)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
resorcinol + FADH2 + O2 = hydroxyquinol + FAD + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
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gamma-resorcylate degradation I
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
resorcinol,FADH2:oxygen oxidoreductase (4-hydroxylating)
The enzyme, characterized from the bacterium Rhizobium sp. strain MTP-10005, uses FADH2 as a substrate rather than a cofactor. FADH2 is provided by a dedicated EC 1.5.1.36, flavin reductase (NADH). The enzyme participates in the degradation of gamma-resorcylate and resorcinol. cf. EC 1.14.13.220, resorcinol 4-hydroxylase (NADH), and EC 1.14.13.219, resorcinol 4-hydroxylase (NADPH).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
orcinol + FADH2 + O2
? + FAD + H2O
show the reaction diagram
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90% of the hydroxylation activity as compared to resorcinol
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?
resorcinol + FADH2 + O2
hydroxyquinol + FAD + H2O
show the reaction diagram
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
resorcinol + FADH2 + O2
hydroxyquinol + FAD + H2O
show the reaction diagram
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the enzyme participates in the degradation of gamma-resorcylate and resorcinol
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FADH2
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contains approximately 1 mol of FAD for each polypeptide chain. The enzyme uses FADH2 as a substrate rather than a cofactor. FADH2 is provided by flavin reductase (NADH)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.6
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pH 6.8, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
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gel filtration
70000
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1 * 70000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45500, oxygenase components of resorcinol hydroxylase, SDS-PAGE
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
resorcinol hydroxylase accounts for about 3% of the total protein in Pseudomonas putida ORC after growth on resorcinol
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli