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

for references in articles please use BRENDA:EC1.14.14.27
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The enzyme appears in viruses and cellular organisms

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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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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gamma-resorcylate degradation I
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Benzoate degradation
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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).
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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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
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
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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
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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-
?
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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)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.6
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pH 6.8, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
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gel filtration
70000
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1 * 70000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45500, oxygenase components of resorcinol hydroxylase, SDS-PAGE
monomer
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.14.27)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)