Information on EC 1.14.12.16 - 2-Hydroxyquinoline 5,6-dioxygenase

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The expected taxonomic range for this enzyme is: Comamonas testosteroni

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EC NUMBER
COMMENTARY hide
1.14.12.16
-
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RECOMMENDED NAME
GeneOntology No.
2-Hydroxyquinoline 5,6-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
quinolin-2-ol + NADH + H+ + O2 = 2,5,6-trihydroxy-5,6-dihydroquinoline + NAD+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-methylquinoline degradation
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-
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SYSTEMATIC NAME
IUBMB Comments
quinolin-2-ol,NADH:oxygen oxidoreductase (5,6-hydroxylating)
3-Methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also substrates. Quinolin-2-ols exist largely as their quinolin-2(1H)-one tautomers
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CAS REGISTRY NUMBER
COMMENTARY hide
172399-50-7
not distinguished from EC 1.14.13.65
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
2-Oxo-1,2-dihydroquinoline + NADH + O2
?
show the reaction diagram
3-Methyl-2-oxo-1,2-dihydroquinoline + NADH + O2
5,6-Dihydro-5,6-dihydroxy-(3-methyl-)2-oxo-1,2-dihydroquinoline + NAD+
show the reaction diagram
6-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
?
show the reaction diagram
8-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
?
show the reaction diagram
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-
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8-Hydroxyquinoline + NADH + O2
?
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
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
required, cannot be replaced by NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
enhances activity 1.5fold
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
0.5 mM, 82% loss of activity
4-hydroxymercuribenzoate
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0.1 mM, complete loss of activity
Acriflavin
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0.5 mM, 69% loss of activity
diethyldithiocarbaminate
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inhibits after a prolonged incubation time
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EDTA
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inhibits after a prolonged incubation time
iodoacetate
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2 mM, complete loss of activity
NaCl
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0.2 M, 50% loss of activity
Quinacrine
-
0.5 mM, 15% loss of activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
5 min, 30% loss of activity
65
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5 min, complete loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithioerythritol, dithiothreitol and 2-oxo-1,2-dihydroquinoline stabilize
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.12.16)
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)