Information on EC 1.14.13.10 - 2,6-dihydroxypyridine 3-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.10
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RECOMMENDED NAME
GeneOntology No.
2,6-dihydroxypyridine 3-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,6-dihydroxypyridine + NADH + H+ + O2 = 2,3,6-trihydroxypyridine + NAD+ + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxylation
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oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nicotine degradation I (pyridine pathway)
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Nicotinate and nicotinamide metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
39279-38-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JS614
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,6-dihydroxypyridine + NADH + electron acceptor
2,3,6-trihydroxypyridine + NAD+ + reduced electron acceptor
show the reaction diagram
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methylene blue and 2,6-dichlorophenol-indophenol can act as alternative electron acceptors
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?
2,6-dihydroxypyridine + NADH + O2
2,3,6-trihydroxypyridine + NAD+ + H2O
show the reaction diagram
additional information
?
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2-hydroxypyridine, 3-hydroxypyridine, 4-hydroxypyridine, 2,5-dihydroxypyridine, 2,6-dipicolinic acid, p-hydroxybenzoic acid, nicotinic acid and nicotine are no substrates for this enzyme
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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
2,6-dihydroxypyridine + NADH + O2
2,3,6-trihydroxypyridine + NAD+ + H2O
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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less effective than NADH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dihydroxypyridine
2,6-dihydroxynicotinamide
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55% inhibition at 0.1 mM, reversible inhibitor
2,6-dimethoxypyridine
2-Hydroxypyridine
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48% inhibition at 0.1 mM, reversible inhibitor
Cu2+
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50% inhibition at 0.017 mM
Hg2+
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50% inhibition at 0.005 mM
NaN3
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50% inhibition at 2 mM
p-chloromercuribenzoate
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50% inhibition at 0.01 mM
resorcine
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51% inhibition at 0.1 mM, reversible inhibitor
Zn2+
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50% inhibition at 0.7 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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38% activation at 0.05 mM
KCN
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18% activation at 0.5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
2,6-Dihydroxypyridine
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pH 8, 20°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Arthrobacter nicotinovorans
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
89000
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sucrose density gradient centrifugation
90000
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gel filtration
113000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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most stable in 50 mM potassium phosphate buffer
439040
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
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30% loss of activity in 10 min
30
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complete loss of activity in 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 1.5 M guanidinium hydrochloride removes FAD, no renaturation possible
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
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complete loss of activity
Ethanol
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stabilizes during preparative manipulations
Glycerol
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stabilizes during preparative manipulations
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL-1 blue
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His-tag, expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C323S
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mutation did not cause any relevant structural disturbance
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
after removal of FAD through precipitation with 50% (NH4)2SO4 at pH 2.0, incubation with 0.1 mM FAD leeds to 90% activity recovery
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