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

for references in articles please use BRENDA:EC1.14.13.10
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.13.10
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RECOMMENDED NAME
GeneOntology No.
2,6-dihydroxypyridine 3-monooxygenase
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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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-
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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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-
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
39279-38-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
Nocardioides sp. JS614 / ATCC BAA-499
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SwissProt
Manually annotated by BRENDA team
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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
2,6-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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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
less effective than NADH
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
38% activation at 0.05 mM
KCN
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18% activation at 0.5 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
2,6-Dihydroxypyridine
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pH 8, 20°C
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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 OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43400
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2 * 43400, crystal structure
89000
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sucrose density gradient centrifugation
90000
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gel filtration
113000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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most stable in 50 mM potassium phosphate buffer
439040
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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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.10)
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)