Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.13.10 - 2,6-dihydroxypyridine 3-monooxygenase and Organism(s) Paenarthrobacter nicotinovorans and UniProt Accession Q93NG3

for references in articles please use BRENDA:EC1.14.13.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A flavoprotein.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Paenarthrobacter nicotinovorans
UNIPROT: Q93NG3
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Paenarthrobacter nicotinovorans
The enzyme appears in selected viruses and cellular organisms
Synonyms
2,6-dihydroxypyridine hydroxylase, 2,6-dihydroxypyridine-3-hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,6-dihydroxypyridine hydroxylase
-
2,6-dihydroxypyridine-3-hydroxylase
-
2,6-dihydroxypyridine oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
hydroxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
39279-38-4
-
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
-
methylene blue and 2,6-dichlorophenol-indophenol can act as alternative electron acceptors
-
-
?
2,6-dihydroxypyridine + NADH + O2
2,3,6-trihydroxypyridine + NAD+ + H2O
show the reaction diagram
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + O2
2,3,6-trihydroxypyridine + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
less effective than NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dihydroxypyridine
-
100% inhibition at 0.1 mM, irreversible inhibitor
2,6-dihydroxynicotinamide
-
55% inhibition at 0.1 mM, reversible inhibitor
2,6-dimethoxypyridine
-
100% inhibition at 0.1 mM, irreversible inhibitor
2-Hydroxypyridine
-
48% inhibition at 0.1 mM, reversible inhibitor
Cu2+
-
50% inhibition at 0.017 mM
Hg2+
-
50% inhibition at 0.005 mM
NaN3
-
50% inhibition at 2 mM
p-chloromercuribenzoate
-
50% inhibition at 0.01 mM
resorcine
-
51% inhibition at 0.1 mM, reversible inhibitor
Zn2+
-
50% inhibition at 0.7 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
38% activation at 0.05 mM
KCN
-
18% activation at 0.5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
2,6-Dihydroxypyridine
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHPH_PAENI
397
0
43400
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43400
2 * 43400, crystal structure
89000
-
sucrose density gradient centrifugation
90000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 43400, crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C323S
mutation did not cause any relevant structural disturbance
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
most stable in 50 mM potassium phosphate buffer
439040
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
30% loss of activity in 10 min
30
-
complete loss of activity in 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 1.5 M guanidinium hydrochloride removes FAD, no renaturation possible
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
complete loss of activity
Ethanol
-
stabilizes during preparative manipulations
Glycerol
-
stabilizes during preparative manipulations
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tag, expressed in Escherichia coli
expressed in Escherichia coli XL-1 blue
-
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baitsch, D.; Sandu, C.; Brandsch, R.; Igloi, G.L.
Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of 2,6-dihydroxypyridine 3-hydroxylase
J. Bacteriol.
183
5262-5267
2001
Paenarthrobacter nicotinovorans
Manually annotated by BRENDA team
Holmes, P.E.; Rittenberg, S.C.
The bacterial oxidation of nicotine. VII. Partial purification and properties of 2,6-dihydroxypyridine oxidase
J. Biol. Chem.
247
7622-7627
1972
Paenarthrobacter nicotinovorans
Manually annotated by BRENDA team
Holmes, P.E.; Rittenberg, S.C.; Knackmuss, H.J.
The bacterial oxidation of nicotine. 8. Synthesis of 2,3,6-trihydroxypyridine and accumulation and partial characterization of the product of 2,6-dihydroxypyridine oxidation
J. Biol. Chem.
247
7628-7633
1972
Paenarthrobacter nicotinovorans
Manually annotated by BRENDA team
Ganas, P.; Sachelaru, P.; Mihasan, M.; Igloi, G.L.; Brandsch, R.
Two closely related pathways of nicotine catabolism in Arthrobacter nicotinovorans and Nocardioides sp. strain JS614
Arch. Microbiol.
189
511-517
2008
Nocardioides sp. (A1SE94), Nocardioides sp. JS614 / ATCC BAA-499 (A1SE94), Paenarthrobacter nicotinovorans (Q93NG3), Paenarthrobacter nicotinovorans
Manually annotated by BRENDA team
Treiber, N.; Schulz, G.
Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading pathway
J. Mol. Biol.
379
94-104
2008
Paenarthrobacter nicotinovorans (Q93NG3), Paenarthrobacter nicotinovorans
Manually annotated by BRENDA team