Information on EC 3.7.1.19 - 2,6-dihydroxypseudooxynicotine hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.7.1.19
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RECOMMENDED NAME
GeneOntology No.
2,6-dihydroxypseudooxynicotine hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O = 2,6-dihydroxypyridine + 4-methylaminobutanoate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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Nicotinate and nicotinamide metabolism
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nicotine degradation I (pyridine pathway)
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SYSTEMATIC NAME
IUBMB Comments
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one hydrolase
The enzyme, characterized from the soil bacterium Arthrobacter nicotinovorans, participates in nicotine degradation.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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-dihydroxypseudooxynicotine + H2O
2,6-dihydroxypyridine + 4-methylaminobutanoate
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
2,6-dihydroxypseudooxynicotine
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in 75 mM phosphate buffer, pH 7.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
792
2,6-dihydroxypseudooxynicotine
Paenarthrobacter nicotinovorans
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in 75 mM phosphate buffer, pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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gel filtration
43555
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1 * 43555, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 43000, SDS-PAGE; 1 * 43555, calculated from amino acid sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-chelating Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL-1 Blue cells
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