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Information on EC 3.7.1.19 - 2,6-dihydroxypseudooxynicotine hydrolase and Organism(s) Paenarthrobacter nicotinovorans and UniProt Accession Q93NG6

for references in articles please use BRENDA:EC3.7.1.19
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EC Tree
     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.19 2,6-dihydroxypseudooxynicotine hydrolase
IUBMB Comments
The enzyme, characterized from the soil bacterium Arthrobacter nicotinovorans, participates in nicotine degradation.
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This record set is specific for:
Paenarthrobacter nicotinovorans
UNIPROT: Q93NG6
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The taxonomic range for the selected organisms is: Paenarthrobacter nicotinovorans
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
2,6-dihydroxy-pseudo-oxynicotine hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,6-dihydroxy-pseudo-oxynicotine hydrolase
-
2,6-dihydroxypseudooxynicotine hydrolase
-
-
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.
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
-
-
-
?
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
-
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
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHPON_PAENI
367
0
40995
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
gel filtration
43555
-
1 * 43555, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-chelating Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL-1 Blue cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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., Nocardioides sp. JS614 / ATCC BAA-499, Paenarthrobacter nicotinovorans (Q93NG6), Paenarthrobacter nicotinovorans
Manually annotated by BRENDA team
Sachelaru, P.; Schiltz, E.; Igloi, G.L.; Brandsch, R.
An alpha/beta-fold C-C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans
J. Bacteriol.
187
8516-8519
2005
Paenarthrobacter nicotinovorans
Manually annotated by BRENDA team