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Information on EC 1.5.99.4 - nicotine dehydrogenase and Organism(s) Pseudomonas sp. HZN6 and UniProt Accession M4T5L3

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EC Tree
IUBMB Comments
A metalloprotein (FMN). The enzyme can act on both the naturally found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine, with retention of configuration in both cases .
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This record set is specific for:
Pseudomonas sp. HZN6
UNIPROT: M4T5L3
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The taxonomic range for the selected organisms is: Pseudomonas sp. HZN6
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nicotinic acid hydroxylase, nicotine dehydrogenase, ndhab, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-nicotine oxidase
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nicotine dehydrogenase
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nicotine oxidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
nicotine:acceptor 6-oxidoreductase (hydroxylating)
A metalloprotein (FMN). The enzyme can act on both the naturally found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine, with retention of configuration in both cases [4].
CAS REGISTRY NUMBER
COMMENTARY hide
37256-31-8
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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
(RS)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
show the reaction diagram
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
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?
(S)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
show the reaction diagram
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
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-
?
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
(S)-nicotine + acceptor + H2O
pseudooxynicotine + reduced acceptor
show the reaction diagram
via N-methylmyosmine, which then spontaneously hydrolyzes to pseudooxynicotine. The two enantiomers are degraded at approximately the same rate, indicating that NOX does not show chiral selectivity
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene nox
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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a nox disruption mutant of strain HZN6 loses the ability to degrade nicotine, but not pseudooxynicotine
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metabolism
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the enzyme is responsible for the first step of nicotine degradation
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physiological function
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the enzyme nonenantioselectively degrades nicotine to pseudooxynicotine
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additional information
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the conserved FAD-binding GXGXXG motif and His456 are essential for nicotine degradation activity
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
M4T5L3_9PSED
478
0
52226
TrEMBL
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H456R
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site-directed mutagenesis
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additional information
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construction of the nox deletion mutant strain, that loses the ability to degrade nicotine, but not pseudooxynicotine
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Qiu, J.; Ma, Y.; Zhang, J.; Wen, Y.; Liu, W.
Cloning of a novel nicotine oxidase gene from Pseudomonas sp. strain HZN6 whose product nonenantioselectively degrades nicotine to pseudooxynicotine
Appl. Environ. Microbiol.
79
2164-2171
2013
no activity in Escherichia coli strain DH5alpha, no activity in Pseudomonas putida strain KT2440, Pseudomonas sp. (M4T5L3), Pseudomonas sp. HZN6 (M4T5L3)
Manually annotated by BRENDA team