Information on EC 1.6.6.9 - trimethylamine-N-oxide reductase

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The expected taxonomic range for this enzyme is: Gammaproteobacteria

EC NUMBER
COMMENTARY
1.6.6.9
-
RECOMMENDED NAME
GeneOntology No.
trimethylamine-N-oxide reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NADH + H+ + trimethylamine N-oxide = NAD+ + trimethylamine + H2O
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Methane metabolism
-
Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
NADH:trimethylamine-N-oxide oxidoreductase
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
reductase, trimethylamine N-oxide
-
-
-
-
TMAO reductase
-
-
-
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TOR
-
-
-
-
trimethylamine N-oxide reductase
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-
-
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trimethylamine oxide reductase
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-
-
-
trimethylamine-N-oxide reductase
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-
CAS REGISTRY NUMBER
COMMENTARY
37256-34-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
in dead fish the nonavailability of oxygen induces the enteric bacteria, Echerichia coli, to change their respiration from aerobic to anaerobic under trimethylamine N-oxide The induced enzyme, trimethylamine N-oxide reductase of Escherichia coli, uses trimethylamine N-oxide as the terminal electron acceptor instead of oxygen
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NADH + H+ + trimethylamine N-oxide
NAD+ + trimethylamine + H2O
show the reaction diagram
-
-
-
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
-
NADH as electron donor
-
?
[MoIVO(benzenedithiolate)(dimethylethylenedicarboxylate)]2 + trimethylamine N-oxide
? + trimethylamine + H2O
show the reaction diagram
-
-
-
-
?
[MoIVO(maleonitriledithiolate)(dimethylethylenedicarboxylate)]2 + trimethylamine N-oxide
? + trimethylamine + H2O
show the reaction diagram
-
-
-
-
?
[MoIVO(toluenedithiolate)(dimethylethylenedicarboxylate)]2 + trimethylamine N-oxide
? + trimethylamine + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
synthesis of three complexes, i.e. [MoIVO(maleonitriledithiolate)(dimethylethylenedicarboxylate)]2, [MoIVO(benzenedithiolate)(dimethylethylenedicarboxylate)]2, and [MoIVO(toluenedithiolate)(dimethylethylenedicarboxylate)]2, each possessing two different dithiolene ligands. The complexes reduce trimethylamine-N-oxide, the biological substrate of trimethylamine-N-oxide reductase, to trimethylamine, responsible for the fishy smell of dead aquatic animals, overview. These complexes follow the Michaelis? Menten saturation kinetics
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADH + H+ + trimethylamine N-oxide
NAD+ + trimethylamine + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Iron
-
slight stimulation by Fe3+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2,2-dipyridyl
-
97% inhibition at 1 mM
8-hydroxyquinoline
-
slight
Co2+
-
30% inhibition at 1 mM
Cupferron
-
82% inhibition at 1 mM
CuSO4
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6% inhibition at 0.01 mM with 0.1 mM sodium diethyldithiocarbamate
Fe2+
-
30% inhibition at 0.1 mM
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hydroxylamine
-
17% inhibition at 1 mM
iodoacetate
-
partial
KCN
-
not inhibitory
Mn2+
-
24% inhibition at 1 mM
Mo6+
-
18% inhibition at 1 mM
NADH
-
slight inhibition at 14 mM
NaN3
-
not inhibitory
Ni2+
-
27% inhibition at 1 mM
p-chloromercuribenzoate
-
100% inhibition at 0.3 mM, 70% inhibition at 0.01 mM, 13% inhibition at 0.01 mM with 0.2 mM 2-mercaptoethanol
Semicarbazide
-
30% inhibition at 1 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.7
-
Trimethylamine N-oxide
-
-
additional information
-
additional information
-
reaction Michaelis-Menten saturation kinetics, overview
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
pH 6.0: about 35% of activity maximum, pH 8.0: about 80% of activity maximum
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme associated with the membrane portion of lysed spheroplasts
Manually annotated by BRENDA team
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol protects against inactivation during preparation of cell extract, ineffective as stabilizer during storage
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, 30% loss of activity after 24 hours, 50% loss of activity after 48 hours
-
2°C, 30% loss of activity after 24 hours, 50% loss of activity after 48 hours
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
three complexes, i.e. [MoIVO(maleonitriledithiolate)(dimethylethylenedicarboxylate)]2, [MoIVO(benzenedithiolate)(dimethylethylenedicarboxylate)]2, and [MoIVO(toluenedithiolate)(dimethylethylenedicarboxylate)]2, each possessing two different dithiolene ligands, are synthesized as model of trimethylamine-N-oxide reductase