Information on EC 1.6.6.9 - trimethylamine-N-oxide reductase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.6.6.9
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RECOMMENDED NAME
GeneOntology No.
trimethylamine-N-oxide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + trimethylamine N-oxide = NAD+ + trimethylamine + H2O
show the reaction diagram
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Methane metabolism
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Microbial metabolism in diverse environments
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-
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SYSTEMATIC NAME
IUBMB Comments
NADH:trimethylamine-N-oxide oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37256-34-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
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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
NADH + H+ + trimethylamine N-oxide
NAD+ + trimethylamine + H2O
show the reaction diagram
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-
-
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
show the reaction diagram
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NADH as electron donor
-
?
[Mo(IV)O(maleonitriledithiolate)(benzenethiolate)]2- + trimethylamine N-oxide
? + trimethylamine + H2O
show the reaction diagram
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-
-
-
?
[Mo(IV)O(maleonitriledithiolate)(dimethylethylenedicarboxylatedithiolate)]2- + trimethylamine N-oxide
? + trimethylamine + H2O
show the reaction diagram
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-
-
-
?
[Mo(IV)O(maleonitriledithiolate)(toluenedithiolate)]2- + trimethylamine N-oxide
? + trimethylamine + H2O
show the reaction diagram
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-
-
-
?
additional information
?
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADH + H+ + trimethylamine N-oxide
NAD+ + trimethylamine + H2O
show the reaction diagram
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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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stimulation
FMN
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stimulation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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slight stimulation by Fe3+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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2,2-dipyridyl
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97% inhibition at 1 mM
8-hydroxyquinoline
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slight
Co2+
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30% inhibition at 1 mM
Cupferron
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82% inhibition at 1 mM
CuSO4
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6% inhibition at 0.01 mM with 0.1 mM sodium diethyldithiocarbamate
Fe2+
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30% inhibition at 0.1 mM
hydroxylamine
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17% inhibition at 1 mM
iodoacetate
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partial
KCN
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not inhibitory
Mn2+
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24% inhibition at 1 mM
Mo6+
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18% inhibition at 1 mM
NADH
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slight inhibition at 14 mM
NaN3
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not inhibitory
Ni2+
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27% inhibition at 1 mM
p-chloromercuribenzoate
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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
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30% inhibition at 1 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
Trimethylamine N-oxide
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additional information
additional information
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reaction Michaelis-Menten saturation kinetics, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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pH 6.0: about 35% of activity maximum, pH 8.0: about 80% of activity maximum
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme associated with the membrane portion of lysed spheroplasts
Manually annotated by BRENDA team
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol protects against inactivation during preparation of cell extract, ineffective as stabilizer during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 30% loss of activity after 24 hours, 50% loss of activity after 48 hours
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2°C, 30% loss of activity after 24 hours, 50% loss of activity after 48 hours
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
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Show AA Sequence (159 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.6.6.9)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)