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Information on EC 1.7.2.3 - trimethylamine-N-oxide reductase
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1.7.2.3 trimethylamine-N-oxide reductaseIUBMB Comments
Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
tmao reductase, trimethylamine n-oxide reductase, trimethylamine-n-oxide reductase, torecad, trimethylamine oxide reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.6.6.9
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formerly
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reductase, trimethylamine N-oxide
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TMAO reductase
TOR
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TorA
TorD
TorZ
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trimethylamine N-oxide reductase
trimethylamine oxide reductase
additional information
TMAO reductase
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TorA
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trimethylamine oxide reductase
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additional information
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two other genes (torYZ and dmsABC) coding for enzymes with trimethylamine-N-oxide reductase function identified, but they are much less active than the torECA gene, experimental data suggest that torECA encodes the major TMAO reductase under laboratory culture conditions and that TorYZ and DmsABC do not significantly contribute to trimethylamine-N-oxide reduction
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
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-
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trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
molybdenum serves as electron donor within the enzyme, enzyme-MoIV + (CH3)3NdO + 2H+ = enzyme-MoVI + (CH3)3N + H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
trimethylamine:cytochrome c oxidoreductase
Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide.
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CAS REGISTRY NUMBER
COMMENTARY
37256-34-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloropyridine N-oxide + electron donor
2-chloropyridine + oxidized electron donor + H2O
-
-
-
?
3-hydroxypyridine N-oxide + electron donor
3-hydroxypyridine + oxidized electron donor + H2O
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-
-
?
3-picoline N-oxide + electron donor
3-picoline + oxidized electron donor + H2O
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-
-
?
4-chloropyridine N-oxide + electron donor
4-chloropyridine + oxidized electron donor + H2O
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-
-
?
4-methylmorpholine N-oxide + electron donor
4-methylmorpholine + oxidized electron donor + H2O
4-methylmorpholine-N-oxide + (ferrocytochrome c)-subunit + H+
4-methylmorpholine + (ferricytochrome c)-subunit + H2O
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-
-
-
?
biotin sulfoxide + (ferrocytochrome c)-subunit
? + (ferrocytochrome c)-subunit
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-
-
-
?
bromate + (ferrocytochrome c)-subunit
? + (ferricytochrome c)-subunit
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-
-
-
?
dimethylsulfoxide + (ferrocytochrome c)-subunit + 2 H+
dimethylsulfide + (ferricytochrome c)-subunit + H2O
hydroxylamine + (ferrocytochrome c)-subunit
? + (ferricytochrome c)-subunit
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-
-
-
?
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine + H2O + oxidized electron donor
N,N-dimethylhexylamine N-oxide + electron donor
N,N-dimethylhexylamine + oxidized electron donor + H2O
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-
-
?
N-cyclohexyldimethylamine N-oxide + electron donor
N-cyclohexyldimethylamine + oxidized electron donor + H2O
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-
-
?
nicotinic acid N-oxide + (ferrocytochrome c)-subunit + H+
nicotinic acid + (ferricytochrome c)-subunit + H2O
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-
-
-
?
picoline N-oxide + (ferrocytochrome c)-subunit + H+
picoline + (ferricytochrome c)-subunit + H2O
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-
-
-
?
tetramethylene sulfoxide + (ferrocytochrome c)-subunit + H+
? + (ferricytochrome c)-subunit
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-
-
-
?
tetramethylene sulfoxide + electron donor
tetrahydrothiophene + oxidized electron donor + H2O
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tungsten-substituted enzyme
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
trimethylamine N-oxide + benzyl viologen + H+
trimethylamine + oxidized benzyl viologen + H2O
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-
-
-
?
trimethylamine N-oxide + oxidized benzyl viologen + 2 H+
trimethylamine + reduced benzyl viologen + H2O
trimethylamine N-oxide + oxidized benzyl viologen + H+
trimethylamine + reduced benzyl viologen + H2O
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-
-
-
r
trimethylamine N-oxide + oxidized methyl viologen + H+
trimethylamine + reduced methyl viologen + H2O
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r
trimethylamine-N-oxide + enzyme-MoIV
trimethylamine + enzyme-MoVI + H2O
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anaerobic respiration
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?
4-methylmorpholine N-oxide + electron donor
4-methylmorpholine + oxidized electron donor + H2O
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good substrate
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?
4-methylmorpholine N-oxide + electron donor
4-methylmorpholine + oxidized electron donor + H2O
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wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme
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?
4-methylmorpholine N-oxide + electron donor
4-methylmorpholine + oxidized electron donor + H2O
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-
?
adenosine N-oxide + electron donor
adenosine + H2O + oxidized electron donor
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-
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?
adenosine N-oxide + electron donor
adenosine + H2O + oxidized electron donor
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40% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 35% relative activity to trimethylamine N-oxide with the purified enzyme
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?
alpha-picoline N-oxide + electron donor
alpha-picoline + H2O + oxidized electron donor
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?
alpha-picoline N-oxide + electron donor
alpha-picoline + H2O + oxidized electron donor
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-
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?
alpha-picoline N-oxide + electron donor
alpha-picoline + H2O + oxidized electron donor
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wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme
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?
alpha-picoline N-oxide + electron donor
alpha-picoline + H2O + oxidized electron donor
alpha-picoline N-oxide is not an efficient substrate for the enzyme
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?
chlorate + electron donor
?
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?
dimethylsulfoxide + (ferrocytochrome c)-subunit + 2 H+
dimethylsulfide + (ferricytochrome c)-subunit + H2O
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-
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?
dimethylsulfoxide + (ferrocytochrome c)-subunit + 2 H+
dimethylsulfide + (ferricytochrome c)-subunit + H2O
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-
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?
dimethylsulfoxide + electron donor
? + oxidized electron donor + H2O
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tungsten-substituted enzyme
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?
dimethylsulfoxide + electron donor
? + oxidized electron donor + H2O
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?
dimethylsulfoxide + electron donor
? + oxidized electron donor + H2O
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9% relative activity to trimethylamine N-oxide
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?
dimethylsulfoxide + electron donor
? + oxidized electron donor + H2O
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?
diphenylsulfoxide + electron donor
diphenylsulfide + oxidized electron donor + H2O
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tungsten-substituted enzyme
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?
diphenylsulfoxide + electron donor
diphenylsulfide + oxidized electron donor + H2O
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-
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?
gamma-picoline N-oxide + electron donor
gamma-picoline + H2O + oxidized electron donor
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-
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?
gamma-picoline N-oxide + electron donor
gamma-picoline + H2O + oxidized electron donor
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wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme
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?
gamma-picoline N-oxide + electron donor
gamma-picoline + H2O + oxidized electron donor
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11% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 12% relative activity to trimethylamine N-oxide with the purified enzyme
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?
hydroxylamine N-oxide + electron donor
hydroxylamine + H2O + oxidized electron donor
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?
hydroxylamine N-oxide + electron donor
hydroxylamine + H2O + oxidized electron donor
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?
hydroxylamine N-oxide + electron donor
hydroxylamine + H2O + oxidized electron donor
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?
hydroxylamine N-oxide + electron donor
hydroxylamine + H2O + oxidized electron donor
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wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme
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?
hydroxylamine N-oxide + electron donor
hydroxylamine + H2O + oxidized electron donor
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19% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 3% relative activity to trimethylamine N-oxide with the purified enzyme
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?
L-methionine sulfoxide + electron donor
L-methionine + oxidized electron donor + H2O
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26% relative activity to trimethylamine N-oxide
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?
L-methionine sulfoxide + electron donor
L-methionine + oxidized electron donor + H2O
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?
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine + H2O + oxidized electron donor
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-
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?
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine + H2O + oxidized electron donor
N,N-dimethyldodecylamine N-oxide is not an efficient substrate for the enzyme
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?
N,N-dimethyldodecylamine N-oxide + electron donor
N,N-dimethyldodecylamine + H2O + oxidized electron donor
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63% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 41% relative activity to trimethylamine N-oxide with the purified enzyme
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?
pyridine N-oxide + electron donor
pyridine + oxidized electron donor + H2O
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-
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?
pyridine N-oxide + electron donor
pyridine + oxidized electron donor + H2O
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wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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cytochrome c, cytochrome b-c1 and cytochrome c551 can act as electron donors
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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cytochrome c, cytochrome b-c1 and cytochrome c551 can act as electron donors
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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reaction mechanism
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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reduction of trimethylamine N-oxide is catalyzed by at least 2 enzymes: trimethylamine N-oxide reductase and dimethyl sulfoxide reductase
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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-
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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enzyme forms a functional association with cytochrome c-556
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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trimethylamine N-oxide reductase and dimethyl sulfoxide reductase are identical enzymes
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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cytochrome c2, cytochrome c552 and methylviologen can serve as electron donors
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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-
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?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
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-
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?
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
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-
-
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?
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
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-
-
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
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methyl viologen as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
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formate as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
methyl viologen as electron donor
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-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
formate as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
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quinone as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
NADH as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
NADH as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
NADH as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
NADH as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
methyl viologen as electron donor
-
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
methyl viologen as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
vitamin K5 or FMN as electron donors
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
the activity with 3.4 mM FMN is 17% of that obtained with 0.33 mM benzyl viologen
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
NADH as electron donor
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?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
methyl viologen as electron donor
-
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
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reduced methylene blue, reduced N-methylphenazonium methosulfate as electron donors
-
-
?
trimethylamine N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
benzyl viologen as electron donor
-
-
?
trimethylamine N-oxide + NADH
NAD+ + trimethylamine + H2O
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enzyme is highly specific for trimethylamine oxide as alternative terminal electron acceptor
-
-
?
trimethylamine N-oxide + NADH
NAD+ + trimethylamine + H2O
-
enzyme is highly specific for trimethylamine oxide as electron acceptor
trimethylamine is volatile
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?
trimethylamine N-oxide + oxidized benzyl viologen + 2 H+
trimethylamine + reduced benzyl viologen + H2O
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-
-
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?
trimethylamine N-oxide + oxidized benzyl viologen + 2 H+
trimethylamine + reduced benzyl viologen + H2O
Vibrio fluvialis ATCC33809
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-
-
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?
trimethylamine N-oxide + oxidized benzyl viologen + 2 H+
trimethylamine + reduced benzyl viologen + H2O
Vibrio fluvialis QY27
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-
-
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
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anaerobic respiration
-
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
anaerobic respiration
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
cytochrome 554,557 may be the physiological electron donor
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
cytochrome c-556 may be the physiological electron donor
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
-
?
additional information
?
-
-
other electron acceptors: nitrate and fumarate
-
-
?
additional information
?
-
-
the enzyme binds to the trimethylamine oxide reductase TorA apoenzyme, EC 1.6.6.9, recognizing a signal peptide, and allows TorA to bind the essential molybdenum cofactor for transport from the periplasm across the cytoplasmic membrane, TorD is not involved in the transport itself, TorD has a regulatory and controlling function on TorA assembly
-
-
?
additional information
?
-
-
TorD chaperone is a chaperone of trimethylamine oxide reductase, EC 1.6.6.9, addition of the chaperone activates the TorA apoenzyme up to 4fold, allowing its maturation, in absence or presence of the TorA molybdenum cofactor, TorD modifies the TorA apoenzyme conformation in absence of the cofactor, probably making the apoenzyme competent for cofactor binding, binding study
-
-
?
additional information
?
-
-
TorD is an essentially required chaperone for cofactor binding and enzyme maturation of the trimethylamine oxide reductase TorA, EC 1.6.6.9, in absence of TorD at 42°C, the TorA is poorly maturated and almost completely degraded, at elevated temperatures above 37°C TorD prevents the missfolding of TorA apoenzyme before molybdenum cofactor binding, temperature-dependent effect
-
-
?
additional information
?
-
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the enzyme performs trimethylamine oxide reduction during aerobiosis, in the absence of oxygen, Escherichia coli can use alternative exogenous electron acceptors, including trimethylamine oxide, to generate energy, regulation, overview
-
-
?
additional information
?
-
-
the enzyme performs trimethylamine oxide reduction
-
-
?
additional information
?
-
-
the TMAO reductase active site can exist in multiple forms, molecular modelling, overview
-
-
?
additional information
?
-
-
a single enzyme responsible for both trimethylamine N-oxide and dimethylsulfoxide reductase
-
-
?
additional information
?
-
-
a single enzyme responsible for both trimethylamine N-oxide and dimethylsulfoxide reductase
-
-
?
additional information
?
-
-
nitrate does not act as electron acceptor
-
-
?
additional information
?
-
-
when FMN, FAD, cytochrome c, NADPH, NADH or ascorbate are substituted at equimolar concentration for benzyl viologen, none facilitates the oxidation of dithionite by the trimethylamine N-oxide
-
-
?
additional information
?
-
-
the enzyme has very slight activity with nitrate, but no activity with nitrite, sulfite or thiosulfate
-
-
?
additional information
?
-
-
enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently
-
-
?
additional information
?
-
-
regulator TorR and sensor TorS, encoded by genes torR and torS in the same operon as torA, are required for the trimethylamine oxide respiration pathway
-
-
?
additional information
?
-
-
no activity with FADH2, NADH, NADPH and the reduced forms of methylene blue and N-methylphenazonium methosulphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
trimethylamine N-oxide + NADH
NAD+ + trimethylamine + H2O
-
enzyme is highly specific for trimethylamine oxide as alternative terminal electron acceptor
-
-
?
trimethylamine-N-oxide + enzyme-MoIV
trimethylamine + enzyme-MoVI + H2O
-
anaerobic respiration
-
-
?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
-
reaction mechanism
-
-
?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
-
reduction of trimethylamine N-oxide is catalyzed by at least 2 enzymes: trimethylamine N-oxide reductase and dimethyl sulfoxide reductase
-
-
?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
-
trimethylamine N-oxide reductase and dimethyl sulfoxide reductase are identical enzymes
-
-
?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
-
-
-
?
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+
trimethylamine + (ferricytochrome c)-subunit + H2O
-
-
-
?
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
-
-
-
-
?
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
-
-
-
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
anaerobic respiration
-
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
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anaerobic respiration
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
cytochrome 554,557 may be the physiological electron donor
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
cytochrome c-556 may be the physiological electron donor
-
?
trimethylamine-N-oxide + electron donor
trimethylamine + oxidized electron donor + H2O
-
-
?
additional information
?
-
-
the enzyme binds to the trimethylamine oxide reductase TorA apoenzyme, EC 1.6.6.9, recognizing a signal peptide, and allows TorA to bind the essential molybdenum cofactor for transport from the periplasm across the cytoplasmic membrane, TorD is not involved in the transport itself, TorD has a regulatory and controlling function on TorA assembly
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-
?
additional information
?
-
-
TorD chaperone is a chaperone of trimethylamine oxide reductase, EC 1.6.6.9, addition of the chaperone activates the TorA apoenzyme up to 4fold, allowing its maturation, in absence or presence of the TorA molybdenum cofactor, TorD modifies the TorA apoenzyme conformation in absence of the cofactor, probably making the apoenzyme competent for cofactor binding, binding study
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-
?
additional information
?
-
-
TorD is an essentially required chaperone for cofactor binding and enzyme maturation of the trimethylamine oxide reductase TorA, EC 1.6.6.9, in absence of TorD at 42°C, the TorA is poorly maturated and almost completely degraded, at elevated temperatures above 37°C TorD prevents the missfolding of TorA apoenzyme before molybdenum cofactor binding, temperature-dependent effect
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-
?
additional information
?
-
-
the enzyme performs trimethylamine oxide reduction during aerobiosis, in the absence of oxygen, Escherichia coli can use alternative exogenous electron acceptors, including trimethylamine oxide, to generate energy, regulation, overview
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-
?
additional information
?
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enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently
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-
?
additional information
?
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regulator TorR and sensor TorS, encoded by genes torR and torS in the same operon as torA, are required for the trimethylamine oxide respiration pathway
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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the enzyme contains more than 0.4 atoms of acid-labile sulfur per molecular weight of 200000
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cytochrome c
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c-type cytochrome Tor C is required for electron transfer to terminal enzyme Tor A
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Molybdenum
molybdopterin
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in the molybdopterin molybdenum cofactor, Mo-S and Mo-O interactions, molecular structure modelling, overview
Molybdenum
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in vivo tungsten substitution of the molybdoenzyme, 0.89 atoms of tungsten per mol of purified enzyme
Molybdenum
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involved in the catalytic mechanism, experimental data suggest that the active site of TMAO reductase with bound molybdenum can exist in three different forms
Molybdenum
-
deduced from inhibition of enzyme synthesis by tungstate and reduction of enzyme levels in charcoal-treated media
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE