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Information on EC 4.1.2.32 - trimethylamine-oxide aldolase
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4.1.2.32 trimethylamine-oxide aldolaseSpecify your search results
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
tmaoase, trimethylamine-n-oxide demethylase, tmao demethylase, trimethylamine n-oxide demethylase, trimethylamine oxide aldolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TMAO demethylase
-
-
-
-
TMAOase
Trimethylamine N-oxide aldolase
-
-
-
-
Trimethylamine N-oxide demethylase
-
-
-
-
Trimethylamine N-oxide formaldehyde-lyase
-
-
-
-
trimethylamine oxide aldolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trimethylamine N-oxide = dimethylamine + formaldehyde
-
-
-
-
trimethylamine N-oxide = dimethylamine + formaldehyde
non-oxidative, non-hydrolytic cleavage
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
retro aldol-condensation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
trimethylamine-N-oxide formaldehyde-lyase (dimethylamine-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
72561-08-1
-
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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
(+)-Propoxyphene N-oxide
?
-
5% of the activity with trimethylamine N-oxide
-
-
?
(+)-Propoxyphene N-oxide
?
-
5% of the activity with trimethylamine N-oxide
-
-
?
Benzyldimethylamine N-oxide
?
-
50% of the activity with trimethylamine N-oxide
-
-
?
Benzyldimethylamine N-oxide
?
-
5% of the activity with trimethylamine N-oxide
-
-
?
Benzyldimethylamine N-oxide
?
-
5% of the activity with trimethylamine N-oxide
-
-
?
Chlorpromazine N-oxide
?
-
5% of the activity with trimethylamine N-oxide
-
-
?
Chlorpromazine N-oxide
?
-
5% of the activity with trimethylamine N-oxide
-
-
?
Trimethylamine N-oxide
Dimethylamine + formaldehyde
-
anaerobic conditions
-
?
Trimethylamine N-oxide
Dimethylamine + formaldehyde
-
anaerobic conditions
-
?
additional information
?
-
-
enzyme is present in cells grown on methylamine, dimethylamine, trimethylamine and trimethyl N-oxide and is induced before growth begins when succinate-grown Pseudomonas aminovorans is transferred to an amine growth medium
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
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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
additional information
?
-
-
enzyme is present in cells grown on methylamine, dimethylamine, trimethylamine and trimethyl N-oxide and is induced before growth begins when succinate-grown Pseudomonas aminovorans is transferred to an amine growth medium
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
additional information
?
-
-
the accumulation of formaldehyde and the resulting deterioration of seafood products during frozen storage are primarily caused by the enzymatic activity of trimethylamine oxide aldolase
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
cofactor system composed of Fe2+, cysteine and/or ascorbate functions under aerobic and anaerobic conditions, a second cofactor system with NADH/FMN requires anaerobic conditions
FMN
-
cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
NADH
-
cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
cofactor system composed of Fe2+, cysteine and/or ascorbate functions under aerobic and anaerobic conditions, a second cofactor system with NADH/FMN requires anaerobic conditions
Fe2+
-
no activity when Fe2+ is replaced by the Cl-salts of Ca2+, Mn2+, Mg2+, Ni2+, Zn2+, or Co2+ for the ascorbate, cysteine, and Fe2+ cofactor system
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
activity stimulated by NADH and FMN (anaerobic) is inhibited by 40%
FeCl2
-
activity stimulated by NADH and FMN (anaerobic) is inhibited by 95% in the presence of 0.2 mM FeCl2, inhibition cannot be relieved by the presence of EDTA. Activity stimulated by ascorbate is inhibited by 94% in the presence of 0.2 mM FeCl2
iodoacetamide
-
pre-incubation results in 25% loss of activity in both cofactor systems
NaN3
-
100% inhibition of NADH/FMN cofactor system (anaerobic conditions), 40% inhibition of the ascorbate/cysteine/Fe2+ cofactor system under anaerobic conditions
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
cofactor system composed of Fe2+, cysteine and/or ascorbate functions under aerobic and anaerobic conditions, a second cofactor system with NADH/FMN requires anaerobic conditions
additional information
-
antagonistic relationship between two cofactor systems, implying competition for a single site
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.7
Trimethylamine N-oxide
-
catalyzed aerobically in presence of Fe2+ (0.2 mM), ascorbate (2 mM), and cysteine (2 mM)
21
Trimethylamine N-oxide
-
catalyzed anaerobically in presence of FMN (0.1 mM) and NADH (0.4 mM)
26.2
Trimethylamine N-oxide
-
in 100 mM Tris-acetate (pH 7.0), 2 mM cysteine, 2 mM ascorbate, and 0.2 mM FeCl2, at 50°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
specific activity is much higher in ultrasonic extracts of Pseudomonas aminovorans grown on methylamine than in cells grown on trimethylamine and trimethylamine N-oxide, low activity in trimethylamine and trimethylamine N-oxide grown cells is due to the presence of an inactivating factor. The inactivating factor is absent from methylamine-grown cells
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
-
pH 5.0: about 75% of maximal activity, pH 7.5: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
exposure of the enzyme for 30 min at 0°C to buffers of pH values in the region 4 to 9 does not result in loss of activity followed by adjustment of the pH 6.0
-
inclusion of mercaptoethanol, EDTA and PMSF in the preparative buffers enhance yield and stability of microsomal activity
-
trimethylamine-grown Pseudomonas aminovorans enzyme is more labile at 40°C than enzyme from methylamine-grown bacteria in French press extracts
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diethylaminoethyl-cellulose chromatography and Sephacryl S-300 gel filtration
-
partial
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Large, P.J.
Non-oxidative demethylation of trimethylamine N-oxide by Pseudomonas aminovorans
FEBS Lett.
18
297-300
1979
Aminobacter aminovorans
brenda
Boulton, C.A.; Large, P.J.
Inactivation of trimethylamine N-oxide aldolase (demethylase) during preparation of bacterial extracts
FEMS Microbiol. Lett.
5
159-162
1979
Aminobacter aminovorans
-
brenda
Myers, P.A.; Zatman, L.J.
The metabolism of trimethylamine N-oxide by Bacillus PM 6
Biochem. J.
121
10P
1971
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) PM 6
brenda
Parkin, K.L.; Hultin, H.O.
Characterisation of trimethylamine-N-oxide (TMAO) demethylase activity from fish muscle microsomes
J. Biochem.
100
77-86
1986
Urophycis chuss
brenda
Parkin, K.L.; Hultin, H.O.
Partial purification of trimethyl-N-oxide (TMAO) demethylase from crude fish muscle microsomes by detergents
J. Biochem.
100
87-97
1986
Urophycis chuss
brenda
Nielsen, M.K.; Havemeister, W.; Rehbein, H.; Sotelo, C.G.; Jorgensen, B.M.
A sensitive trimethylamine-N-oxide aldolase assay in two steps without deproteinisation.
J. Sci. Food Agric.
80
197-200
2000
Pollachius virens
brenda
Nielsen, M.K.; Jorgensen, B.M.
Quantitative relationship between trimethylamine oxide aldolase activity and formaldehyde accumulation in white muscle from gadiform fish during frozen storage
J. Agric. Food Chem.
52
3814-3822
2004
Gadus morhua, Pollachius virens, no activity in Oncorhynchus mykiss, no activity in Lophius piscatorius, no activity in Sebastes marinus, no activity in Squalus acanthias, no activity in Hippoglossus hippoglossus, no activity in Pleuronectes platessa, no activity in Anarhichas lupus, no activity in Loligo forbesi, no activity in Nephrops norvegicus, no activity in Pecten maximus, no activity in Pandalus borealis, Molva molva, no activity in Penaeus monodon, no activity in Scomber scombrus, no activity in Limanda limanda, no activity in Platichthys flesus, Molva dypterygia, Brosme brosme, Merlangius merlangus, Lota lota, Melanogrammus aeglefinus, Pollachius pollachius
brenda
Fu, X.Y.; Xue, C.H.; Miao, B.C.; Liang, J.N.; Li, Z.J.; Cui, F.X.
Purification and characterization of trimethylamine-N-oxide demethylase from jumbo squid (Dosidicus gigas)
J. Agric. Food Chem.
54
968-972
2006
Dosidicus gigas
brenda
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