Information on EC 4.1.2.32 - trimethylamine-oxide aldolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.2.32
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RECOMMENDED NAME
GeneOntology No.
trimethylamine-oxide aldolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
trimethylamine N-oxide = dimethylamine + formaldehyde
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
retro aldol-condensation
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-
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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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trimethylamine degradation
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SYSTEMATIC NAME
IUBMB Comments
trimethylamine-N-oxide formaldehyde-lyase (dimethylamine-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
72561-08-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PM 6
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Manually annotated by BRENDA team
PM 6
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Anarhichas lupus
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Hippoglossus hippoglossus
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Limanda limanda
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Loligo forbesi
no activity in mantle
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Manually annotated by BRENDA team
no activity in Lophius piscatorius
no activity in white muscle and jar
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Manually annotated by BRENDA team
no activity in Nephrops norvegicus
no activity in tail
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Manually annotated by BRENDA team
no activity in Oncorhynchus mykiss
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Pandalus borealis
no activity in tail
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Manually annotated by BRENDA team
no activity in Pecten maximus
no activity in adductor muscle
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Manually annotated by BRENDA team
no activity in Penaeus monodon
no activity in tail
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Manually annotated by BRENDA team
no activity in Platichthys flesus
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Pleuronectes platessa
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Scomber scombrus
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Sebastes marinus
no activity in white muscle
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Manually annotated by BRENDA team
no activity in Squalus acanthias
no activity in white muscle
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Manually annotated by BRENDA team
red hake
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-Propoxyphene N-oxide
?
show the reaction diagram
Benzyldimethylamine N-oxide
?
show the reaction diagram
Chlorpromazine N-oxide
?
show the reaction diagram
Trimethylamine N-oxide
Dimethylamine + formaldehyde
show the reaction diagram
additional information
?
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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
Trimethylamine N-oxide
Dimethylamine + formaldehyde
show the reaction diagram
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-
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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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
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cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
NADH
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cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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10 mM, 20.5% increase of activity
Mg2+
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10 mM, 28.8% increase of activity
additional information
-
not affected by Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
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97.1% inhibition at 10 mM
ascorbate
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activity stimulated by NADH and FMN (anaerobic) is inhibited by 40%
cyanide
FeCl2
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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
FMN
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30% inhibition in the presence of Fe2+, cysteine, and ascorbate
iodoacetamide
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pre-incubation results in 25% loss of activity in both cofactor systems
mercaptoethanol
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96% inhibition at concentration of 20 mM
Mercurials
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active at 0.001 mM
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NaN3
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100% inhibition of NADH/FMN cofactor system (anaerobic conditions), 40% inhibition of the ascorbate/cysteine/Fe2+ cofactor system under anaerobic conditions
Phytic acid
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95.6% inhibition at 10 mM
Proadifen hydrochloride
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i.e. SKF 525-A, , competitive
tea polyphenol
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98.6% inhibition at 10 mM
Triethylamine N-oxide
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trimethylamine
Urea
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about 100% inhibition at concentration of 4 mM
additional information
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overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
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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
dithiothreitol
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1 mM, 17.9% increase of activity
EDTA
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10 mM, 94.2% increase of activity
glutathione
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strongly stimulates
L-ascorbate
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strongly stimutates
Na2SO3
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10 mM, 97.4% increase of activity
NADH
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0.4 mM, 41.7% increase of activity
additional information
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antagonistic relationship between two cofactor systems, implying competition for a single site
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
140
Benzyldimethylamine N-oxide
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2 - 26.2
Trimethylamine N-oxide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.19
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cell extract, at 50C
159
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after 839fold purification, at 50C
additional information
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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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
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assay at
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
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practically inactive outside this pH range
4.5 - 5
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90-100% activity
5 - 7.5
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pH 5.0: about 75% of maximal activity, pH 7.5: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17500
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SDS-PAGE
17700
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gel filtration
36000 - 47000
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sedimentation equilibrium centrifugation
50000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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activity generated by both cofactor systems is lost
100
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heating for 5 min deactivates partial purified fraction
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is unstable when purified more than about 5-fold
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exposure of the enzyme for 30 min at 0C 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
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inclusion of mercaptoethanol, EDTA and PMSF in the preparative buffers enhance yield and stability of microsomal activity
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trimethylamine-grown Pseudomonas aminovorans enzyme is more labile at 40C 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
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partial