Information on EC 1.5.8.2 - trimethylamine dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.8.2
-
RECOMMENDED NAME
GeneOntology No.
trimethylamine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transfer flavoprotein
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative demethylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methane metabolism
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating)
A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors; phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors. Contains FAD and a [4Fe-4S] cluster.
CAS REGISTRY NUMBER
COMMENTARY hide
39307-09-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Hyphomicrobium X
-
-
Manually annotated by BRENDA team
strain NQ-521
-
-
Manually annotated by BRENDA team
strain NQ-521
-
-
Manually annotated by BRENDA team
methylotrophic bacterium
methylotrophic bacterium 4B6
strain 4B6
-
-
Manually annotated by BRENDA team
methylotrophic bacterium C2A1
strain C2A1
-
-
Manually annotated by BRENDA team
no activity in Bacillus sp.
strains S2A1, PM6
-
-
Manually annotated by BRENDA team
no activity in methylotrophic bacterium
facultative methylotrophs
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas sp.
strain 3A2
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas sp. 3A2
strain 3A2
-
-
Manually annotated by BRENDA team
strain T231
-
-
Manually annotated by BRENDA team
; strain is able to grow on trimethylamine as a nitrogen source and trimethylamine also accumulates in the cell, slowing the bacterial growth
-
-
Manually annotated by BRENDA team
Pseudomonas putida ATCC 12633
; strain is able to grow on trimethylamine as a nitrogen source and trimethylamine also accumulates in the cell, slowing the bacterial growth
-
-
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
2-aminoethyldimethylamine + H2O + phenazine methosulfate
? + reduced phenazine methosulfate
show the reaction diagram
2-chloroethyldimethylamine + H2O + phenazine methosulfate
? + reduced phenazine methosulfate
show the reaction diagram
methylotrophic bacterium
-
40% of the activity compared to trimethylamine
-
?
2-hydroxyethyldimethylamine + H2O + phenazine methosulfate
? + reduced phenazine methosulfate
show the reaction diagram
methylotrophic bacterium
-
70% of the activity compared to trimethylamine
-
?
diethylamine + H2O + phenazine methosulfate
ethylamine + acetaldehyde + reduced phenazine methosulfate
show the reaction diagram
diethylmethylamine + H2O + electron acceptor
diethylamine + formaldehyde + reduced electron acceptor
show the reaction diagram
diethylmethylamine + H2O + phenazine methosulfate
diethylamine + ethylmethylamine + formaldehyde + acetaldehyde + reduced phenazine methosulfate
show the reaction diagram
ethyldimethylamine + H2O + phenazine methosulfate
ethylmethylamine + formaldehyde + reduced phenazine methosulfate
show the reaction diagram
FMN + O2 + H2O
6-hydroxy-FMN + H2O2
show the reaction diagram
-
reaction mechanism, reoxidation of the cofactor, mutant C30A enzyme, low activity with wild-type enzyme and mutant W355L
the hydroxy group oxygen is derived from molecular oxygen not from water
-
r
triethylamine + H2O + phenazine methosulfate
diethylamine + acetaldehyde + reduced phenazine methosulfate
show the reaction diagram
methylotrophic bacterium
-
3% of the activity compared to trimethylamine
-
?
trimethylamine + H2O + 2,6-dichlorophenolindophenol
dimethylamine + formaldehyde + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
trimethylamine + H2O + alphaR237K mutant electron transferring flavoprotein
dimethylamine + formaldehyde + reduced alphaR237K mutant electron transferring flavoprotein
show the reaction diagram
trimethylamine + H2O + electron acceptor
dimethylamine + formaldehyde + reduced electron acceptor
show the reaction diagram
trimethylamine + H2O + electron transferring flavoprotein
dimethylamine + formaldehyde + reduced electron transferring flavoprotein
show the reaction diagram
trimethylamine + H2O + electron-transfer flavoprotein
dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
show the reaction diagram
trimethylamine + H2O + ferricenium hexafluorophosphate
dimethylamine + formaldehyde + ferrocenium hexafluorophosphate
show the reaction diagram
trimethylamine + H2O + FMN
dimethylamine + formaldehyde + FMNH2
show the reaction diagram
trimethylamine + H2O + NADP+
dimethylamine + formaldehyde + NADPH
show the reaction diagram
-
-
-
-
?
trimethylamine + H2O + oxidized electron-transferring flavoprotein
dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
show the reaction diagram
-
-
-
-
r
trimethylamine + H2O + phenazine methosulfate
dimethylamine + formaldehyde + reduced phenazine methosulfate
show the reaction diagram
trimethylamine + H2O + semiquinone electron-transferring flavoprotein
dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
show the reaction diagram
-
-
-
-
r
additional information
?
-
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
diethylmethylamine + H2O + electron acceptor
diethylamine + formaldehyde + reduced electron acceptor
show the reaction diagram
trimethylamine + H2O + electron acceptor
dimethylamine + formaldehyde + reduced electron acceptor
show the reaction diagram
trimethylamine + H2O + electron transferring flavoprotein
dimethylamine + formaldehyde + reduced electron transferring flavoprotein
show the reaction diagram
trimethylamine + H2O + electron-transfer flavoprotein
dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
show the reaction diagram
trimethylamine + H2O + FMN
dimethylamine + formaldehyde + FMNH2
show the reaction diagram
additional information
?
-
-
versatile metabolic pathways for the degradation of trimethylamine, phylogenetic analysis of the Paracoccus strains
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
electron transferring flavoprotein
electron-transferring flavoprotein
-
interaction with the enzyme, binding study, reaction mechanism and kinetics
additional information
-
independent of NADPH
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-phenylcyclopropylamine
-
irreversible inactivation of both wild-type and mutant C30A
1-phenylethylhydrazine
methylotrophic bacterium
-
potent inhibition at very low concentration
2,6-dichlorophenolindophenol
-
-
2-phenylcyclopropylamine
methylotrophic bacterium
-
82% inhibition at 0.1 mM
2-phenylethylhydrazine
methylotrophic bacterium
-
potent inhibition at very low concentration
acetaldehyde
-
noncompetitive inhibition with respect to diethylamine, uncompetitive inhibition with respect to phenazine methosulfate
Ag+
methylotrophic bacterium
-
strong inhibition at 1 mM
benzylhydrazine
methylotrophic bacterium
-
potent inhibition at very low concentration
Betaine hydrochloride
methylotrophic bacterium
-
37% inhibition at 1 mM
choline chloride
methylotrophic bacterium
-
potent inhibition at 1 mM
Co2+
methylotrophic bacterium
-
strong inhibition at 1 mM
Cu2+
methylotrophic bacterium
-
strong inhibition at 1 mM
Diethylamine
-
noncompetitive product inhibition with respect to phenazine methosulfate
diphosphate
-
noncompetitive inhibition to 50% of initial activity with respect to trimethylamine
ethylamine
-
noncompetitive product inhibition with respect to phenazine methosulfate
ferricinium
-
Val334 is involved in binding and initiates a conformational change interrupting the electron transfer between FMN and the [4Fe-4S] cluster
Harmaline
methylotrophic bacterium
-
65% inhibition at 0.1 mM
hexamethylene bis-trimethylammonium chloride
methylotrophic bacterium
-
potent inhibition at 1 mM
Hg2+
methylotrophic bacterium
-
strong inhibition at 1 mM
iodoacetamide
methylotrophic bacterium
-
inhibition at 1 mM
Iproniazid
methylotrophic bacterium
-
potent inhibition at very low concentration
isocarboxazid
methylotrophic bacterium
-
potent inhibition at very low concentration
isopropylhydrazine
methylotrophic bacterium
-
potent inhibition at very low concentration
N,N,N-trimethyl-N-phenylammonium chloride
methylotrophic bacterium
-
potent inhibition at 1 mM
N,N,N-trimethylhydrazonium iodide
methylotrophic bacterium
-
potent inhibition at 1 mM
N-benzyl-N-methylpropargylamine
methylotrophic bacterium
-
27% inhibition at 0.1 mM
N-cyclopropyl-alpha-methylbenzylamine
-
irreversible inactivation of both wild-type and mutant C30A, more potent than 1-phenylcyclopropylamine
N-ethylmaleimide
methylotrophic bacterium
-
inhibition at 1 mM
Ni2+
methylotrophic bacterium
-
strong inhibition at 1 mM
nialamid
methylotrophic bacterium
-
potent inhibition at very low concentration
p-chloromercuribenzoate
methylotrophic bacterium
-
inhibition at 1 mM
phenylhydrazine
Tetramethylammonium chloride
trimethylamine
trimethylsulfomium chloride
methylotrophic bacterium
-
potent inhibition at 1 mM
additional information
-
no inhibition by (dimethylamino)methylene ferrocene, ferrocenedicarboxylic acid, ferrocenemonocarboxylic acid, ferrocenedimathanol, (dimethylamino)methylene ferrocene, ferricyanide, and thionine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the enzyme is not activated by AlCl3
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067
2-aminoethyldimethylamine
methylotrophic bacterium
-
electron acceptor: phenazine methosulfate
0.002
2-chloroethyldimethylamine
methylotrophic bacterium
-
electron acceptor: phenazine methosulfate
0.006
2-hydroxyethyldimethylamine
methylotrophic bacterium
-
electron acceptor: phenazine methosulfate
0.0031
alphaR237K mutant electron transferring flavoprotein
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at 25C
-
1.7
Diethylamine
methylotrophic bacterium
-
electron acceptor: phenazine methosulfate
0.008
diethylmethylamine
methylotrophic bacterium
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electron acceptor: phenazine methosulfate
0.0105
electron transferring flavoprotein
-
at 25C
0.002
ethyldimethylamine
methylotrophic bacterium
-
electron acceptor: phenazine methosulfate
1.25
phenazine methosulfate
methylotrophic bacterium
-
substrate: trimethylamine
0.13
triethylamine
methylotrophic bacterium
-
electron acceptor: phenazine methosulfate
0.002 - 4
trimethylamine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.46
alphaR237K mutant electron transferring flavoprotein
Methylophilus methylotrophus
-
at 25C
-
9.67
electron transferring flavoprotein
Methylophilus methylotrophus
-
at 25C
0.25 - 40
trimethylamine
additional information
Abz-VAA
Methylophilus methylotrophus
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.75
trimethylamine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000031
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tetradecyltrimethylammonium bromide-grown cells, pH 7.4, 30C
0.022
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cell extract, strain GPR21, anaerobic condition
0.043
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cell extract, strain PH32, aerobic condition
0.0964
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cell extract, strain PH34, anaerobic condition
0.097
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cell extract, strain GPR21, aerobic condition
0.107
-
cell extract, strain GP43, anaerobic condition
0.119
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cell extract, strain GP43, aerobic condition
0.126
-
strain W3A1
0.131
-
cell extract, strain PH34, aerobic condition
0.18
-
cell extract, strain PH32, anaerobic condition
2
methylotrophic bacterium
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
strains PH32, PH34, and GRP21 are halophilic and do not grow without NaCl in the culture medium
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
146800
-
sedimentation equilibrium ultracentrifugation
161000
methylotrophic bacterium
-
gel filtration
163000
-
gel filtration
166000
-
calculation from X-ray data
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion technique, 2.0 A resolution
-
macro-seeding of sitting drops, 6 A resolution
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X-ray structure, 2.4 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
methylotrophic bacterium
-
loss of 50% of activity in 20 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20 mM sodium phosphate, pH 7.5, 0.4 mg protein/ml, stable for 3 months
methylotrophic bacterium
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme, and recombinant wild-type and mutant T442G enzymes expressed in Escherichia coli strain BL21(DE3)
-
to homogeneity, chromatography steps
to homogeneity, chromatography steps; to homogeneity, recombinant enzyme
-
to homogeneity, recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant C30A in Escherichia coli strain JM109
-
expression of wild-type and mutant T442G enzymes in Escherichia coli strain Bl21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-terminal truncations
-
C-terminal truncations of 5, 10 or 17 residues do not affect dimer stability, but compromise the ability of the enzyme to become covalently coupled with FMN in the active site
H172Q
-
no change of turnover, but 25fold increase of Km-value
V344I
-
increase of Km-value, decrease of turnover
C-terminal truncations
-
C-terminal truncations of 5, 10 or 17 residues do not affect dimer stability, but compromise the ability of the enzyme to become covalently coupled with FMN in the active site
-
C30A
-
binds FMN non-covalently; binds FMN non-covalently; removal of the 6-S-cysteinyl-FMN bond, diminishes limiting rate for the first of three observed kinetic phases
-
H172Q
-
no change of turnover, but 25fold increase of Km-value
-
V344I
-
increase of Km-value, decrease of turnover
-
Y442F
-
; 1.4fold reduction of electron transfer
-
Y442G
-
30.5fold reduction of electron transfer
-
Y442L
-
; 2.2fold reduction of electron transfer
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
nutrition
-
quality control, development of an amperometric enzyme electrode sensor for rapid detection of trimethylamine in different fish muscle samples using phenazine methosulfate as redox cofactor and NBT-based colorimetric detectiona nd quantification