BRENDA - Enzyme Database
show all sequences of 4.1.2.32

Characterisation of trimethylamine-N-oxide (TMAO) demethylase activity from fish muscle microsomes

Parkin, K.L.; Hultin, H.O.; J. Biochem. 100, 77-86 (1986)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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
Urophycis chuss
additional information
antagonistic relationship between two cofactor systems, implying competition for a single site
Urophycis chuss
General Stability
General Stability
Organism
inclusion of mercaptoethanol, EDTA and PMSF in the preparative buffers enhance yield and stability of microsomal activity
Urophycis chuss
Inhibitors
Inhibitors
Commentary
Organism
Structure
ascorbate
activity stimulated by NADH and FMN (anaerobic) is inhibited by 40%
Urophycis chuss
cyanide
K-salt of inhibits both cofactor systems by 75%
Urophycis chuss
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
Urophycis chuss
FMN
30% inhibition in the presence of Fe2+, cysteine, and ascorbate
Urophycis chuss
iodoacetamide
pre-incubation results in 25% loss of activity in both cofactor systems
Urophycis chuss
additional information
overview
Urophycis chuss
NaN3
100% inhibition of NADH/FMN cofactor system (anaerobic conditions), 40% inhibition of the ascorbate/cysteine/Fe2+ cofactor system under anaerobic conditions
Urophycis chuss
trimethylamine
-
Urophycis chuss
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7
-
Trimethylamine N-oxide
catalyzed aerobically in presence of Fe2+ (0.2 mM), ascorbate (2 mM), and cysteine (2 mM)
Urophycis chuss
21
-
Trimethylamine N-oxide
catalyzed anaerobically in presence of FMN (0.1 mM) and NADH (0.4 mM)
Urophycis chuss
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Urophycis chuss
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
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; 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
Urophycis chuss
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Urophycis chuss
-
red hake
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
muscle
-
Urophycis chuss
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Trimethylamine N-oxide
-
5136
Urophycis chuss
Dimethylamine + formaldehyde
-
5136
Urophycis chuss
-
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
activity generated by both cofactor systems is lost
Urophycis chuss
100
-
heating for 5 min deactivates partial purified fraction
Urophycis chuss
Cofactor
Cofactor
Commentary
Organism
Structure
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
Urophycis chuss
FMN
cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
Urophycis chuss
NADH
cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
Urophycis chuss
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
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
Urophycis chuss
additional information
antagonistic relationship between two cofactor systems, implying competition for a single site
Urophycis chuss
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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
Urophycis chuss
FMN
cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
Urophycis chuss
NADH
cofactor system NADH/FMN requires anaerobic conditions, a second cofactor system composed of Fe2+, cysteine and/or ascorbate under aerobic or anaerobic conditions
Urophycis chuss
General Stability (protein specific)
General Stability
Organism
inclusion of mercaptoethanol, EDTA and PMSF in the preparative buffers enhance yield and stability of microsomal activity
Urophycis chuss
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ascorbate
activity stimulated by NADH and FMN (anaerobic) is inhibited by 40%
Urophycis chuss
cyanide
K-salt of inhibits both cofactor systems by 75%
Urophycis chuss
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
Urophycis chuss
FMN
30% inhibition in the presence of Fe2+, cysteine, and ascorbate
Urophycis chuss
iodoacetamide
pre-incubation results in 25% loss of activity in both cofactor systems
Urophycis chuss
additional information
overview
Urophycis chuss
NaN3
100% inhibition of NADH/FMN cofactor system (anaerobic conditions), 40% inhibition of the ascorbate/cysteine/Fe2+ cofactor system under anaerobic conditions
Urophycis chuss
trimethylamine
-
Urophycis chuss
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.7
-
Trimethylamine N-oxide
catalyzed aerobically in presence of Fe2+ (0.2 mM), ascorbate (2 mM), and cysteine (2 mM)
Urophycis chuss
21
-
Trimethylamine N-oxide
catalyzed anaerobically in presence of FMN (0.1 mM) and NADH (0.4 mM)
Urophycis chuss
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Urophycis chuss
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
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; 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
Urophycis chuss
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
muscle
-
Urophycis chuss
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Trimethylamine N-oxide
-
5136
Urophycis chuss
Dimethylamine + formaldehyde
-
5136
Urophycis chuss
-
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
activity generated by both cofactor systems is lost
Urophycis chuss
100
-
heating for 5 min deactivates partial purified fraction
Urophycis chuss
Other publictions for EC 4.1.2.32
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
680290
Fu
Purification and characterizat ...
Dosidicus gigas
J. Agric. Food Chem.
54
968-972
2006
4
-
-
-
-
-
3
1
-
3
2
-
-
4
-
-
1
-
-
-
2
-
1
-
1
-
-
-
1
1
-
-
-
-
-
4
-
-
-
-
-
-
-
3
-
1
-
3
2
-
-
-
-
1
-
-
2
-
1
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
665261
Nielsen
Quantitative relationship betw ...
Brosme brosme, Gadus morhua, Lota lota, Melanogrammus aeglefinus, Merlangius merlangus, Molva dipterygia, Molva molva, no activity in Anarhichas lupus, no activity in Hippoglossus hippoglossus, no activity in Limanda limanda, no activity in Loligo forbesi, no activity in Lophius piscatorius, no activity in Nephrops norvegicus, no activity in Oncorhynchus mykiss, no activity in Pandalus borealis, no activity in Pecten maximus, no activity in Penaeus monodon, no activity in Platichthys flesus, no activity in Pleuronectes platessa, no activity in Scomber scombrus, no activity in Sebastes marinus, no activity in Squalus acanthias, Pollachius pollachius, Pollachius virens
J. Agric. Food Chem.
52
3814-3822
2004
-
-
-
-
-
-
-
-
-
-
-
9
-
25
-
-
-
-
-
16
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
16
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
653047
Nielsen
-
A sensitive trimethylamine-N-o ...
Pollachius virens
J. Sci. Food Agric.
80
197-200
2000
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
2
-
-
-
-
-
-
-
-
5136
Parkin
Characterisation of trimethyla ...
Urophycis chuss
J. Biochem.
100
77-86
1986
2
-
-
-
-
1
8
2
1
1
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
2
-
-
-
-
3
-
-
-
2
-
-
3
-
-
1
-
8
-
2
1
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
5137
Parkin
Partial purification of trimet ...
Urophycis chuss
J. Biochem.
100
87-97
1986
1
-
-
-
-
-
3
-
1
1
-
-
-
2
-
-
1
-
-
1
-
-
1
-
-
-
1
-
-
-
-
3
-
-
-
1
-
-
3
-
-
-
-
3
-
-
1
1
-
-
-
-
-
1
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
5133
Large
Non-oxidative demethylation of ...
Aminobacter aminovorans
FEBS Lett.
18
297-300
1979
-
-
-
-
-
3
3
2
-
-
-
1
-
1
-
-
1
1
-
-
-
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
3
-
3
-
2
-
-
-
1
-
-
-
1
-
-
-
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
5134
Boulton
-
Inactivation of trimethylamine ...
Aminobacter aminovorans
FEMS Microbiol. Lett.
5
159-162
1979
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5135
Myers
The metabolism of trimethylami ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) PM 6
Biochem. J.
121
10P
1971
2
-
-
-
-
-
2
1
-
1
2
-
-
2
-
-
-
-
-
-
-
-
8
1
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
2
-
1
-
1
2
-
-
-
-
-
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-
-
-
8
1
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-
-
-
1
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-
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-