1.5.8.2: trimethylamine dehydrogenase
This is an abbreviated version!
For detailed information about trimethylamine dehydrogenase, go to the full flat file.
Word Map on EC 1.5.8.2
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1.5.8.2
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flavin
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flavoproteins
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fmn
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iron-sulfur
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semiquinone
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mononucleotide
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methylotrophus
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methylophilus
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dimethylamine
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6-s-cysteinyl
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isoalloxazine
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ferricenium
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flavocytochrome
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nocardioides
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flavinylation
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fmn-binding
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tetramethylammonium
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deflavo
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hyphomicrobium
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analysis
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nutrition
- 1.5.8.2
- flavin
- flavoproteins
- fmn
-
iron-sulfur
- semiquinone
- mononucleotide
- methylotrophus
- methylophilus
- dimethylamine
-
6-s-cysteinyl
- isoalloxazine
- ferricenium
-
flavocytochrome
-
nocardioides
-
flavinylation
-
fmn-binding
- tetramethylammonium
-
deflavo
- hyphomicrobium
- analysis
- nutrition
Reaction
Synonyms
EC 1.5.99.7, More, TMA dehydrogenase, TMADH, TMD, TMDH
ECTree
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Engineering
Engineering on EC 1.5.8.2 - trimethylamine dehydrogenase
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C-terminal truncations
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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
Y442F
Y442G
Y442L
C-terminal truncations
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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
Y442F
Y442G
Y442L
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removal of the 6-S-cysteinyl-FMN bond, diminishes limiting rate for the first of three observed kinetic phases
C30A
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mutant shows highly increased activity to oxidate of the cofactor FMN to 6-hydroxyFMN compared to the wild-type enzyme
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removal of the 6-S-cysteinyl-FMN bond, diminishes limiting rate for the first of three observed kinetic phases
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