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Literature summary extracted from

  • Craciun, S.; Balskus, E.P.
    Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme (2012), Proc. Natl. Acad. Sci. USA, 109, 21307-21312.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.99.4 expression in Escherichia coli Oleidesulfovibrio alaskensis

Protein Variants

EC Number Protein Variants Comment Organism
4.3.99.4 C489A complete loss of activity Oleidesulfovibrio alaskensis
4.3.99.4 G821A complete loss of activity Oleidesulfovibrio alaskensis

Organism

EC Number Organism UniProt Comment Textmining
4.3.99.4 Desulfovibrio desulfuricans
-
-
-
4.3.99.4 Desulfovibrio desulfuricans B8J0I2 member of the glycyl radical enzyme family
-
4.3.99.4 Oleidesulfovibrio alaskensis Q30W70 member of the glycyl radical enzyme family
-
4.3.99.4 Oleidesulfovibrio alaskensis G20 Q30W70 member of the glycyl radical enzyme family
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.99.4 choline
-
 Oleidesulfovibrio alaskensis trimethylamine + acetaldehyde a glycyl radical-based mechanism of C-N cleavage ?
4.3.99.4 choline
-
 Desulfovibrio desulfuricans trimethylamine + acetaldehyde a glycyl radical-based mechanism of C-N cleavage ?
4.3.99.4 choline
-
 Oleidesulfovibrio alaskensis G20 trimethylamine + acetaldehyde a glycyl radical-based mechanism of C-N cleavage ?

Synonyms

EC Number Synonyms Comment Organism
4.3.99.4 choline TMA-lyase
-
 Oleidesulfovibrio alaskensis
4.3.99.4 choline TMA-lyase
-
 Desulfovibrio desulfuricans
4.3.99.4 cutC
-
 Oleidesulfovibrio alaskensis
4.3.99.4 cutC
-
 Desulfovibrio desulfuricans
4.3.99.4 Dde_3282 locus name Oleidesulfovibrio alaskensis
4.3.99.4 Dde_3282 locus name Desulfovibrio desulfuricans

General Information

EC Number General Information Comment Organism
4.3.99.4 physiological function gene disruption impairs growth on choline and abolishes production of trimethylamine, with no difference in growth between wild-type and mutant in media containing lactate. Expression of choline trimethylamine-lyase CutC and its activating protein CutD in Escherichia coli BL21 results in production of d9-TMA from (trimethyl-d9)-choline. Expression of either enzyme on its own completely abolishes trimethylamine production Oleidesulfovibrio alaskensis