EC Number |
General Information |
Reference |
---|
4.3.99.4 | evolution |
choline TMA-lyase belongs to the glycyl radical enzymes (GREs) utilize protein-based radical intermediates to catalyze a variety of reactions, including nucleotide reduction (class III ribonucleotide reductase (RNR)), C-C bond formation (benzylsuccinate synthase (BSS)), C-C bond cleavage (pyruvate formate-lyase (PFL) and 4-hydroxyphenylacetate decarboxylase (4-HPAD)), and dehydration (B12-independent glycerol dehydratase (GDH)) |
-, 728855 |
4.3.99.4 | metabolism |
the enzyme is involved in anaerobic choline metabolism and encoded in the choline utilization (cut) gene cluster |
-, 728855 |
4.3.99.4 | more |
enzyme homology modeling, docking of choline in the active site of a the enzyme, docking model, overview |
-, 728855 |
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 |
-, 720938 |