EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.3.1.7 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.3.1.7 | adenosylcobalamin | pulsed-laser photolysis of substrate-triggered cleavage of the cobalt-carbon bond and formation of the cob(II)alamin-5'-deoxyadenosyl radical pair in the adenosylcobalamin-dependent ethanolamine ammonia-lyase. Visible absorption spectra of holo-ethanolamine ammonia-lyase and ternary complex are comparable, indicating that the binding of substrate does not labilize the cofactor cobalt-carbon bond by significantly distorting the equilibrium structure. Following the substrate trigger, the protein interacts with the cofactor to contiguously guide the cleavage of the Co-C bond, at every step along the cleavage coordinate, starting from the equilibrium configuration of the ternary complex. The cleavage is represented by a diagonal trajectory across a free energy surface, that is defined by chemical, Co-C separation, and protein configuration coordinates | Salmonella enterica subsp. enterica serovar Typhimurium |