Literature summary for 4.3.1.7 extracted from

Robertson, W.D.; Wang, M.; Warncke, K.
Characterization of protein contributions to cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase by using photolysis in the ternary complex (2011), J. Am. Chem. Soc., 133, 6968-6977.

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Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
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

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Release 2023.1 (January 2023)