Literature summary extracted from

Mori, K.; Bando, R.; Hieda, N.; Toraya, T.
Identification of a reactivating factor for adenosylcobalamin-dependent ethanolamine ammonia lyase (2004), J. Bacteriol., 186, 6845-6854.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
4.3.1.7	additional information	the holoenzyme of adenosylcobalamin-dependent ethanolamine ammonia lyase undergoes suicidal inactivation during catalysis as well as inactivation in the absence of substrate. The inactivation involves the irreversible cleavage of the Co-C bond of the coenzyme. Inactivated holoenzyme undergoes rapid and continuous reactivation in the presence of ATP, Mg2+ and free adensosylcobalamin. EutA is essential for reactivation. Reactivation and activation occur through the exchange of modified coenzyme for free intact adenosylcobalamin	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.3.1.7	Escherichia coli	-	-	-

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
4.3.1.7	adenosylcobalamin	the holoenzyme of adenosylcobalamin-dependent ethanolamine ammonia lyase undergoes suicidal inactivation during catalysis as well as inactivation in the absence of substrate. The inactivation involves the irreversible cleavage of the Co-C bond of the coenzyme. Inactivated holoenzyme undergoes rapid and continuous reactivation in the presence of ATP, Mg2+ and free adensosylcobalamin. EutA is essential for reactivation. Reactivation and activation occur through the exchange of modified coenzyme for free intact adenosylcobalamin	Escherichia coli

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Release 2023.1 (January 2023)