The Mechanism of Action of Ethanolamine Deaminase
Year: 1969
Type: article
Abstract: A study was carried out on the effect of a large number of Blz analogues on the coenzyme BIP-dependent enzyme ethanolamine deaminase.The analogues tested included MeB12, E&Z, AB12, Rl312, BB2, %Z, DBvz, uB12, CNBl2, and OHBU.DBlz was found to be capable of replacing the coenzyme.In contrast, all the rest of the analogues were inhibitors.With all the inhibitors except IB12, the inhibition was progressive, with the reaction velocity decaying exponentially with time to a final, constant value.The extent of inhibition by IB12 was independent of time; kinetics showed that this inhibition was competitive with respect to the coenzyme.Inhibition by MeB12 was also found to be competitive with DMBC, when its effect of the initial reaction rate was considered.Studies of the time-dependent increase in the extent of inhibition observed with MeB12 showed that the rate constant for this process (the deactivation constant) followed saturation kinetics with respect to the concentration of inhibitor.A similar dependence of the deactivation constant on the inhibitor concentration was observed with R&2.
Source: Journal of Biological Chemistry
Author: B M Babior
Institution: National Institutes of Health
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1504820765