The enigmatic conservation of enzyme dynamics in evolution

Publication date: Available online 14 September 2016 Source:Perspectives in Science Author(s): Amnon Kohen Examination of the chemical step catalyzed by dihydrofolate reductase (DHFR) suggested preservation of an “ideal” transition state as the enzyme evolves from bacteria to human. This observation is enigmatic: since evolutionary pressure is most effective on enzymes’ second order rate constant (k cat/K M) and since the chemistry is not rate limiting on that kinetic parameter, why is the nature of the chemical step preserved? Studies addressing this question were presented in the 2015 Beilstein ESCEC Symposium and are summarized below.

Source: Perspectives in Science - September 14, 2016 Category: Science Source Type: research