Quantifying the limits of transition state theory in enzymatic catalysis
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چکیده
منابع مشابه
Quantifying the limits of transition state theory in enzymatic catalysis
While being one of the most popular reaction rate theories, the applicability of transition state theory to the study of enzymatic reactions has been often challenged. The complex dynamic nature of the protein environment raised the question about the validity of the nonrecrossing hypothesis, a cornerstone in this theory. We present a computational strategy to quantify the error associated to t...
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The incredible catalytic rate enhancements caused by enzymes led Linus Pauling (1) to suggest that enzymes bind tightly to substrates distorted toward the transition state, thereby concentrating them and enforcing catalysis. Wolfenden (2) explained that chemically stable analogues that resemble the transition state would be expected to bind more tightly than substrate by factors resembling the ...
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THE KEY TO UNDERSTANDING THE FUNDAMENTAL PROCESSES OF CATALYSIS IS THE TRANSITION STATE (TS): indeed, catalysis is a transition-state molecular recognition event. Practical objectives, such as the design of TS analogues as potential drugs, or the design of synthetic catalysts (including catalytic antibodies), require prior knowledge of the TS structure to be mimicked. Examples, both old and new...
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BACKGROUND Phosphoryl transfer, typically involving high energy phosphate donors such as ATP, is the most common class of biological reactions. Despite this, the transition state for phosphoryl transfer from ATP in solution has not been systematically investigated. Characterization of the transition state for the uncatalyzed hydrolysis of ATP would provide a starting point for dissection of enz...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2017
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1710820114