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Catalysis may thus stabilize an enzyme.
This correlation suggests that the protein motions necessary for catalysis are an intrinsic property of the enzyme and may even limit the overall turnover rate.
SummaryMaximal efficiency of catalysis appears to require that an enzyme and a substrate combine productively in the ground state.
It may play a role in enzymatic catalysis by contributing to the formation of the catalytically potent enzyme–substrate complex.
We conclude that enzyme catalysis is significantly enhanced by the ability of the enzyme to preorganize the reaction environment.
Enzyme catalysis can now be seen not as enzyme acting on its substrate, but rather as enzyme and substrate entering into a relation which allows them to traverse the reaction coordinate as an ontologic unity.
Enzyme catalysis, as a green, efficient process, displays exceptional functionality, adaptivity and sustainability.
Both strategies of enzyme engineering can be successful and are very useful for improving the utility of enzymes for applied catalysis.
This comparison underlines what is important to catalysis in these two enzymes and concurrently highlights fundamental issues in enzyme catalysis.
Open accessBook ChapterDOI
Buyong Ma, Ruth Nussinov 
41 Citations
Collectively, these effects contribute to enzyme catalysis.

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