Understanding the catalytic activity of enzymes

Published on December 9, 2011

There is a tremendous amount of information that is not yet fully understood about how proteins function.

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An enzymatic catalysis presents itself as an immensely complex mechanism: solvation and desolvation takes place, entropy and enthalpy are redistributed, intramolecular interactions in the protein matrix and intermolecular interactions occur, and the binding energy continuously changes when the catalytic cycle takes its course.
The impact of the Commision for Standards for Reporting Enzymology Data (STRENDA) on the biological community is also discussed.

Thomas S. Leyh is a professor of Biochemistry at the Albert Einstein College of Medicine in New York. He is a mechanistic enzymologist with a research focus on sulfur biochemistry, GTPase function, and the conformational coupling of energetics. He is also a founding member of the STRENDA Commission.

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