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Lysozyme Lab Report

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Summary: The Lysozyme Mechanism Sorted- After 50 Years
Nearly 50 years after the first lysozyme crystal structure had been published, the missing piece, the SN2 reaction of the glycosyl-enzyme intermediate, was found. The first lysozyme structure was that of a hen egg white, and it provided a deeper understanding of the mechanism of enzyme reactions. Lysozyme enables the transfer of a glycosyl group to water to occur more quickly. The cleavage of the C-O bond in glycosides without the lysozyme occurs rather slowly.
Although the structures of the reactants for the reaction are known, the complete reaction mechanism is not known for certain. Specifically, the part of the mechanism that researchers are uncertain about is when the glycosidic bond is made. Two mechanisms have been proposed for the reaction. Because the substrate retained its configuration when a water molecule was …show more content…

The catalytic efficiency, or the catalytic factor, is known to be the ratio of the catalyzed rate to the uncatalyzed rate. As simple as this ratio may seem, it is hard to determine in most cases. The difficulty in determining these ratios is due to the inability to measure the uncatalyzed rate and the effects of an intramolecular catalyst if it is used in the reaction.
Linus Pauling mentioned that an enzyme was complementary to the transition state. This complementarity would allow the reaction catalyzed by the enzyme to occur at a lower activation energy and more quickly. Experiments have shown that the enzyme does not have complete complementarity with the substrate, but its partial complementarity still allows the reaction to occur. The complementarity of the enzyme to the substrate affects the catalytic efficiency such as the arrangement of the molecules in the active site and the electrostatics of the

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