| Abstract: | Hen egg-white lysozyme was the first enzyme whose tertiary structure could be elucidated. The peptide chain of this enzyme is arranged in two sections, of approximately equal size, that are separated by a deep cleft. Substrates (and inhibitors) are bound in this cleft via hydrogen bonds and are hydrolyzed under the action of Glu 35 and Asp 52, which form the active site of the enzyme. Although the lysozymes, which occur in many species of animals and plants, exhibit differences in their chemical behavior, they have the same qualitative biological activity; quantitatively important differences have been noted which also concern the specificity. Infection of E. coli with bacteriophages gives rise to a lysozyme whose formation is controlled by the phage DNA. The fact that mutated lysozymes are produced when the phages are treated with mutagens opens new fields of research in molecular biology. |
