Mechanism and stereoelectronic effects in the lysozyme reaction.
Lysozyme occupies a special place in the history of enzymology as the first enzyme to have its three-dimensional crystal structure elucidated by Phillips and co-workers in 1965. The crystallography, and much biochemical work, revealed three factors likely to be important for the mechanism of action: catalysis by the carboxyl group of Glu-35, catalysis by the ionized carboxyl group of Asp-52, and the conformation of the bound polysaccharide substrate. The work of the last 20 years has defined likely roles for the catalytic groups, but discussion of the conformational question came to a head only very recently with the suggestion that the fundamental stereoelectronic requirements of the glycoside-cleavage reaction might be decisive. Recent work on all three interlinked factors are reviewed.
Kirby
A J
AJ
University Chemical Laboratory, University of Cambridge, England.
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D009113:Muramidase / Q000378:metabolism*; D011487:Protein Conformation; D013237:Stereoisomerism
D009113:Muramidase