The Detection of Substrate Distortion by Lysozyme: An Appli¬cation of NMR to the Study of Enzyme Substrate Reactions
Patt, S.L., David Dolphin, and Sykes, B.D.
Ann. N.Y. Acad. Sci.
The title topics are considered in relation to the lysozyme-catalyzed cleavage of the tetrasaccharide (NAG-NAM)2 (NAG = 2-acetamido-2-deoxy-D-glucopyranose; NAM = 2-acetamido-2-deoxy-D-muramic acid) from Micrococcus lysodeikticus. The processes are subjected to mathematical and spectrographic interpretation. Two methods indicated approximately50% cleavage of the tetramer by the enzyme. There was a clear indication that the reducing ring of NAG-NAM2 was substantially distorted towards a half-chair conformation when bound to the enzyme. Only the α-anomer, which, according to NMR integration, forms approximately 60% of the total tetramer, was observed. Probably the same effects occur with both anomeric forms.