Pub No:
45
Title:
The Detection of Substrate Distortion by Lysozyme: An Appli¬cation of NMR to the Study of Enzyme Substrate Reactions
Authors:
Patt, S.L., David Dolphin, and Sykes, B.D.
Journal:
Ann. N.Y. Acad. Sci.
Year:
1973
Pages:
222, 211-219
Abstract:
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.

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