Co-Authors:
Moult, J., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Eshdat, Y., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Sharon, N., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Abstract:
Tetragonal crystals of hen egg-white lysozyme were treated with the active sitedirected irreversible inhibitor 2′,3′epoxypropyl β-glycoside of N-acetyl-d-glucosamine, β(1→4)-linked dimer. The crystals were examined by X-ray crystallography, and the results compared to those obtained from crystals of the reversible complex formed between hen egg-white lysozyme and the β-phenyl glycoside of GlcNAc β(1→4)GlcNAc. It is concluded that the GlcNAc β(1→4)GlcNAc moiety of the irreversible inhibitor occupies subsites B and C in the active site of the enzyme, and that the inhibitor is linked covalently to the enzyme through the carboxyl side-chain of Asp 52. © 1973.
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