Abstract
BLAKE et al. proposed that during cleavage of oligosaccharides, the saccharide bound in subsite D of the active site of lysozyme is distorted into a half chair conformation1,2. In agreement with this mechanism, Dahlquist et al.3,4 concluded that considerable carbonium ion character is involved in the hydrolysis of the synthetic substrate phenyl-4-O-(2-deoxy-2-acetamido-β-D-glucopyranosyl)-β-D-glucopyranoside (NAG-GLU-ϕ). Lowe and Sheppard5 found, however, in their study of the hydrolysis of NAG-GLU-(ϕNO2 that participation of the acetamido group is important in the lysozyme mechanism.
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References
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SYKES, B., DOLPHIN, D. The Role of Distortion in the Lysozyme-catalysed Hydrolysis of Glucosides. Nature 233, 421–422 (1971). https://doi.org/10.1038/233421a0
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DOI: https://doi.org/10.1038/233421a0
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