Abstract
A THREE-dimensional model of the ES-complex formed between a chito-oligosaccharide and hen egg white lyso-zyme was presented by Blake et al. as a result of X-ray crystallographic investigations1. We reported that partially O-carboxymethylated chitin, which had satisfactory solubility, was highly susceptible to the action of lysozyme2 where the contents of the carboxymethyl groups were very roughly 0.3 mole/mole of N-acetoglucosamine residue. It is to be expected that the fairly bulky O-substituents will not permit such a free binding as that between unsubstituted chito-oligosaccharides and the enzyme, but will force the enzyme to select some suitable portions of the substrate molecules for making the ES-complex. Although it is impossible to know the exact location of the O-substituents on the high molecular substrate, the location of those on the enzymatic reaction products—which are low molecular compounds—can be determined. The orientation of the O-substituents in the product molecules must be reflexions of the conformation of the binding sub-sites in the ES-complex, because those suitable portions of the substrate molecule must have been fitted in the sub-sites before being released as low molecular saccharides.
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References
Blake, C. C. F., Johnson, L. N., Mair, G. A., North, A. C. T., Phillips, D. C., and Sarma, V. R., Proc. Roy. Soc., B 167, 378 (1967).
Matsushima, Y., Hara, S., Miyazaki, T., and Umemura, Y., Thirty-eighth Annual Meeting of Japanese Biochemical Society (October 1965).
Miyazaki, T., and Matsushima, Y., Twenty-first Annual Meeting of the Chemical Society of Japan (April 1968).
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MATSUSHIMA, Y., MIYAZAKI, T. & KASAI, S. Chemical Evidence for the Phillips Model of the Action of Hen Egg White Lysozyme. Nature 219, 265 (1968). https://doi.org/10.1038/219265a0
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DOI: https://doi.org/10.1038/219265a0
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