Title : The importance of precise positioning of negatively charged carboxylate in the catalytic action of human lysozyme.

Pub. Date : 1991 Aug 30

PMID : 1911846






3 Functional Relationships(s)
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1 The role of aspartic acid 53 of human lysozyme (peptidoglycan N-acetylmuramoylhydrolase, EC 3.2.1.17) has been investigated by a site-directed mutagenesis. Aspartic Acid lysozyme Homo sapiens
2 These results indicate that the precise positioning of the negatively charged carboxylate in the geometry of reaction center is essential for the rate enhancement in the catalytic action of lysozyme, and suggest that Asp-53 of human lysozyme participates in the catalytic action not simply in an electrostatical manner but partly in a nucleophilical manner. Aspartic Acid lysozyme Homo sapiens
3 These results indicate that the precise positioning of the negatively charged carboxylate in the geometry of reaction center is essential for the rate enhancement in the catalytic action of lysozyme, and suggest that Asp-53 of human lysozyme participates in the catalytic action not simply in an electrostatical manner but partly in a nucleophilical manner. Aspartic Acid lysozyme Homo sapiens