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对酶进行调整:我们学到了什么?

Tinkering with enzymes: what are we learning?

作者信息

Knowles J R

出版信息

Science. 1987 Jun 5;236(4806):1252-8. doi: 10.1126/science.3296192.

Abstract

It is now possible, by site-directed mutagenesis of the gene, to change any amino acid residue in a protein to any other. In enzymology, application of this technique is leading to exciting new insights both into the mechanism of catalysis by particular enzymes, and into the basis of catalysis itself. The precise and often delicate changes that are being made in and near the active sites of enzymes are illuminating the interdependent roles of catalytic groups, and are allowing the first steps to be taken toward the rational alteration of enzyme specificity and reactivity.

摘要

现在,通过对基因进行定点诱变,可以将蛋白质中的任何氨基酸残基替换为其他任何氨基酸残基。在酶学领域,这项技术的应用正在为我们带来令人兴奋的新见解,既涉及特定酶的催化机制,也关乎催化作用本身的基础。在酶的活性位点及其附近所进行的精确且往往微妙的改变,正揭示着催化基团的相互依存作用,并使我们朝着合理改变酶的特异性和反应性迈出了第一步。

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