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Science 11 September 1959:
Vol. 130. no. 3376, pp. 625 - 626
DOI: 10.1126/science.130.3376.625
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Articles

Mechanism of Enzyme Inhibition by Phosphate Esters

SIDNEY A. BERNHARD 1 and LESLIE E. ORGEL 1

1 Hallett Hall, Boulder, Colorado

A theory for the rapid specific reaction of certain phosphorous-containing esters with many proteolytic enzymes based on the ability of phosphorous to form one additional bond relative to carbon is presented. A stable tetrahedral phosphate ester is compared with a labile tetrahedral orthocarbonyl ester and a relatively stable pentagonal enzyme-phosphate ester complex is compared with a pentagonal enzyme-carbonyl substrate complex. The latter complex is assumed to be the transition state in the enzyme-catalyzed reaction. If the theory is correct, it opens up the possibility of studying intermediates and transition states from the known structures of chemical inhibitors.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
How do enzymes work?.
J Kraut (1988)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)