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Science 10 January 1986:
Vol. 231. no. 4734, pp. 145 - 148
DOI: 10.1126/science.3510454
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Articles

Science, Vol 231, Issue 4734, 145-148
Copyright © 1986 by American Association for the Advancement of Science

articles

Modification of the active site of alkaline phosphatase by site-directed mutagenesis

SS Ghosh, SC Bock, SE Rokita, and ET Kaiser

The catalytically essential amino acid in the active site of bacterial alkaline phosphatase (Ser-102) has been replaced with a cysteine by site-directed mutagenesis. The resulting thiol enzyme catalyzes the hydrolysis of a variety of phosphate monoesters. The rate-determining step of hydrolysis, however, is no longer the same for catalysis when the active protein nucleophile is changed from the hydroxyl of serine to the thiol of cysteine. Unlike the steady-state kinetics of native alkaline phosphatase, those of the mutant show sensitivity to the leaving group of the phosphate ester.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Tinkering with enzymes: what are we learning?.
J. Knowles (1987)
Science 236, 1252-1258
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