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Science 21 August 1987:
Vol. 237. no. 4817, pp. 905 - 909
DOI: 10.1126/science.3112942
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Articles

Science, Vol 237, Issue 4817, 905-909
Copyright © 1987 by American Association for the Advancement of Science

articles

The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis

S Sprang, T Standing, RJ Fletterick, RM Stroud, J Finer-Moore, NH Xuong, R Hamlin, WJ Rutter, and CS Craik

The structure of the Asn102 mutant of trypsin was determined in order to distinguish whether the reduced activity of the mutant at neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine. The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton.


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