A site-directed mutagenesis experiment was done on the catalytic triad of the serine protease subtilisin where all of the amino acids of the catalytic triad were mutated to alanine. The triple mutant enzyme was characterized kinetically and the mutant displayed a thousand-fold (103) rate enhancement over the uncatalyzed reaction. Explain the source of this rate enhancement.  (The native wild-type subtilisin has a rate acceleration of 1010,  when compared to the uncatalyzed reaction.)

Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Chapter15: From Dna To Protein
Section: Chapter Questions
Problem 15TYK
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A site-directed mutagenesis experiment was done on the catalytic triad of the serine protease subtilisin where all of the amino acids of the catalytic triad were mutated to alanine. The triple mutant enzyme was characterized kinetically and the mutant displayed a thousand-fold (103) rate enhancement over the uncatalyzed reaction. Explain the source of this rate enhancement.  (The native wild-type subtilisin has a rate acceleration of 1010,  when compared to the uncatalyzed reaction.)
 
 
 
 
 
 
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