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28 Sep 2019
When the aspartate at position 32 in subtilisin, a serineprotease, was converted to alanine by site-directed mutagenesis,the kcat value for the hydrolysis catalyzed by theenzyme fell to 0.005% of its wildtype value. Because Asp32 is acrucial part of the catalytic triad of this enzyme, provide ahypothesis to explain the residual enzyme activity after itsconversion to alanine.
When the aspartate at position 32 in subtilisin, a serineprotease, was converted to alanine by site-directed mutagenesis,the kcat value for the hydrolysis catalyzed by theenzyme fell to 0.005% of its wildtype value. Because Asp32 is acrucial part of the catalytic triad of this enzyme, provide ahypothesis to explain the residual enzyme activity after itsconversion to alanine.
Sixta KovacekLv2
28 Sep 2019