Article
Covalent modification of subtilisin Bacillus lentus cysteine mutants with enantiomerically pure chiral auxiliaries causes remarkable changes in activity.
Bioorganic & medicinal chemistry - 1 Aug 2000
Dickman M, Jones J B
Abstract excerpt
Methanethiosulfonate reagents may be used to introduce virtually unlimited structural modifications in enzymes via reaction with the thiol group of cysteine. The covalent coupling of enantiomerically pure (R) and (S) chiral auxiliary methanethiosulfonate ligands to cysteine mutants of subtilisin Bacillus lentus induces spectacular changes in catalytic activity between diastereomeric enzymes. Amidase and esterase...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
