Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis
Site-selective glycosylation at position 166 at the base of the primary specificity S1 pocket in the serine protease subtilisin Bacillus lentus (SBL) created glycoproteins that are capable of catalyzing the coupling reactions of not only L- amino acid esters but also D-amino acid esters to give the...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2001
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