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...

詳細記述

書誌詳細
主要な著者: Matsumoto, K, Davis, B, Jones, J
フォーマット: Journal article
言語:English
出版事項: 2001