126530-12-9Relevant articles and documents
Expanded structural and stereospecificity in peptide synthesis with chemically modified mutants of subtilisin
Khumtaveeporn, Kanjai,DeSantis, Grace,Jones, J. Bryan
, p. 2563 - 2572 (1999)
Employing the strategy of combined site directed mutagenesis and chemical modification, we previously generated chemically modified mutant enzymes (CMMs) of subtilisin Bacillus lentus (SBL). We now report the use of these SBL-CMMs for peptide coupling rea
Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis
Matsumoto,Davis,Jones
, p. 903 - 904 (2007/10/03)
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- ami