Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis

Citation
K. Matsumoto et al., Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis, CHEM COMMUN, (10), 2001, pp. 903-904
Citations number
15
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry
Journal title
CHEMICAL COMMUNICATIONS
ISSN journal
1359-7345 → ACNP
Issue
10
Year of publication
2001
Pages
903 - 904
Database
ISI
SICI code
1359-7345(2001):10<903:GOTPBP>2.0.ZU;2-X
Abstract
Site-selective glycosylation at position 166 at the base of the primary spe cificity S-1 pocket in the serine protease subtilisin Bacillus lentus (SBL) created glycoproteins that are capable of catalyzing the coupling reaction s of not only L-amino acid esters but also D-amino acid esters to give the corresponding dipeptides in good yields as a result of greatly broadened su bstrate specificities that can be rationalized by the interaction of the gl ycans acting as chiral auxiliaries in stereochemically mismatched pairs.