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Journal article

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

Abstract:
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 corresponding dipeptides in good yields as a result of greatly broadened substrate specificities that can be rationalized by the interaction of the glycans acting as chiral auxiliaries in stereochemically mismatched pairs.
Publication status:
Published

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Publisher copy:
10.1039/b010021h

Authors

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author


Journal:
CHEMICAL COMMUNICATIONS More from this journal
Issue:
10
Pages:
903-904
Publication date:
2001-01-01
DOI:
EISSN:
1364-548X
ISSN:
1359-7345


Language:
English
Pubs id:
pubs:52091
UUID:
uuid:f3b2ffa8-d66b-4b7f-9d6b-9ef7cde674f2
Local pid:
pubs:52091
Source identifiers:
52091
Deposit date:
2012-12-19
ARK identifier:

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