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A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase.

Abstract:

SNi-like mechanisms, which involve front-face leaving group departure and nucleophile approach, have been observed experimentally and computationally in chemical and enzymatic substitution at α-glycosyl electrophiles. Since SNi-like, SN1 and SN2 substitution pathways can be energetically comparable, engineered switching could be feasible. Here, engineering of Sulfolobus solfataricus β-glycosidase, which originally catalyzed double SN2 substitution, changed its mode to SNi-like. Destruction of...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/nchembio.2394

Authors


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Name:
Royal Society
Funding agency for:
Davis, B
Grant:
Wolfson Research Merit Award
More from this funder
Name:
Catalan Agency for Management of University and Research Grants
Grant:
2014SGR-987
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Name:
Spanish Ministry of Economy, Industry and Competitiveness
Grant:
CTQ2014-55174
More from this funder
Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/E004350/1
Publisher:
Nature Publishing Group
Journal:
Nature Chemical Biology More from this journal
Volume:
13
Pages:
874–881
Publication date:
2017-06-01
Acceptance date:
2017-03-08
DOI:
ISSN:
1552-4469
Language:
English
Keywords:
Pubs id:
pubs:700677
UUID:
uuid:cbbc32e0-523f-446b-85a6-e6c4f2ba7c03
Local pid:
pubs:700677
Source identifiers:
700677
Deposit date:
2017-07-08

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