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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
Version:
Accepted manuscript

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Publisher copy:
10.1038/nchembio.2394

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Funding agency for:
Davis, BG
Engineering and Physical Sciences Research Council More from this funder
High Force Research More from this funder
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Chemical Biology Journal website
Volume:
13
Pages:
874–881
Publication date:
2017-06-05
Acceptance date:
2017-03-08
DOI:
ISSN:
1552-4469
Pubs id:
pubs:700677
URN:
uri:cbbc32e0-523f-446b-85a6-e6c4f2ba7c03
UUID:
uuid:cbbc32e0-523f-446b-85a6-e6c4f2ba7c03
Local pid:
pubs:700677
Language:
English
Keywords:

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