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Structure and mechanism of acetolactate decarboxylase
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Marlow, Victoria A., Rea, Dean, Najmudin, Shabir, Wills, Martin and Fülöp, Vilmos (2013) Structure and mechanism of acetolactate decarboxylase. ACS Chemical Biology, 8 (10). pp. 2339-2344. doi:10.1021/cb400429h ISSN 1554-8929.
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WRAP_Fulop_9773196-lf-170913-cb-2013-00429h-wrap.pdf - Accepted Version Download (1109Kb) | Preview |
Official URL: http://dx.doi.org/10.1021/cb400429h
Abstract
Acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that has been shown to involve a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer. In this paper, a series of crystal structures of ALDC complex with designed transition state mimics are reported. These structures, coupled with inhibition studies and site-directed mutagenesis provide an improved understanding of the molecular processes involved in the stereoselective decarboxylation/protonation events. A mechanism for the transformation of each enantiomer of acetolactate is proposed.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QD Chemistry | ||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
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Library of Congress Subject Headings (LCSH): | Acetolactate synthase, Decarboxylation, Proton transfer reactions | ||||||||
Journal or Publication Title: | ACS Chemical Biology | ||||||||
Publisher: | American Chemical Society | ||||||||
ISSN: | 1554-8929 | ||||||||
Official Date: | 18 October 2013 | ||||||||
Dates: |
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Volume: | 8 | ||||||||
Number: | 10 | ||||||||
Page Range: | pp. 2339-2344 | ||||||||
DOI: | 10.1021/cb400429h | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||
Date of first compliant deposit: | 25 December 2015 | ||||||||
Date of first compliant Open Access: | 25 December 2015 | ||||||||
Funder: | Engineering and Physical Sciences Research Council (EPSRC) |
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