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Structure and Mechanism of Acetolactate Decarboxylase

DOI: 10.1021/cb400429h DOI Help
PMID: 23985082 PMID Help

Authors: Vicky Marlow (University of Warwick) , Dean Rea (University of Warwick) , Shabir Najmudin (Universidade T├ęcnica de Lisboa) , Martin Wills (The University of Warwick) , Vilmos Fulop (Department of Biological Sciences, University of Warwick)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acs Chemical Biology , VOL 8 (10)

State: Published (Approved)
Published: August 2013
Diamond Proposal Number(s): 6388

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.

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Other Facilities: BM14 at ESRF 9.6 at SRS, Daresbury

Added On: 29/08/2013 11:46

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