title: Structure and mechanism of acetolactate decarboxylase.
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.
authors.affiliation: MOAC Doctoral Training Centre, The University of Warwick , Coventry, CV4 7AL, United Kingdom.
authors.forename: Victoria A
authors.initials: VA
authors.lastname: Marlow
authors.forename: Dean
authors.initials: D
authors.lastname: Rea
authors.forename: Shabir
authors.initials: S
authors.lastname: Najmudin
authors.forename: Martin
authors.initials: M
authors.lastname: Wills
authors.forename: Vilmos
authors.initials: V
authors.lastname: Fülöp
mesh_terms: D001407:Bacillus / Q000201:enzymology; D002262:Carboxy-Lyases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003653:Decarboxylation; D008958:Models, Molecular; D013237:Stereoisomerism
chemical_list: D002262:Carboxy-Lyases; C023746:acetolactate decarboxylase