Structural highlights
Function
ALDC_BREBE
Publication Abstract from PubMed
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.
Structure and Mechanism of Acetolactate Decarboxylase.,Marlow VA, Rea D, Najmudin S, Wills M, Fulop V ACS Chem Biol. 2013 Aug 28. PMID:23985082[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marlow VA, Rea D, Najmudin S, Wills M, Fulop V. Structure and Mechanism of Acetolactate Decarboxylase. ACS Chem Biol. 2013 Aug 28. PMID:23985082 doi:10.1021/cb400429h