4bt5

acetolactate decarboxylase with a bound (2S,3R)-2,3-Dihydroxy-2- methylbutanoic acid

spinqualitylabelsall models 4bt5, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bt5 is a 1 chain structure with sequence from Brevibacillus brevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: 23B, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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