4BT2

acetolactate decarboxylase with a bound 1,2-ETHANEDIOL

Summary for 4BT2

Entry DOI	10.2210/pdb4bt2/pdb
Related	4BT3 4BT4 4BT5 4BT6 4BT7
Descriptor	ALPHA-ACETOLACTATE DECARBOXYLASE, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywords	lyase, acetoin biosynthesis, stereoselective decarboxylation, bifunctional enzyme
Biological source	BREVIBACILLUS BREVIS
Total number of polymer chains	1
Total formula weight	28958.10
Authors	A Marlow, V.,Rea, D.,Najmudin, S.,Wills, M.,Fulop, V. (deposition date: 2013-06-12, release date: 2013-09-11, Last modification date: 2024-05-08)
Primary citation	A Marlow, V.,Rea, D.,Najmudin, S.,Wills, M.,Fulop, V. Structure and Mechanism of Acetolactate Decarboxylase Acs Chem.Biol., 8:2339-, 2013 Cited by PubMed 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. PubMed: 23985082 DOI: 10.1021/CB400429 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.1 Å)

Structure validation