4BT6

acetolactate decarboxylase with a bound glycerol

Summary for 4BT6

• Entry DOI: 10.2210/pdb4bt6/pdb
• Related: 4BT2 4BT3 4BT4 4BT5 4BT7
• Descriptor: ALPHA-ACETOLACTATE DECARBOXYLASE, ZINC ION, GLYCEROL, ... (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: 29264.41

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: 2023-12-20)

Primary citation

Marlow, V.A.,Rea, D.,Najmudin, S.,Wills, M.,Fulop, V.
Structure and Mechanism of Acetolactate Decarboxylase.
Acs Chem.Biol., 8:2339-, 2013

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/CB400429H

Experimental method

X-RAY DIFFRACTION (1.6 Å)