4BT5

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

4BT5 の概要

• エントリーDOI: 10.2210/pdb4bt5/pdb
• 関連するPDBエントリー: 4BT2 4BT3 4BT4 4BT6 4BT7
• 分子名称: ALPHA-ACETOLACTATE DECARBOXYLASE, ZINC ION, (2S,3R)-2,3-dihydroxy-2-methylbutanoic acid, ... (4 entities in total)
• 機能のキーワード: lyase, acetoin biosynthesis, stereoselective decarboxylation, bifunctional enzyme
• 由来する生物種: BREVIBACILLUS BREVIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29030.16

構造登録者

A Marlow, V.,Rea, D.,Najmudin, S.,Wills, M.,Fulop, V. (登録日: 2013-06-12, 公開日: 2013-09-11, 最終更新日: 2023-12-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.1 Å)