3IAE

Structure of benzaldehyde lyase A28S mutant with benzoylphosphonate

3IAE の概要

• エントリーDOI: 10.2210/pdb3iae/pdb
• 関連するPDBエントリー: 3IAF
• 分子名称: Benzaldehyde lyase, 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: thiamine adduct, lyase
• 由来する生物種: Pseudomonas fluorescens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121119.15

構造登録者

Brandt, G.S.,Petsko, G.A.,Ringe, D.,McLeish, M.J. (登録日: 2009-07-13, 公開日: 2010-03-02, 最終更新日: 2023-09-06)

主引用文献

Brandt, G.S.,Kneen, M.M.,Petsko, G.A.,Ringe, D.,McLeish, M.J.
Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition.
J.Am.Chem.Soc., 132:438-439, 2010

PubMed Abstract: Benzaldehyde lyase (BAL) from Pseudomonas putida is a thiamin diphosphate (ThDP)-dependent enzyme that catalyzes the breakdown of (R)-benzoin. Here we report that a point mutant, BAL A28S, not only catalyzes the decarboxylation of benzoylformate but, like benzoylformate decarboxylase (BFDC), is also inactivated by the benzoylformate analogues methyl benzoylphosphonate (MBP) and benzoylphosphonate (BP). The latter has no effect on wild-type BAL, and the inactivation of the A28S variant is shown to result from phosphorylation of the newly introduced serine residue. This lends support to the proposal that an appropriately placed nucleophile facilitates the expulsion of carbon dioxide from the active site in many ThDP-dependent decarboxylases.

PubMed: 20030408
DOI: 10.1021/ja907064w

実験手法

X-RAY DIFFRACTION (2.3 Å)