9FD8

Re-engineered peroxygenase variant of 2-deoxy-D-ribose-5-phosphate aldolase, Schiff-base complex with 4-chloro-cinnamaldehyde

これはPDB形式変換不可エントリーです。

9FD8 の概要

• エントリーDOI: 10.2210/pdb9fd8/pdb
• 分子名称: Deoxyribose-phosphate aldolase, (2E)-3-(4-chlorophenyl)prop-2-enal, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: protein engineering, directed evolution, aldolase, peroxygenase, schiff base, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57860.80

構造登録者

Thunnissen, A.M.W.H.,Zhou, H.,Frietema, H.O.T.,Poelarends, G.J. (登録日: 2024-05-16, 公開日: 2025-03-12, 最終更新日: 2025-05-21)

主引用文献

Zhou, H.,Kunzendorf, A.,Xu, G.,Frietema, H.O.T.,Thunnissen, A.W.H.,Poelarends, G.J.
Engineering 2-Deoxy-D-ribose-5-phosphate Aldolase for anti- and syn-Selective Epoxidations of alpha , beta-Unsaturated Aldehydes.
Angew.Chem.Int.Ed.Engl., 64:e202503054-e202503054, 2025

PubMed Abstract: The enzyme 2-deoxy-D-ribose-5-phosphate aldolase (DERA) naturally catalyzes the reversible aldol addition between acetaldehyde and D-glyceraldehyde-3-phosphate to yield 2-deoxy-D-ribose-5-phosphate. Herein we describe the redesign of DERA into a proficient non-natural peroxygenase that promotes the asymmetric epoxidation of various α,β-unsaturated aldehydes. This repurposed aldolase, named DERA-EP, is able to utilize HO to accomplish both anti- and syn-selective epoxidations of various α,β-unsaturated aldehydes to give the corresponding epoxides with moderate to high diastereoselectivity (diastereomeric ratio up to 99 : 1) and excellent enantioselectivity (enantiomeric ratio up to 99 : 1). Crystallographic analysis of DERA-EP in a substrate-free and substrate-bound state provides a structural context for the evolved activity, a clear explanation for the high enantioselectivity, and compelling evidence for catalysis via enzyme-bound iminium ion intermediates. The unprecedented anti-selectivity of DERA-EP with multiple α,β-unsaturated aldehydes is complementary to the syn-selectivity of previously reported enzyme-, metal- and organo-catalysts, making DERA-EP an attractive new asset to the toolbox of epoxidation catalysts.

PubMed: 39993220
DOI: 10.1002/anie.202503054

実験手法

X-RAY DIFFRACTION (1.58 Å)