7UTW

Cd-substituted Horse Liver Alcohol Dehydrogenase in Complex with NADH and N-Cyclohexylformamide

7UTW の概要

• エントリーDOI: 10.2210/pdb7utw/pdb
• 分子名称: Alcohol dehydrogenase E chain, CADMIUM ION, ZINC ION, ... (6 entities in total)
• 機能のキーワード: ternary complex, oxidoreductase
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82017.80

構造登録者

Zheng, C.,Boxer, S.G. (登録日: 2022-04-27, 公開日: 2023-02-01, 最終更新日: 2023-12-13)

主引用文献

Zheng, C.,Ji, Z.,Mathews, I.I.,Boxer, S.G.
Enhanced active-site electric field accelerates enzyme catalysis.
Nat.Chem., 15:1715-1721, 2023

PubMed Abstract: The design and improvement of enzymes based on physical principles remain challenging. Here we demonstrate that the principle of electrostatic catalysis can be leveraged to substantially improve a natural enzyme's activity. We enhanced the active-site electric field in horse liver alcohol dehydrogenase by replacing the serine hydrogen-bond donor with threonine and replacing the catalytic Zn with Co. Based on the electric field enhancement, we make a quantitative prediction of rate acceleration-50-fold faster than the wild-type enzyme-which was in close agreement with experimental measurements. The effects of the hydrogen bonding and metal coordination, two distinct chemical forces, are described by a unified physical quantity-electric field, which is quantitative, and shown here to be additive and predictive. These results suggest a new design paradigm for both biological and non-biological catalysts.

PubMed: 37563323
DOI: 10.1038/s41557-023-01287-x

実験手法

X-RAY DIFFRACTION (1.33 Å)