7YCT

HYDROXYNITRILE LYASE FROM THE MILLIPEDE, Oxidus gracilis complexed with (R)-2-Chloromandelonitrile

7YCT の概要

• エントリーDOI: 10.2210/pdb7yct/pdb
• 分子名称: Hydroxynitrile lyase, (2~{R})-2-(2-chlorophenyl)-2-oxidanyl-ethanenitrile, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Oxidus gracilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 83481.92

構造登録者

Chaikaew, S.,Watanabe, Y.,Zheng, D.,Motojima, F.,Asano, Y. (登録日: 2022-07-01, 公開日: 2024-01-24, 最終更新日: 2024-11-13)

主引用文献

Chaikaew, S.,Watanabe, Y.,Zheng, D.,Motojima, F.,Yamaguchi, T.,Asano, Y.
Structure-Based Site-Directed Mutagenesis of Hydroxynitrile Lyase from Cyanogenic Millipede, Oxidus gracilis for Hydrocyanation and Henry Reactions.
Chembiochem, 25:e202400118-e202400118, 2024

PubMed Abstract: Hydroxynitrile lyase (HNL) from the cyanogenic millipede Oxidus gracillis (OgraHNL) is a crucial enzyme in the cyanogenesis pathway. Here, the crystal structures of OgraHNL complexed with sulfate, benzaldehyde (BA), (R)-mandelonitrile ((R)-Man), (R)-2-chloromandelonitrile ((R)-2-Cl-Man), and acetone cyanohydrin (ACN) were solved at 1.6, 1.7, 2.3, 2.1, and 2.0 Å resolutions, respectively. The structure of OgraHNL revealed that it belonged to the lipocalin superfamily. Based on this structure, positive variants were designed to further improve the catalytic activity and enantioselectivity of the enzyme for asymmetric hydrocyanation and Henry reactions.

PubMed: 38526556
DOI: 10.1002/cbic.202400118

実験手法

X-RAY DIFFRACTION (2.01 Å)