1DWP

Crystal Structure of Hydroxynitrile Lyase from Manihot esculenta at 2.2 Angstrom Resolution

1DWP の概要

• エントリーDOI: 10.2210/pdb1dwp/pdb
• 関連するPDBエントリー: 1DWO 1DWQ
• 分子名称: HYDROXYNITRILE LYASE, ACETATE ION (3 entities in total)
• 機能のキーワード: hydroxynitrile lyase, cyanogenesis
• 由来する生物種: MANIHOT ESCULENTA (CASSAVA)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59788.51

構造登録者

Lauble, H.,Wagner, U.,Kratky, C.,Mielich, B.,Wajant, H.,Forster, S.,Effenberger, F. (登録日: 1999-12-10, 公開日: 2000-12-07, 最終更新日: 2024-05-08)

主引用文献

Lauble, H.,Forster, S.,Miehlich, B.,Wajant, H.,Effenberger, F.
Structure of Hydroxynitrile Lyase from Manihot Esculenta in Complex with Substrates Acetone and Chloroacetone: Implications for the Mechanism of Cyanogenesis
Acta Crystallogr.,Sect.D, 57:194-, 2001

PubMed Abstract: The crystal structures of hydroxynitrile lyase from Manihot esculenta (MeHNL) complexed with the native substrate acetone and substrate analogue chloroacetone have been determined and refined at 2.2 A resolution. The substrates are positioned in the active site by hydrogen-bond interactions of the carbonyl O atom with Thr11 OG, Ser80 OG and, to a lesser extent, Cys81 SG. These studies support a mechanism for cyanogenesis as well as for the stereospecific MeHNL-catalyzed formation of (S)-cyanohydrins, which closely resembles the base-catalyzed chemical reaction of HCN with carbonyl compounds.

PubMed: 11173464
DOI: 10.1107/S0907444900015766

実験手法

X-RAY DIFFRACTION (2.2 Å)