1DWP

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

Summary for 1DWP

• Entry DOI: 10.2210/pdb1dwp/pdb
• Related: 1DWO 1DWQ
• Descriptor: HYDROXYNITRILE LYASE, ACETATE ION (3 entities in total)
• Functional Keywords: hydroxynitrile lyase, cyanogenesis
• Biological source: MANIHOT ESCULENTA (CASSAVA)
• Total number of polymer chains: 2
• Total formula weight: 59788.51

Authors

Lauble, H.,Wagner, U.,Kratky, C.,Mielich, B.,Wajant, H.,Forster, S.,Effenberger, F. (deposition date: 1999-12-10, release date: 2000-12-07, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)