1DWO

Crystal Structure of Hydroxynitrile Lyase from Manihot esculenta in Complex with Substrates Acetone and Chloroacetone:Implications for the Mechanism of Cyanogenesis

Summary for 1DWO

Entry DOI	10.2210/pdb1dwo/pdb
Related	1DWP 1DWQ
Descriptor	HYDROXYNITRILE LYASE, ACETONE (3 entities in total)
Functional Keywords	hydroxynitrile lyase, acetone complex
Biological source	MANIHOT ESCULENTA (CASSAVA)
Total number of polymer chains	2
Total formula weight	59728.50
Authors	Lauble, H.,Forster, S.,Miehlich, B.,Wajant, H.,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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation