1dwq | pdb_00001dwq
CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS
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Overview
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.
About this Structure
1DWQ is a [Single protein] structure of sequence from [Manihot esculenta] with ATO as [ligand]. Active as [Transferred entry: 3.3.2.4], with EC number [4.2.1.37]. Structure known Active Sites: ASA and ASB. Full crystallographic information is available from [OCA].
Reference
Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis., Lauble H, Forster S, Miehlich B, Wajant H, Effenberger F, Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):194-200. PMID:11173464
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