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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 DOI10.2210/pdb1dwo/pdb
Related1DWP 1DWQ
DescriptorHYDROXYNITRILE LYASE, ACETONE (3 entities in total)
Functional Keywordshydroxynitrile lyase, acetone complex
Biological sourceMANIHOT ESCULENTA (CASSAVA)
Total number of polymer chains2
Total formula weight59728.50
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 citationLauble, 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

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