1e8d | pdb_00001e8d
MECHANISTIC ASPECTS OF CYANOGENESIS FROM ACTIVE SITE MUTANT SER80ALA OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH ACETONE CYANOHYDRIN
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Overview
The structure and function of hydroxynitrile lyase from Manihot esculenta, (MeHNL) have been analyzed by X-ray crystallography and site-directed, mutagenesis. The crystal structure of the MeHNL-S80A mutant enzyme has, been refined to an R-factor of 18.0% against diffraction data to 2.1-A, resolution. The three-dimensional structure of the MeHNL-S80A-acetone, cyanohydrin complex was determined at 2.2-A resolution and refined to an, R-factor of 18.7%. Thr11 and Cys81 involved in substrate binding have been, substituted by Ala in site-directed mutagenesis. The kinetic measurements, of these mutant enzymes are presented. Combined with structural data, the, results support a mechanism for cyanogenesis in which His236 as a general, base abstracts a proton from Ser80, thereby allowing proton ... [(full description)]
About this Structure
1E8D is a [Single protein] structure of sequence from [Manihot esculenta] with CNH 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
Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin., Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F, Protein Sci. 2001 May;10(5):1015-22. PMID:11316882
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