1eb8 | pdb_00001eb8
STRUCTURE DETERMINANTS OF SUBSTRATE SPECIFICITY OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA
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Overview
Tryptophan 128 of hydroxynitrile lyase of Manihot esculenta (MeHNL) covers, a significant part of a hydrophobic channel that gives access to the, active site of the enzyme. This residue was therefore substituted in the, mutant MeHNL-W128A by alanine to study its importance for the substrate, specificity of the enzyme. Wild-type MeHNL and MeHNL-W128A showed, comparable activity on the natural substrate acetone cyanohydrin (53 and, 40 U/mg, respectively). However, the specific activities of MeHNL-W128A, for the unnatural substrates mandelonitrile and 4-hydroxymandelonitrile, are increased 9-fold and approximately 450-fold, respectively, compared, with the wild-type MeHNL. The crystal structure of the MeHNL-W128A, substrate-free form at 2.1 A resolution indicates that the W128A, substitution ... [(full description)]
About this Structure
1EB8 is a [Single protein] structure of sequence from [Manihot esculenta] with MPD as [ligand]. Active as [Transferred entry: 3.3.2.4], with EC number [4.2.1.37]. Structure known Active Site: ASA. Full crystallographic information is available from [OCA].
Reference
Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta., Lauble H, Miehlich B, Forster S, Kobler C, Wajant H, Effenberger F, Protein Sci. 2002 Jan;11(1):65-71. PMID:11742123
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