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Holger Bühler, Franz Effenberger, Siegfried Förster, Jürgen Roos and Harald Wajant Substrate Specificity of Mutants of the Hydroxynitrile Lyase from Manihot esculenta ChemBioChem 4

Version of Record online: 27 FEB 2003 | DOI: 10.1002/cbic.200390033

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Tryptophan is a bulky doorman: The enantioselective formation of (S)-cyanohydrins from a variety of aldehydes catalyzed by the hydroxynitrile lyase from Manihot esculenta or one of several mutants was investigated (see scheme). Tryptophan128, which blocks the channel entrance to the active site of the wild-type enzyme, was substituted by amino acids with decreasing size. As demonstrated in the preparation of the pyrethroid precursor (S)-3-phenoxybenzaldehyde cyanohydrin, the bulkiness of the amino acids plays an important role as determinant for reactivity and substrate specificity.

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