Abstract
N-(N- Acetyl- l-phenylalanyl)glycinenitrile is a reversible inhibitor of papain which forms a thioimidate adduct with the cysteine thiol in the enzyme's active site. It is possible for this thioimidate to undergo reactions with external thiols, namely β-mercaptoethanol and N-acetylcysteamine. The reactions were followed by 13C- and 15N-NMR techniques which indicated that the initial nitrile was converted to N-(N- acetyl- l-phenylalanyl)glycinamide and then further hydrolysed to N-(N- acetyl- l-phenylalanyl)glycine . In essence papain is acting as a nitrile hydratase, and this activity, coupled with papain's well-characterized amidase activity, results in the synthesis of a carboxylic acid from a nitrile).
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