Detection of enzyme-bound intermediates by cross-saturation in nuclear magnetic resonance spectroscopy; an investigation of the papain–N-benzoylaminoacetaldehyde complex

Abstract

A hemithioacetal formed between the active site thiol of the proteolytic enzyme papain, and the inhibitor N-benzoylaminoacetaldehyde, has been detected by a double resonance experiment in which magnetisation is transferred between the enzyme-bound and free inhibitor.