Transition‐state analogs of an aliphatic amidase

摘要: The use of transition-state analogs in the elucidation enzyme mechanisms has assumed importance recent years [ 1,2] . idea that synthetic compounds resembling proposed should be extremely effective inhibitors compared to ground-state analogs, and bind more effectively even than substrate, been substantiated. Recent studies with papain [3] elastase [4] showing aldehydes appropriate peptide side chains are led proposal free aldehyde reacts an amino acid residue (cysteine-papain; setie-elastase) active centre form a hemithibacetal or hemiacetal; this being ‘true’ analog on reaction pathway acylenzyme formation. Aldehydes, however, exist appreciable amounts aqueous solution as hydrates formed rapidly by general base catalysed [S] At present time there is no way determining whether true inhibitor its hydrate. This paper presents evidence that, at least for aliphatic amidase from Pseudomonas aeruginosa, it hydrated inhibitor. T%is conclusion substantiated observation acetaldehyde-ammonia potent might considered amide hydrolysis.