Substratbedingte Nachbargruppeneffekte als bestimmende Faktoren bei der enzymatischen Hydrolyse. II. Kinetische Untersuchungen an Chymotrypsin-Substraten

✍ Scribed by Ernst Wenger; Hans Urheim; Max Rottenberg

• Publisher: John Wiley and Sons
• Year: 1962
• Tongue: German
• Weight: 362 KB
• Volume: 45
• Category: Article
• ISSN: 0018-019X
• DOI: 10.1002/hlca.19620450330

✦ Synopsis

Abstract

Kinetic evidence is presented to demonstrate that α‐acylamino esters and N‐acyl‐dipeptide esters exhibit unusually high reactivities toward neutral and alkaline hydrolysis. The authors infer that the same must be true for other typical chymotrypsin substrates such as dipeptide amides, higher peptides and proteins, the peptide carbonyl acting in each case as a rate‐enhancing neighbouring group. They conclude that, quite generally, the peptide bond in enzyme proteins does not merely serve as a backbone to support the functional groups but that, on the contrary, the amide groups may themselves participate both as nucleophilic and as electrophilic centers in the enzymatic reactions.