It has been shown that carbinolamides are intermediates in the enzyme-catalyzed synthesis of α-amidated peptides. Although carbinolamides are important intermediates in the production of these hormones and have roles in other biological functions, little attention has been given to their mechanisms of reaction in water, and, thus, it is difficult to speculate how their reaction is enzymatically catalyzed. The purpose of the work presented here was to synthesize structural analogs of the biological intermediates and study their mechanism of breakdown in water. α-Hydroxyhippuric acid (<b>1</b>), substrate for the enzymatic system, provides an easily modified template for the study of the breakdown of this carbinolamide system. The pH-rate profiles for various aromatic substituted derivatives of <b>1</b> will be presented, and the mechanism of the acid, hydroxide and buffer catalyzed reactions discussed. The effect of metal-ions of the rate of the reaction was also investigated as it is know that peptidylglycine α-amidating monooxygenase has a metal-cofactor whose role is poorly defined.

Aqueous kinetics of α-hydroxyhippuric acid derivatives as a function of pH, buffer and metal-ion concentration

2019 Spring National Meeting

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