Carnosine-anserine synthetase of muscle: III. Experiments on the mechanism of peptide bond formation

Abstract

Studies of the mechanism of carnosine and anserine formation have been performed with an ATP-dependent enzyme from chick muscle. The process of dipeptide formation was strongly inhibited by the addition of pyrophosphate or hydroxylamine. Although several techniques were used, it was not possible to detect an activated β-alanine intermediate. Synthetic β-alanine adenylate was found to react non-enzymically with histidine and methylhistidine, and also with other types of amino acids, to form peptides. Accordingly its role in carnosine-anserine biosynthesis could not be readily ascertained.