E. L. Smith, N. Slonim
Nov 1, 1948
Citations
0
Influential Citations
32
Citations
Journal
The Journal of biological chemistry
Abstract
Since Linderstr@m-Lang’s demonstration that the hydrolysis of Lleucylglycine (LG) is due to a distinctileucyl peptidase (l), various studies have shown that this enzyme is widely distributed (24) and requires for its activity the presence of Mn++ or Mg++ ions (2, 5). The enzyme has been regarded as a typical aminopeptidase (5), since it does not hydrolyze acylated compounds Such as benzoyl-L-leucylglycine, and since, in addition to the dipeptide, it hydrolyzes L-leucinamide (LA) and the tripeptides, L-leucylglycylglycine (LGG) and L-leucyl-L-leucylglycine. It has now been observed that a highly purified preparation of leucine aminopeptidase from hog intestinal mucosa can hydrolyze glycyl-Lleucinamide (GLA). Under the conditions of our experiments, the reaction ceases after the decomposition of a single peptide bond. Since glycyl-r,leucine is not appreciably hydrolyzed, the hydrolysis must occur at the terminal amide bond, as indicated by the dotted line; R represents the