gamma-Glutamylamine cyclotransferase. An enzyme involved in the catabolism of epsilon-(gamma-glutamyl)lysine and other gamma-glutamylamines

Abstract

gamma-Glutamylamine cyclotransferase, an enzyme found in a number of animal tissues and cells, catalyzes the conversion of epsilon-(L-gamma-glutamyl)-L-lysine to free lysine and 5-oxo-L-proline as well as the release of free amines and the formation of 5-oxo-L-proline from a variety of other L-gamma-glutamylamines. Among its substrates are both the mon- and di-gamma-glutamyl derivatives of putrescine, spermidine and spermine, and a derivative of epsilon-(L-gamma-glutamyl)-L-lysine in which both the alpha-amino group and the carboxyl group of the lysine moiety are blocked. The enzyme does not act on most gamma-glutamyl-alpha-amino acids, nor is it active toward the epsilon-lysyl derivatives of L-aspartic acid or D-glutamic acid. Derivatives of epsilon-(L-gamma-glutamyl)-L-lysine in which the alpha-amino or the alpha-carboxyl function of the glutamyl moiety is blocked also do not serve as substrates. The specificity of gamma-glutamylamine cyclotransferase is in accordance with the proposal that it functions biologically in the latter stages of the catabolism of products of the action of transglutaminases. Some suggestions as to the manner in which gamma-glutamylamine cyclotransferase serves this function are made based on present knowledge of protein degradation.