Studies of enzyme-catalyzed modification of proteins. I. Tyrosinase-catalyzed modification of asparaginase.

Abstract

Asparaginase [EC 3.5.1.1.] of Escherichia coli, an anti-tumor enzyme, was inactivated in a time-dependent fashion by mushroom tyrosinase [EC1.14.18.1.]. The inactivation did not proceed, however, when heat-inactivated tyrosinase was used. Exculusion of the atmospheric oxygen or addition of diethyldithiocarbamate, a copper selective chelating agent, prevented the inactivation. The difference absorption spectrum of tyrosinase-inactivated asparaginase versus intact asparaginase exhibited the appearance of marked absorption peaks at 300 and 350 nm. These results indicate that the tyrosyl residue(s) of asparaginase, which is essential for the activity is enzymatically modified by tyrosianes.