Endogenous Inactivators of Arginase, l-Arginine Decarboxylase, and Agmatine Amidinohydrolase in Evernia prunastri Thallus

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Abstract
Arginase (EC 3.4.3.1), L-arginine decarboxylase (EC 4.1.1.19) and agmatine amidinohydrolase (EC 3.5.3.11) activities spontaneously decay in E. prunastri thalli incubated on 40 mM L-arginine used as inducer of the 3 enzymes if dithiothreitol is not added to the media. Lichen thalli accumulate chloroatranorin and evernic acid in parallel to the loss of activity. These substances behave as inactivators of the enzymes at a range of concentrations between 2 and 20 .mu.M, whereas several concentrations of dithiothreitol reverse, to some extent, the in vitro inactivation.