This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Web of Science (56) Citing Articles via Google Scholar Google Scholar Articles by Legaz, M. E. Articles by Vicente, C. Search for Related Content PubMed PubMed Citation Articles by Legaz, M. E. Articles by Vicente, C. Agricola Articles by Legaz, M. E. Articles by Vicente, C.

Articles

Endogenous Inactivators of Arginase, L-Arginine Decarboxylase, and Agmatine Amidinohydrolase in Evernia prunastri Thallus ¹

Department of Plant Physiology, The Lichen Team, Faculty of Biology, Complutense University, Madrid 3, Spain

Arginase (EC 3.5.3.1), L-arginine decarboxylase (EC 4.1.1.19), and agmatine amidinohydrolase (EC 3.5.3.11) activities spontaneously decay in Evernia prunastri thalli incubated on 40 millimolar L-arginine used as inducer of the three enzymes if dithiothreitol is not added to the media. Lichen thalli accumulate both 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 micromolar, whereas several concentrations of dithiothreitol reverse, to some extent, the in vitro inactivation.