Open AccessInhibition of Ornithine Decarboxylase and Growth of the Fungus Helminthosporium maydis
Author(s) -
H. Birecka,
Michael O. Garraway,
Russell J. Baumann,
Peter P. McCann
Publication year - 1986
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.80.3.798
Subject(s) - fungus , ornithine decarboxylase , microbiology and biotechnology , biology , filamentous fungus , botany , biochemistry , enzyme
alpha-dl-Difluoromethylornithine (DFMO), a specific enzyme-activated inhibitor of ornithine decarboxylase, at 0.5 to 2.0 millimolar significantly inhibited mycelial growth and especially sporulation of Helminthosporium maydis in the dark; its inhibitory effect on sporulation was greatly increased under light conditions. Putrescine at 0.25 millimolar fully prevented the inhibitory effects of DFMO; the inhibition caused by the latter could not be prevented by cadaverine or CaCl(2). alpha-dl-Difluoromethylarginine, a specific enzyme-activated inhibitor of arginine decarboxylase, at 0.1 to 2.0 millimolar had a weak inhibitory effect on the fungus. The effect was not dependent on the inhibitor concentration and there was no detectable arginine decarboxylase activity in the fungus.