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B6db references: 87222422

type Journal Article
authors DiGangi, J. J.; Seyfzadeh, M.; Davis, R. H.
title Ornithine decarboxylase from Neurospora crassa. Purification, characterization, and regulation by inactivation
journal J Biol Chem
ui 87222422
year (1987)
volume 262
number 16
pages 7889-93.
keywords Eflornithine/metabolism/pharmacology
abstract Ornithine decarboxylase, a highly regulated enzyme of the polyamine pathway, was purified 670-fold from mycelia of Neurospora crassa that were highly augmented for enzyme activity. The enzyme is significantly different from those reported from three other lower eucaryotic organisms: Saccharomyces cerevisiae, Physarum polycephalum, and Tetrahymena pyriformis. Instead, the enzyme closely resembles the enzymes from mammals. The Mr = 110,000 enzyme is a dimer of 53,000 Da subunits, with a specific activity of 2,610 mumol per h per mg of protein. Antisera were raised to the purified enzyme and were rendered highly specific by cross-absorption with extracts of a mutant strain lacking ornithine decarboxylase protein. With the antisera, we show that the inactivation of the enzyme in response to polyamines is proportional to the loss of ornithine decarboxylase protein over almost 2 orders of magnitude. This is similar to the inactivation process in certain mammalian tissues, and different from the process in S. cerevisiae and P. polycephalum, in which enzyme modification, without proportional loss of antigen, accompanies enzyme inactivation. The N. crassa enzyme is therefore suitable as a microbial model for studies of the molecular regulation of the mammalian enzyme.
last changed 2002/11/12 16:17

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