Activities of Arginine and Ornithine Decarboxylases in Various Plant Species

Birecka, H.; Bitonti, Alan J.; McCann, Peter P.

doi:10.1104/pp.79.2.515

Cited by 43 publications

(17 citation statements)

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“…a-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.Our recent investigation on in vitro activities of ADC2 and ODC from higher plants (4,5) under the same conditions sporulation is three to four times as high as that found in cultures exposed to light (M. 0. Garraway, unpublished data).…”

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Inhibition of Ornithine Decarboxylase and Growth of the Fungus Helminthosporium maydis

Birecka¹,

Garraway²,

Baumann³

et al. 1986

Plant Physiol.

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a-DL-DifluoromethylomUithine (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 CaC12. a-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.Our recent investigation on in vitro activities of ADC2 and ODC from higher plants (4,5) under the same conditions sporulation is three to four times as high as that found in cultures exposed to light (M. 0. Garraway, unpublished data). MATERIALS AND METHODSThe fungus was grown on a synthetic medium containing asparagine described previously (6). The sterilized agar culture media (20 ml per 100 x 20 mm sterile Petri dish) contained glucose, L-asparagine, KH2PO4, and MgSO4 at 0.5, 0.2, 0.3, and 0.15%. Sterilized solutions of Mn, Zn, Fe, and Cu salts at 1 ug/ 1 each were added at 0.2 ml per dish. Solutions of other compounds were filter sterilized prior to application. The pH of the culture media in experiment I was 5.0; in the remaining experiments it was adjusted to 6.0, which proved to be optimal for the fungal growth. Each Petri dish was inoculated at its center with a plug of mycelium 7 mm in diameter. Each experiment was carried out in four replicates. In experiments I and III the Petri dishes were placed in the dark at room temperature. In experiment II, 2 d after inoculation, the plates were transferred from darkness to diffused fluorescent light. Growth was determined by linear extension, and sporulation was expressed on dry weight basis (6).In experiment III the activities of ODC and ADC were determined after the enzymes were extracted with phosphate buffer (pH 7.6) (14) from mycelia exposed to the highest DFMO and DFMA concentrations. Repeated freezing and thawing, sonication, and maceration with glass beads was applied during extraction at 0 to 4°C. The enzymes were assayed as described previously (3,4)

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“…Our recent investigation on in vitro activities of ADC2 and ODC from higher plants (4,5) under the same conditions sporulation is three to four times as high as that found in cultures exposed to light (M. 0. Garraway, unpublished data).…”

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confidence: 99%

Inhibition of Ornithine Decarboxylase and Growth of the Fungus Helminthosporium maydis

Birecka¹,

Garraway²,

Baumann³

et al. 1986

Plant Physiol.

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“…The negative results of the ADC assays prompted us to reexamine oat cv Garry that previously exhibited very high ADC activities, 334 and 1096 nmol/h x mg protein, in the first leaf of seedlings grown in the greenhouse and on a windowsill, respectively; the Put-based ODC activity was about 0.2 to 0.3 nmol/h x mg protein in both cases (6,7). It was worrisome that the activities of the two enzymes reported for comparable leaves of oat cv Victory seedlings, grown under controlled conditions, were much different from ours and at the same time showed significant variability.…”

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“…In L. albus no synthesis of quinolizidines from labeled endogenous precursors was found in young pods; synthesis in green stems was minimal; at flowering, the side shoot leaves were the main contributors to alkaloid accumulation (3,4). In young H. spathulatum the leaves were the main if not the exclusive organ responsible for necine biosynthesis (8) and there is much evidence for PA translocation to stems, roots, inflorescence, seeds, and even to very young immature leaves at least in some Heliotropium species (7,8,14). Similar patterns of translocation may also occur in S. riddellii and C. retusa if the location of the key enzymes involved in necine biosynthesis from Put coincides with the site of ODC activity.…”

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Ornithine Decarboxylase, Polyamines, and Pyrrolizidine Alkaloids in Senecio and Crotalaria

Birecka¹,

Birecki²,

Cohen³

et al. 1988

Plant Physiol.

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When tested for ornithine and arginine decarboxylases, pyrrolizidine alkaloid-bearing Senecio riddellii, S. longilobus (Compositae), and Crotalaria retusa (Leguminosae) plants exhibited only ornithine decarboxylase activity. This contrasts with previous studies of four species of pyrrolizidine alkaloid-bearing Heliotropium (Boraginaceae) in which arginine decarboxylase activity was very high relative to that of ornithine decarboxylase. Unlike Heliotropium angiospermum and Heliotropium indicum, in which endogenous arginine was the only detectable precursor of putrescine channeled into pyrrolizidines, in the species studied here using difluoromethylornithine and difluoromethylarginine as the enzyme inhibitors-endogenous ornithine was the main if not the only precursor of putrescine converted into the alkaloid aminoalcohol moiety. In S.riddeliji and C. retusa at flowering, ornithine decarboxylase activity was present mainly in leaves, especially the young ones. However, other very young organs such as inflorescence and growing roots exhibited much lower or very low activities; the enzyme activity in stems was negligible. There was no correlation between the enzyme activity and polyamine or alkaloid content in either species. In both species only free polyamines were detected except for C. retusa roots and inflorescence-with relatively very high levels of these compounds-in which conjugated putrescine, spermidine, and spermine were also found; agmatine was not identified by HPLC in any plant organ except for C. retusa roots with rhizobial nodules. Organ-or age-dependent differences in the polyamine levels were small or insignificant. The highest alkaloid contents were found in young leaves and inflorescence.Our previous study on PA '- the same borages were able to decarboxylate exogenous Orn to Put that in turn was converted into necines. Thus, in vivo transformation of an exogenous putative precursor does not always indicate the compound formed in situ that normally serves as a precursor. This is especially true in the case of Put, which can derive not only from Orn but also from Arg via Agm, the product of Arg decarboxylation by ADC. Our attempt to identify the in situ precursor(s) of the Put channeled into pyrrolizidines in Senecio vulgaris were unsuccessful due to the extremely low PA content of the shoots.We report here the effects of DFMO and DFMA on necine biosynthesis in S. riddellii, S. longilobus (Compositae), and Crotalaria retusa (Leguminosae) plants. These species occasionally produce extremely high levels of PAs, up to 9 to 17% of leaf dry weight (23). In previously analyzed samples of S. riddellii and S. longilobus plants from New Mexico the PA contents were about 1.5 and 2.8%, respectively (10). Since there is little information about polyamines, including Put, ADC, and ODC activities, or the site(s) of alkaloid biosynthesis in PA-bearing plants, and since such information is available only for Heliotropium (5, 7-9), a more detailed examination of PA-bearing plants seemed important. Flowering...

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Secondary Plant Substances: Ornithine-Derived Alkaloids

Schütte

1994

Progress in Botany

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Activities of Arginine and Ornithine Decarboxylases in Various Plant Species

Cited by 43 publications

References 5 publications

Inhibition of Ornithine Decarboxylase and Growth of the Fungus Helminthosporium maydis

Inhibition of Ornithine Decarboxylase and Growth of the Fungus Helminthosporium maydis

Ornithine Decarboxylase, Polyamines, and Pyrrolizidine Alkaloids in Senecio and Crotalaria

Secondary Plant Substances: Ornithine-Derived Alkaloids

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