Difluoromethylornithine irreversibly inactivates ornithine decarboxylase of <i>Pseudomonas aeruginosa</i>, but does not inhibit the enzymes of <i>Escherichia coli</i>

Kallio, Arja; McCann, PP

doi:10.1042/bj2000069

Cited by 53 publications

(27 citation statements)

References 28 publications

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“…In two separate cultures the uninduced Datura ODC activity was also approximately 5-fold higher than in the control cells. Further evidence that the increased ODC activity was from the Datura cDNA was provided by the sensitivity of the Datura ODC activity to the presence of 1.0 mM DFMO, whereas the background activity represented by the endogenous E. coli ODC was resistant to DFMO as previously described [37].…”

Section: Expression Of Datura Odc In E Colimentioning

confidence: 69%

“…The black circle marks the Lys shown to be the main PLP-binding site and the black square marks the Cys shown to be the DFMO binding site in the mouse ODC [12]. The black triangle marks the cleavage site for the processing of the oat ADC [37] and the underlined sequence is the motif resembling a sequence conserved in methyltransferases and spermidine synthases. Only the DapDC with the greatest similarity to the Datura ODC is presented.…”

Section: Tabacimentioning

confidence: 99%

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Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA

Michael

Furze

Rhodes

et al. 1996

Biochemical Journal

123

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A cDNA for a plant ornithine decarboxylase (ODC), a key enzyme in putrescine and polyamine biosynthesis, has been isolated from root cultures of the solanaceous plant Datura stramonium. Reverse transcription–PCR employing degenerate oligonucleotide primers representing conserved motifs from other eukaryotic ODCs was used to isolate the cDNA. The longest open reading frame potentially encodes a peptide of 431 amino acids and exhibits similarity to other eukaryotic ODCs, prokaryotic and eukaryotic arginine decarboxylases (ADCs), prokaryotic meso-diaminopimelate decarboxylases and the product of the tabA gene of Pseudomonas syringae cv. tabaci. Residues involved at the active site of the mouse ODC are conserved in the plant enzyme. The plant ODC does not possess the C-terminal extension found in the mammalian enzyme, implicated in rapid turnover of the protein, suggesting that the plant ODC may have a longer half-life. Expression of the plant ODC in Escherichia coli and demonstration of ODC activity confirmed that the cDNA encodes an active ODC enzyme. This is the first description of the primary structure of a eukaryotic ODC isolated from an organism where the alternative ADC route to putrescine is present.

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Section: Expression Of Datura Odc In E Colimentioning

confidence: 69%

Section: Tabacimentioning

confidence: 99%

Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA

Michael

Furze

Rhodes

et al. 1996

Biochemical Journal

123

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“…Addition of DL-a-difluoromethyl arginine, a compound known to be an irreversible specific inhibitor of ADC (17), caused a 65% inhibition at 50 ,M, and at 0.5 mm the compound almost completely abolished the decarboxylation. However, addition of 1 mM DL-a-difluoromethyl ornithine, which is known to be a specific inhibitor of ODC activity (16), had no effect. This implies that the decarboxylation observed in this reaction is solely due to the ADC activity.…”

Section: Resultsmentioning

confidence: 92%

Control by Ethylene of Arginine Decarboxylase Activity in Pea Seedlings and Its Implication for Hormonal Regulation of Plant Growth

Apelbaum¹,

Goldlust²,

Icekson³

1985

Plant Physiol.

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Activity of arginine decarboxylase in etiolated pea seedlings appears 24 hours after seed imbibition, reaches its highest level on the 4th day, and levels off until the 7th day. This activity was found in the apical and subapical tissue of the roots and shoots where intensive DNA synthesis occurs. Exposure of the seedlings to ethylene greatly reduced the specific activity of this enzyme. The inhibition was observed within 30 min of the hormone application, and maximal effect-90% inhibition-after 18 hours. Ethylene at physiological concentrations affected the enzyme activity; 50% inhibitory rate was recorded at 0.12 microliters per liter ethylene and maximal response at 1.2 microliters per liter. Ethylene provoked a 5-fold increase in the K,," of arginine decarboxylase for its substrate and reduced the V.w by 10-fold. However, the enzyme recovered from the inhibition and regained control activity 7 hours after transferral of the seedlings to ethylene-free atmosphere. Reducing the endogenous level of ethylene in the tissue by hypobaric pressure, or by exposure to light, as well as interfering with ethylene action by treatment with silver thiosulfate or 2,5-norbornadiene, caused a gradual increase in the specific activity of arginine decarboxylase in the apical tissue of the etiolated seedlings. On the basis of these findings, the possible control of arginine decarboxylase activity by endogenous ethylene, and its implication for the hormone effect on plant growth, are discussed.arises from the study of Bagni (5), who first reported that growth ofdormant Helianthus tuberosus was initiated when either auxin or one of the polyamines was added to the medium and that growth was accompanied by an increase in polyamine titer. There are now recorded instances of increased polyamine biosynthesis and titer in plants following application of each of the growthpromoting plant hormones: auxin (6), GA3 (13), and cytokinin (28). On the other hand, retardation ofgrowth by ABA has been shown to be accompanied by decreased polyamine biosynthesis (28). Consequently, the role of 'second messenger' mediating the effect of plant hormones has been proposed for polyamines (14).Ethylene has been shown to inhibit cell division, DNA synthesis, and growth in meristems of roots, shoots, and axillary buds of etiolated pea seedlings (1). In the shoot apex, cell division was almost completely annulled by ethylene and only 60% inhibition was observed in the root apex (1). The gas inhibits cell division by blocking a stage before prophase (1). In the subapical regions of the seedling, the hormone inhibited cell expansion and DNA synthesis (2). In the various parts of the seedling, a qualitative relationship was found between the inhibition of DNA synthesis, cell division, and growth caused by ethylene (1).In view of the above, a study was undertaken to pursue a possible involvement of polyamines in the effects of ethylene on plant growth. In this communication, we show that ethylene provokes a pronounced and reversible inhibition of ADC2 ac...

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“…First, added [U-'4C]ornithine is readily converted into Put without lag period (Fig. 5) (19,25) and arginine decarboxylase (20), respectively, for determination of whether Put could be formed from decarboxylation of arginine in the aleurone layers have been unsuccessful (Fig. 6).…”

Section: Methodsmentioning

confidence: 99%

“…The lack of effects of the inhibitors on Put formation could be due to poor uptake of the chemicals or lack of sensitivity of the decarboxylases of barley aleurone layers to the chemicals. It has been reported that not all of the ornithine decarboxylases isolated from bacteria (19) and plant tissues (15) are DFMO sensitive.…”

Section: Methodsmentioning

confidence: 99%

Polyamine Metabolism and Its Relation to Response of the Aleurone Layers of Barley Seeds to Gibberellic Acid

Lin¹

1984

Plant Physiol.

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ABSTRACrPolyamine metabolism and its relation to the induction of a-amylase formation in the aleurone layers of barley seeds (Hordeum vulgare cv Himalaya) in response to gibberellic acid (GA3) has been investipted. A high-performance liquid chromatographic system has been employed for qualitative and quantitative analyses of putrescine (Put), cadaverine (Cad), spermidine (Spd), spermine (Spm), and agmatine (Agm).Active polyamine metabolism occurs in the aleurone cells of deembryonate barley half seeds during imbibition. The aleurone layers isolated from fully imbibed half seeds contain about 880 nanomoles of Put, 920 nanomoles of Spd, and 610 nanomoles of Spm as free form per gram tissue dry weight while the levels of Cad and Agm are relatively low. The polyamine levels do not change significantly in the aleurone layers in response to added GA3 (1.5 micromolar) during the 8-hour lag period of the growth substance-induced formation of a-amylase. Also, the polyamine levels are not altered by the presence of abscisic acid (3 micromolar) which inhibits the enzyme induction by GA3. Kinetic studies show that both applied IU-"Cqornithine and lU-'4Carginine are primarily incorporated into Put during 2 hours of incubation, but the incorporation is not significantly affected by added GA3. Additionally, added GA3 does not affect the uptake and turnover of 11, nor research (18,37,38). Experiments with the aleurone layers of barley seeds have shown a number of biochemical events related to the synthesis of a-amylase in response to added GA3. The mass synthesis of a-amylase begins 8 to 10 h after exposure of the tissue to the growth substance (9). Syntheses and accumulation of a-amylase mRNA (17) and ER (38) start as early as 2 to 4 h after treatment of the growth substance. For efficient expression of a-amylase gene(s), it has recently been suggested that a newly synthesized protein is required (26). If GA3 has effects on translation, the synthesis ofthe unidentified protein factor could occur shortly after addition of the growth substance. Thus, it would be interesting to investigate possible biochemical changes within 2 h after exposure of the aleurone layers to GA3, and to determine whether any changes are related to the effects of the growth substance on the transcriptional and/or translational events described.The diamine Put2 and polyamines Spd and Spm are ubiquitous in biological materials (1, 33,35 (1,12,32,36). Several lines of evidence indicate that polyamines may be involved in regulation of structure, function, and/or biosynthesis ofmacromolecules (10,16,24,28). In higher plants, polyamine metabolism has been related to the action of plant growth substances on regulation of plant growth and development (7, 8, 13, 22). In the internodes of light-grown dwarf peas the contents of Put and Spd per internode have been shown to increase during the elongation induced by exogenously applied GA3 (13). Also, it has been reported that the addition of GA3 results in 4-fold increase in the activity ofornithine decarboxyla...

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Difluoromethylornithine irreversibly inactivates ornithine decarboxylase of Pseudomonas aeruginosa, but does not inhibit the enzymes of Escherichia coli

Cited by 53 publications

References 28 publications

Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA

Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA

Control by Ethylene of Arginine Decarboxylase Activity in Pea Seedlings and Its Implication for Hormonal Regulation of Plant Growth

Polyamine Metabolism and Its Relation to Response of the Aleurone Layers of Barley Seeds to Gibberellic Acid

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