Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase

The metabolism of polyamines as well as their functions as growth regulators in plants have been extensively studied for many years. However, almost nothing is known about the biosynthesis and roles of these substances in Phytomonas spp., parasites of several plants. We have used HPLC and electropho...

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Autores principales:	Marcora, María Silvina, González, Nélida Susana, Carrillo, Carolina, Algranati, Israel David
Publicado:	2010
Materias:	Metabolic turnover MG-132 Ornithine decarboxylase Phytomonas Jma Proteasome agmatine arginine benzyloxycarbonylleucylleucylleucinal eflornithine ornithine ornithine decarboxylase polyamine proteasome putrescine pyridoxal 5 phosphate spermidine spermidine synthase spermine biochemistry biodegradation electrokinesis enzyme activity experimental study growth regulator inhibition metabolism parasite plant article controlled study electrophoresis enzyme analysis enzyme degradation enzyme stability half life time high performance liquid chromatography nonhuman Phytomonas Phytomonas jma polyamine synthesis signal transduction Enzyme Stability Ornithine Decarboxylase Polyamines Protozoan Proteins Putrescine Spermidine Spermine Trypanosomatina
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207519_v40_n12_p1389_Marcora http://hdl.handle.net/20.500.12110/paper_00207519_v40_n12_p1389_Marcora
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00207519_v40_n12_p1389_Marcora
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spelling	paper:paper_00207519_v40_n12_p1389_Marcora2023-06-08T14:41:27Z Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase Marcora, María Silvina González, Nélida Susana Carrillo, Carolina Algranati, Israel David Metabolic turnover MG-132 Ornithine decarboxylase Phytomonas Jma Proteasome agmatine arginine benzyloxycarbonylleucylleucylleucinal eflornithine ornithine ornithine decarboxylase polyamine proteasome putrescine pyridoxal 5 phosphate spermidine spermidine synthase spermine biochemistry biodegradation electrokinesis enzyme activity experimental study growth regulator inhibition metabolism parasite plant article controlled study electrophoresis enzyme activity enzyme analysis enzyme degradation enzyme stability half life time high performance liquid chromatography nonhuman Phytomonas Phytomonas jma polyamine synthesis signal transduction Enzyme Stability Ornithine Decarboxylase Polyamines Protozoan Proteins Putrescine Spermidine Spermine Trypanosomatina Phytomonas The metabolism of polyamines as well as their functions as growth regulators in plants have been extensively studied for many years. However, almost nothing is known about the biosynthesis and roles of these substances in Phytomonas spp., parasites of several plants. We have used HPLC and electrophoretic analyses to investigate the presence and metabolism of polyamines in Phytomonas Jma strain, detecting both putrescine and spermidine but not spermine. Experiments carried out by incubation of intact parasites with labelled ornithine or putrescine showed the formation of radioactive putrescine or spermidine, respectively. These results indicated that Phytomonas Jma can synthesise these polyamines through the action of ornithine decarboxylase (ODC) and spermidine synthase. On the other hand, we could not detect the conversion of arginine to agmatine, suggesting the absence of arginine decarboxylase (ADC) in Phytomonas. However, we cannot ensure the complete absence of this enzymatic activity in the parasite. Phytomonas ODC required pyridoxal 5'-phosphate for maximum activity and was specifically inhibited by α-difluoromethylornithine. The metabolic turnover of the enzyme was very high, with a half-life of 10-15 min, one of the shortest found among all ODC enzymes studied to date. The parasite proteasome seems to be involved in degradation of the enzyme, since Phytomonas ODC can be markedly stabilized by MG-132, a well known proteasome inhibitor. The addition of polyamines to Phytomonas cultures did not decrease ODC activity, strongly suggesting the possible absence of antizyme in this parasite. © 2010 Australian Society for Parasitology Inc. Fil:Marcora, M.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Carrillo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207519_v40_n12_p1389_Marcora http://hdl.handle.net/20.500.12110/paper_00207519_v40_n12_p1389_Marcora
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Metabolic turnover MG-132 Ornithine decarboxylase Phytomonas Jma Proteasome agmatine arginine benzyloxycarbonylleucylleucylleucinal eflornithine ornithine ornithine decarboxylase polyamine proteasome putrescine pyridoxal 5 phosphate spermidine spermidine synthase spermine biochemistry biodegradation electrokinesis enzyme activity experimental study growth regulator inhibition metabolism parasite plant article controlled study electrophoresis enzyme activity enzyme analysis enzyme degradation enzyme stability half life time high performance liquid chromatography nonhuman Phytomonas Phytomonas jma polyamine synthesis signal transduction Enzyme Stability Ornithine Decarboxylase Polyamines Protozoan Proteins Putrescine Spermidine Spermine Trypanosomatina Phytomonas
spellingShingle	Metabolic turnover MG-132 Ornithine decarboxylase Phytomonas Jma Proteasome agmatine arginine benzyloxycarbonylleucylleucylleucinal eflornithine ornithine ornithine decarboxylase polyamine proteasome putrescine pyridoxal 5 phosphate spermidine spermidine synthase spermine biochemistry biodegradation electrokinesis enzyme activity experimental study growth regulator inhibition metabolism parasite plant article controlled study electrophoresis enzyme activity enzyme analysis enzyme degradation enzyme stability half life time high performance liquid chromatography nonhuman Phytomonas Phytomonas jma polyamine synthesis signal transduction Enzyme Stability Ornithine Decarboxylase Polyamines Protozoan Proteins Putrescine Spermidine Spermine Trypanosomatina Phytomonas Marcora, María Silvina González, Nélida Susana Carrillo, Carolina Algranati, Israel David Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase
topic_facet	Metabolic turnover MG-132 Ornithine decarboxylase Phytomonas Jma Proteasome agmatine arginine benzyloxycarbonylleucylleucylleucinal eflornithine ornithine ornithine decarboxylase polyamine proteasome putrescine pyridoxal 5 phosphate spermidine spermidine synthase spermine biochemistry biodegradation electrokinesis enzyme activity experimental study growth regulator inhibition metabolism parasite plant article controlled study electrophoresis enzyme activity enzyme analysis enzyme degradation enzyme stability half life time high performance liquid chromatography nonhuman Phytomonas Phytomonas jma polyamine synthesis signal transduction Enzyme Stability Ornithine Decarboxylase Polyamines Protozoan Proteins Putrescine Spermidine Spermine Trypanosomatina Phytomonas
description	The metabolism of polyamines as well as their functions as growth regulators in plants have been extensively studied for many years. However, almost nothing is known about the biosynthesis and roles of these substances in Phytomonas spp., parasites of several plants. We have used HPLC and electrophoretic analyses to investigate the presence and metabolism of polyamines in Phytomonas Jma strain, detecting both putrescine and spermidine but not spermine. Experiments carried out by incubation of intact parasites with labelled ornithine or putrescine showed the formation of radioactive putrescine or spermidine, respectively. These results indicated that Phytomonas Jma can synthesise these polyamines through the action of ornithine decarboxylase (ODC) and spermidine synthase. On the other hand, we could not detect the conversion of arginine to agmatine, suggesting the absence of arginine decarboxylase (ADC) in Phytomonas. However, we cannot ensure the complete absence of this enzymatic activity in the parasite. Phytomonas ODC required pyridoxal 5'-phosphate for maximum activity and was specifically inhibited by α-difluoromethylornithine. The metabolic turnover of the enzyme was very high, with a half-life of 10-15 min, one of the shortest found among all ODC enzymes studied to date. The parasite proteasome seems to be involved in degradation of the enzyme, since Phytomonas ODC can be markedly stabilized by MG-132, a well known proteasome inhibitor. The addition of polyamines to Phytomonas cultures did not decrease ODC activity, strongly suggesting the possible absence of antizyme in this parasite. © 2010 Australian Society for Parasitology Inc.
author	Marcora, María Silvina González, Nélida Susana Carrillo, Carolina Algranati, Israel David
author_facet	Marcora, María Silvina González, Nélida Susana Carrillo, Carolina Algranati, Israel David
author_sort	Marcora, María Silvina
title	Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase
title_short	Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase
title_full	Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase
title_fullStr	Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase
title_full_unstemmed	Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase
title_sort	polyamine biosynthesis in phytomonas: biochemical characterisation of a very unstable ornithine decarboxylase
publishDate	2010
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207519_v40_n12_p1389_Marcora http://hdl.handle.net/20.500.12110/paper_00207519_v40_n12_p1389_Marcora
work_keys_str_mv	AT marcoramariasilvina polyaminebiosynthesisinphytomonasbiochemicalcharacterisationofaveryunstableornithinedecarboxylase AT gonzaleznelidasusana polyaminebiosynthesisinphytomonasbiochemicalcharacterisationofaveryunstableornithinedecarboxylase AT carrillocarolina polyaminebiosynthesisinphytomonasbiochemicalcharacterisationofaveryunstableornithinedecarboxylase AT algranatiisraeldavid polyaminebiosynthesisinphytomonasbiochemicalcharacterisationofaveryunstableornithinedecarboxylase
_version_	1768546476435177472

Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase

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