Stable ornithine decarboxylase in promastigotes of Leishmania mexicana

Studies on the decarboxylation of ornithine in Leishmania mexicana have shown that this activity corresponds to a true ornithine decarboxylase rather than to an oxidative decarboxylation or aminotransferase reaction, both of which also give rise to the release of CO2. The stoichiometric relationship...

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Autores principales: Sanchez, Cecilia Palmira, González, Nélida Susana, Algranati, Israel David
Publicado: 1989
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v161_n2_p754_Sanchez
http://hdl.handle.net/20.500.12110/paper_0006291X_v161_n2_p754_Sanchez
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spelling paper:paper_0006291X_v161_n2_p754_Sanchez2023-06-08T14:30:06Z Stable ornithine decarboxylase in promastigotes of Leishmania mexicana Sanchez, Cecilia Palmira González, Nélida Susana Algranati, Israel David ornithine decarboxylase leishmania mexicana nonhuman priority journal protein stability protozoon Animal Carboxy-Lyases Cell-Free System Kinetics Leishmania mexicana Ornithine Decarboxylase Protein Denaturation Pyridoxal Phosphate Substrate Specificity Support, Non-U.S. Gov't Studies on the decarboxylation of ornithine in Leishmania mexicana have shown that this activity corresponds to a true ornithine decarboxylase rather than to an oxidative decarboxylation or aminotransferase reaction, both of which also give rise to the release of CO2. The stoichiometric relationship between substrate and products has indicated that extracts of L. mexicana were able to catalyse the formation of an unknown compound besides putrescine and CO2. The addition of cycloheximide to cultures of L. mexicana allowed us to demonstrate that ornithine decarboxylase degradation in vivo was extremely slow in this parasite. This remarkable stability of the enzyme is only comparable to that found in Trypanosoma brucei and contrasts with the high turnover rate of ornithine decarboxylases of different mammalian cells. © 1989. Fil:Sanchez, C.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gonzalez, N.S. 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. 1989 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v161_n2_p754_Sanchez http://hdl.handle.net/20.500.12110/paper_0006291X_v161_n2_p754_Sanchez
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic ornithine decarboxylase
leishmania mexicana
nonhuman
priority journal
protein stability
protozoon
Animal
Carboxy-Lyases
Cell-Free System
Kinetics
Leishmania mexicana
Ornithine Decarboxylase
Protein Denaturation
Pyridoxal Phosphate
Substrate Specificity
Support, Non-U.S. Gov't
spellingShingle ornithine decarboxylase
leishmania mexicana
nonhuman
priority journal
protein stability
protozoon
Animal
Carboxy-Lyases
Cell-Free System
Kinetics
Leishmania mexicana
Ornithine Decarboxylase
Protein Denaturation
Pyridoxal Phosphate
Substrate Specificity
Support, Non-U.S. Gov't
Sanchez, Cecilia Palmira
González, Nélida Susana
Algranati, Israel David
Stable ornithine decarboxylase in promastigotes of Leishmania mexicana
topic_facet ornithine decarboxylase
leishmania mexicana
nonhuman
priority journal
protein stability
protozoon
Animal
Carboxy-Lyases
Cell-Free System
Kinetics
Leishmania mexicana
Ornithine Decarboxylase
Protein Denaturation
Pyridoxal Phosphate
Substrate Specificity
Support, Non-U.S. Gov't
description Studies on the decarboxylation of ornithine in Leishmania mexicana have shown that this activity corresponds to a true ornithine decarboxylase rather than to an oxidative decarboxylation or aminotransferase reaction, both of which also give rise to the release of CO2. The stoichiometric relationship between substrate and products has indicated that extracts of L. mexicana were able to catalyse the formation of an unknown compound besides putrescine and CO2. The addition of cycloheximide to cultures of L. mexicana allowed us to demonstrate that ornithine decarboxylase degradation in vivo was extremely slow in this parasite. This remarkable stability of the enzyme is only comparable to that found in Trypanosoma brucei and contrasts with the high turnover rate of ornithine decarboxylases of different mammalian cells. © 1989.
author Sanchez, Cecilia Palmira
González, Nélida Susana
Algranati, Israel David
author_facet Sanchez, Cecilia Palmira
González, Nélida Susana
Algranati, Israel David
author_sort Sanchez, Cecilia Palmira
title Stable ornithine decarboxylase in promastigotes of Leishmania mexicana
title_short Stable ornithine decarboxylase in promastigotes of Leishmania mexicana
title_full Stable ornithine decarboxylase in promastigotes of Leishmania mexicana
title_fullStr Stable ornithine decarboxylase in promastigotes of Leishmania mexicana
title_full_unstemmed Stable ornithine decarboxylase in promastigotes of Leishmania mexicana
title_sort stable ornithine decarboxylase in promastigotes of leishmania mexicana
publishDate 1989
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v161_n2_p754_Sanchez
http://hdl.handle.net/20.500.12110/paper_0006291X_v161_n2_p754_Sanchez
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AT gonzaleznelidasusana stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana
AT algranatiisraeldavid stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana
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