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, C.P., Gonzalez, N.S., Algranati, I.D.
Formato: JOUR
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v161_n2_p754_Sanchez
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_0006291X_v161_n2_p754_Sanchez
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spelling todo:paper_0006291X_v161_n2_p754_Sanchez2023-10-03T14:03:41Z Stable ornithine decarboxylase in promastigotes of Leishmania mexicana Sanchez, C.P. Gonzalez, N.S. Algranati, I.D. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, C.P.
Gonzalez, N.S.
Algranati, I.D.
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.
format JOUR
author Sanchez, C.P.
Gonzalez, N.S.
Algranati, I.D.
author_facet Sanchez, C.P.
Gonzalez, N.S.
Algranati, I.D.
author_sort Sanchez, C.P.
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
url http://hdl.handle.net/20.500.12110/paper_0006291X_v161_n2_p754_Sanchez
work_keys_str_mv AT sanchezcp stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana
AT gonzalezns stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana
AT algranatiid stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana
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