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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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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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 |
work_keys_str_mv |
AT sanchezceciliapalmira stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana AT gonzaleznelidasusana stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana AT algranatiisraeldavid stableornithinedecarboxylaseinpromastigotesofleishmaniamexicana |
_version_ |
1768544436931788800 |