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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Autor principal: Sanchez, C.P
Otros Autores: Gonzalez, N.S, Algranati, I.D
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1989
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0024373507 
024 7 |2 cas  |a ornithine decarboxylase, 9024-60-6; arginine decarboxylase, EC 4.1.1.19; Carboxy-Lyases, EC 4.1.1.; Ornithine Decarboxylase, EC 4.1.1.17; Pyridoxal Phosphate, 54-47-7 
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030 |a BBRCA 
100 1 |a Sanchez, C.P. 
245 1 0 |a Stable ornithine decarboxylase in promastigotes of Leishmania mexicana 
260 |c 1989 
270 1 0 |m Sánchez, C.P.; Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires A. Machado 151, 1405 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Jänne, Pössö, Raina, (1978) Biochim. Biophys. Acta, 473, pp. 241-293 
504 |a Pegg, (1988) Cancer Res, 48, pp. 759-774 
504 |a Heby, (1981) Differentiation, 19, pp. 1-20 
504 |a Sunkara, Baylin, Luck, (1987) Inhibition of Polyamine Metabolism. Biological Significance and Basis for New Therapies, pp. 121-140. , P.P. McCann, A.E. Pegg, A. Sjoerdsma, Academic Press, Orlando, FL 
504 |a Talpaz, Plager, Quesda, Benjamin, Kantarjian, Gutterman, (1986) Eur. J. Cancer Clin. Oncol, 22, pp. 685-689 
504 |a Bacchi, Nathan, Hutner, McCann, (1980) Science, 210, pp. 332-334 
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504 |a Bacchi, McCann, (1987) Inhibition of Polyamine Metabolism. Biological Significance and Basis for New Therapies, pp. 317-344. , P.P. McCann, A.E. Pegg, A. Sjoerdsma, Academic Press, Orlando, FL 
504 |a Phillips, Coffino, Wang, (1987) J. Biol. Chem, 262, pp. 8721-8727 
504 |a Warren, (1960) J. Parasitol, 46, pp. 529-538 
504 |a Cataldi, Algranati, Polyamines and regulation of ornithine biosynthesis in Escherichia coli. (1989) J Bacteriol, , in press 
504 |a Camargo, Coelho, Moraes, Figuereido, Trypanosoma spp., Leishmania spp. and Leptomonas spp.: Enzymes of ornithine-arginine metabolism (1978) Experimental Parasitology, 46, pp. 141-144 
504 |a Smith, Marshall, (1988) Phytochemistry, 27, pp. 703-710 
504 |a Murphy, Brosnan, (1976) Biochem. J, 157, pp. 33-39 
504 |a Kim, Sobota, Bitonti, McCann, Byers, (1987) J. Protozool, 34, pp. 278-284 
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504 |a Kanamoto, Utsonomiya, Kameji, Hayashi, (1986) Eur. J. Biochem, 154, pp. 539-544 
504 |a Pegg, (1986) Biochem. J, 234, pp. 249-262 
504 |a Rogers, Wells, Rechsteiner, (1986) Science, 234, pp. 364-368 
520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: SAREC 
536 |a Detalles de la financiación: World Health Organization 
536 |a Detalles de la financiación: Secretaria de Ciencia y Tecnica, Universidad de Buenos Aires 
536 |a Detalles de la financiación: We are indebted to Dr. B. Franke de Cazzulo and L. Sferco for parasite cultures and Dr. S.H. Goldemberg for helpful discussions. This work was partially supported by grants from the Swedish Agency for Research Cooperation with Ueveloping Countries (SAREC), WHO Special Programme for Research and Training in Tropical Diseases, Secretaria de Ciencia y Tecnica and the Consejo National Investigaciones Cientificas y Tecnicas (Argentina). C.P. Sa/ncher is a fellow N.S. Gonzalez and I.D. Algranati are career investigators of the latter institution. 
593 |a Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires A. Machado 151, 1405 Buenos Aires, Argentina 
593 |a CONICET, A. Machado 151, 1405 Buenos Aires, Argentina 
690 1 0 |a ORNITHINE DECARBOXYLASE 
690 1 0 |a LEISHMANIA MEXICANA 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN STABILITY 
690 1 0 |a PROTOZOON 
690 1 0 |a ANIMAL 
690 1 0 |a CARBOXY-LYASES 
690 1 0 |a CELL-FREE SYSTEM 
690 1 0 |a KINETICS 
690 1 0 |a LEISHMANIA MEXICANA 
690 1 0 |a ORNITHINE DECARBOXYLASE 
690 1 0 |a PROTEIN DENATURATION 
690 1 0 |a PYRIDOXAL PHOSPHATE 
690 1 0 |a SUBSTRATE SPECIFICITY 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
700 1 |a Gonzalez, N.S. 
700 1 |a Algranati, I.D. 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_0006291X_v161_n2_p754_Sanchez  |y Handle 
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