Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi

1. 1. Heme compounds are necessary as a growth factor for Trypanosoma cruzi in culture, this porphyrin requirement being due to the inability of the parasite to synthesize heme. To obtain supporting evidence for this hypothesis, an extensive study of porphyrin biosynthesis in the epimastogote form o...

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Autores principales:	Salzman, Teresa Ana, Stella de Rosellini, Ana María Cristina, Wider de Xifra, Eva Adela, Batlle, Alcira María del Carmen, Stoppani, Andrés Oscar Manuel
Publicado:	1982
Materias:	5 aminolevulinate synthase aminolevulinate aminotransferase aminotransferase ammonia lyase Ammonia Lyases ferrochelatase heme porphobilinogen synthase porphyrin Succinate CoA Ligases succinyl coenzyme A synthetase animal article biosynthesis enzymology metabolism Trypanosoma cruzi 5-Aminolevulinate Synthetase Ammonia-Lyases Animal Ferrochelatase Heme Porphobilinogen Synthase Porphyrins Succinate-CoA Ligases Support, Non-U.S. Gov't Transaminases
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v72_n4_p663_Salzman http://hdl.handle.net/20.500.12110/paper_03050491_v72_n4_p663_Salzman
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	paper:paper_03050491_v72_n4_p663_Salzman2023-06-08T15:30:19Z Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi Salzman, Teresa Ana Stella de Rosellini, Ana María Cristina Wider de Xifra, Eva Adela Batlle, Alcira María del Carmen Stoppani, Andrés Oscar Manuel 5 aminolevulinate synthase aminolevulinate aminotransferase aminotransferase ammonia lyase Ammonia Lyases ferrochelatase heme porphobilinogen synthase porphyrin Succinate CoA Ligases succinyl coenzyme A synthetase animal article biosynthesis enzymology metabolism Trypanosoma cruzi 5-Aminolevulinate Synthetase Ammonia-Lyases Animal Ferrochelatase Heme Porphobilinogen Synthase Porphyrins Succinate-CoA Ligases Support, Non-U.S. Gov't Transaminases Trypanosoma cruzi 1. 1. Heme compounds are necessary as a growth factor for Trypanosoma cruzi in culture, this porphyrin requirement being due to the inability of the parasite to synthesize heme. To obtain supporting evidence for this hypothesis, an extensive study of porphyrin biosynthesis in the epimastogote form of T. cruzi (Tulahuén strain) was carried out. 2. 2. Low levels of endogenous δ-aminolevulinic acid (ALA) and porphobilinogen (PBG) were found in extracts of T. cruzi. Free porphyrins and heme contents were practically nil. 3. 3. The activity of succinyl CoA synthetase (Suc, CoA-S) was rather high and therefore non-limiting. 4. 4. Both δ-aminolevulinic acid synthetase (ALA-S) and 4,5, dioxovaleric transaminase (DOVA-T), the two enzymes forming ALA, were readily detected and their activities, although low, were of the same order. 5. 5. δ-Aminolevulinic acid dehydratase (ALA-D) activity was almost negligible and both porphobilinogenase (PBGase) and deaminase were absent or inactive. 6. 6. Heme-Synthetase (Heme-S) was totally functional. 7. 7. It is concluded that T. cruzi has lost part of its heme biosynthetic pathway, possibly due to mutations of several genes involved in the synthesis of the soluble enzymes ALA-D, PBGase, deaminase and probably others preceding Heme-S; while the particulate enzymes Suc CoA-S, ALA-S, DOVA-T and Heme-S are functional. As a consequence, the host should supply the parasite with the porphyrin substrate to form its essential heme compounds. © 1982. Fil:Salzman, T.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wider de Xifra, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A.M.D.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Stoppani, A.O.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1982 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v72_n4_p663_Salzman http://hdl.handle.net/20.500.12110/paper_03050491_v72_n4_p663_Salzman
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	5 aminolevulinate synthase aminolevulinate aminotransferase aminotransferase ammonia lyase Ammonia Lyases ferrochelatase heme porphobilinogen synthase porphyrin Succinate CoA Ligases succinyl coenzyme A synthetase animal article biosynthesis enzymology metabolism Trypanosoma cruzi 5-Aminolevulinate Synthetase Ammonia-Lyases Animal Ferrochelatase Heme Porphobilinogen Synthase Porphyrins Succinate-CoA Ligases Support, Non-U.S. Gov't Transaminases Trypanosoma cruzi
spellingShingle	5 aminolevulinate synthase aminolevulinate aminotransferase aminotransferase ammonia lyase Ammonia Lyases ferrochelatase heme porphobilinogen synthase porphyrin Succinate CoA Ligases succinyl coenzyme A synthetase animal article biosynthesis enzymology metabolism Trypanosoma cruzi 5-Aminolevulinate Synthetase Ammonia-Lyases Animal Ferrochelatase Heme Porphobilinogen Synthase Porphyrins Succinate-CoA Ligases Support, Non-U.S. Gov't Transaminases Trypanosoma cruzi Salzman, Teresa Ana Stella de Rosellini, Ana María Cristina Wider de Xifra, Eva Adela Batlle, Alcira María del Carmen Stoppani, Andrés Oscar Manuel Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi
topic_facet	5 aminolevulinate synthase aminolevulinate aminotransferase aminotransferase ammonia lyase Ammonia Lyases ferrochelatase heme porphobilinogen synthase porphyrin Succinate CoA Ligases succinyl coenzyme A synthetase animal article biosynthesis enzymology metabolism Trypanosoma cruzi 5-Aminolevulinate Synthetase Ammonia-Lyases Animal Ferrochelatase Heme Porphobilinogen Synthase Porphyrins Succinate-CoA Ligases Support, Non-U.S. Gov't Transaminases Trypanosoma cruzi
description	1. 1. Heme compounds are necessary as a growth factor for Trypanosoma cruzi in culture, this porphyrin requirement being due to the inability of the parasite to synthesize heme. To obtain supporting evidence for this hypothesis, an extensive study of porphyrin biosynthesis in the epimastogote form of T. cruzi (Tulahuén strain) was carried out. 2. 2. Low levels of endogenous δ-aminolevulinic acid (ALA) and porphobilinogen (PBG) were found in extracts of T. cruzi. Free porphyrins and heme contents were practically nil. 3. 3. The activity of succinyl CoA synthetase (Suc, CoA-S) was rather high and therefore non-limiting. 4. 4. Both δ-aminolevulinic acid synthetase (ALA-S) and 4,5, dioxovaleric transaminase (DOVA-T), the two enzymes forming ALA, were readily detected and their activities, although low, were of the same order. 5. 5. δ-Aminolevulinic acid dehydratase (ALA-D) activity was almost negligible and both porphobilinogenase (PBGase) and deaminase were absent or inactive. 6. 6. Heme-Synthetase (Heme-S) was totally functional. 7. 7. It is concluded that T. cruzi has lost part of its heme biosynthetic pathway, possibly due to mutations of several genes involved in the synthesis of the soluble enzymes ALA-D, PBGase, deaminase and probably others preceding Heme-S; while the particulate enzymes Suc CoA-S, ALA-S, DOVA-T and Heme-S are functional. As a consequence, the host should supply the parasite with the porphyrin substrate to form its essential heme compounds. © 1982.
author	Salzman, Teresa Ana Stella de Rosellini, Ana María Cristina Wider de Xifra, Eva Adela Batlle, Alcira María del Carmen Stoppani, Andrés Oscar Manuel
author_facet	Salzman, Teresa Ana Stella de Rosellini, Ana María Cristina Wider de Xifra, Eva Adela Batlle, Alcira María del Carmen Stoppani, Andrés Oscar Manuel
author_sort	Salzman, Teresa Ana
title	Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi
title_short	Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi
title_full	Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi
title_fullStr	Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi
title_full_unstemmed	Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi
title_sort	porphyrin biosynthesis in parasitic hemoflagellates: functional and defective enzymes in trypanosoma cruzi
publishDate	1982
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v72_n4_p663_Salzman http://hdl.handle.net/20.500.12110/paper_03050491_v72_n4_p663_Salzman
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Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi

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