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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todo:paper_03050491_v72_n4_p663_Salzman2023-10-03T15:21:16Z Porphyrin biosynthesis in parasitic hemoflagellates: Functional and defective enzymes in Trypanosoma cruzi Salzman, T.A. Stella, A.M. Wider de Xifra, E.A. Batlle, A.M.D.C. Docampo, R. Stoppani, A.O.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03050491_v72_n4_p663_Salzman |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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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, T.A. Stella, A.M. Wider de Xifra, E.A. Batlle, A.M.D.C. Docampo, R. Stoppani, A.O.M. 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. |
| format |
JOUR |
| author |
Salzman, T.A. Stella, A.M. Wider de Xifra, E.A. Batlle, A.M.D.C. Docampo, R. Stoppani, A.O.M. |
| author_facet |
Salzman, T.A. Stella, A.M. Wider de Xifra, E.A. Batlle, A.M.D.C. Docampo, R. Stoppani, A.O.M. |
| author_sort |
Salzman, T.A. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_03050491_v72_n4_p663_Salzman |
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