Heme synthesis in Crithidia deanei: Influence of the endosymbiote
1. 1. The activity of the following enzymes involved in the biosynthesis of porphyrins was determined in endosymbiote-free and endosymbiote-containing Crithidia deanei grown in a chemically defined medium: succinyl Coenzyme A synthetase (Suc.CoA-S), 5-aminolevulinate synthetase (ALA-S), 4,5-dioxoval...
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| Formato: | Artículo publishedVersion |
| Lenguaje: | Inglés |
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1985
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0020711X_v17_n12_p1343_Salzman |
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paperaa:paper_0020711X_v17_n12_p1343_Salzman2023-06-12T16:42:11Z Heme synthesis in Crithidia deanei: Influence of the endosymbiote Int. J. Biochem. 1985;17(12):1343-1347 Salzman, T.A. Del Batlle, C.A.M. Angluster, J. De Souza, W. enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis 1. 1. The activity of the following enzymes involved in the biosynthesis of porphyrins was determined in endosymbiote-free and endosymbiote-containing Crithidia deanei grown in a chemically defined medium: succinyl Coenzyme A synthetase (Suc.CoA-S), 5-aminolevulinate synthetase (ALA-S), 4,5-dioxovaleric acid transaminase (DOVA-T), 5-aminolevulinate dehydratase (ALA-D), por- phobilinogenase (PBGase), deaminase and heme synthetase (Heme-S). The amount of 5-aminolevulinic acid (ALA) and porphobilinogen, porphyrins and heme was also determined. 2. 2. ALA and PBG were detected in C. deanei. The levels of free porphyrins was low. Heme concentration was nil. 3. 3. The activity of ALA-D. deaminase and PBGase was not detected in C deanei. 4. 4. The activity of Suc.CoA-S and ALA-S were twice higher in symbiote-containing than in aposymbiotic C. deanei. Aposymbiotic cells had a higher activity of DOVA-T than symbiote-containing cells. 5. 5. The level of Heme-S, measured using protoporphyrin as substrate, was twice as high in symbiotecontaining than in symbiote-free cells,. © 1985. Fil:Salzman, T.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del Batlle, C.A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1985 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v17_n12_p1343_Salzman |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| language |
Inglés |
| orig_language_str_mv |
eng |
| topic |
enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis |
| spellingShingle |
enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis Salzman, T.A. Del Batlle, C.A.M. Angluster, J. De Souza, W. Heme synthesis in Crithidia deanei: Influence of the endosymbiote |
| topic_facet |
enzyme heme crithidia deanei nonhuman protozoon 5-Aminolevulinate Synthetase Aminolevulinic Acid Comparative Study Crithidia Heme Porphyrins Rickettsiaceae Succinate-CoA Ligases Support, Non-U.S. Gov't Symbiosis |
| description |
1. 1. The activity of the following enzymes involved in the biosynthesis of porphyrins was determined in endosymbiote-free and endosymbiote-containing Crithidia deanei grown in a chemically defined medium: succinyl Coenzyme A synthetase (Suc.CoA-S), 5-aminolevulinate synthetase (ALA-S), 4,5-dioxovaleric acid transaminase (DOVA-T), 5-aminolevulinate dehydratase (ALA-D), por- phobilinogenase (PBGase), deaminase and heme synthetase (Heme-S). The amount of 5-aminolevulinic acid (ALA) and porphobilinogen, porphyrins and heme was also determined. 2. 2. ALA and PBG were detected in C. deanei. The levels of free porphyrins was low. Heme concentration was nil. 3. 3. The activity of ALA-D. deaminase and PBGase was not detected in C deanei. 4. 4. The activity of Suc.CoA-S and ALA-S were twice higher in symbiote-containing than in aposymbiotic C. deanei. Aposymbiotic cells had a higher activity of DOVA-T than symbiote-containing cells. 5. 5. The level of Heme-S, measured using protoporphyrin as substrate, was twice as high in symbiotecontaining than in symbiote-free cells,. © 1985. |
| format |
Artículo Artículo publishedVersion |
| author |
Salzman, T.A. Del Batlle, C.A.M. Angluster, J. De Souza, W. |
| author_facet |
Salzman, T.A. Del Batlle, C.A.M. Angluster, J. De Souza, W. |
| author_sort |
Salzman, T.A. |
| title |
Heme synthesis in Crithidia deanei: Influence of the endosymbiote |
| title_short |
Heme synthesis in Crithidia deanei: Influence of the endosymbiote |
| title_full |
Heme synthesis in Crithidia deanei: Influence of the endosymbiote |
| title_fullStr |
Heme synthesis in Crithidia deanei: Influence of the endosymbiote |
| title_full_unstemmed |
Heme synthesis in Crithidia deanei: Influence of the endosymbiote |
| title_sort |
heme synthesis in crithidia deanei: influence of the endosymbiote |
| publishDate |
1985 |
| url |
http://hdl.handle.net/20.500.12110/paper_0020711X_v17_n12_p1343_Salzman |
| work_keys_str_mv |
AT salzmanta hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote AT delbatllecam hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote AT anglusterj hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote AT desouzaw hemesynthesisincrithidiadeaneiinfluenceoftheendosymbiote |
| _version_ |
1769810158043529216 |