Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation

The high levels of δ-aminolevulinate synthetase (ALA-S) in Rhodopseudomonas palustris cells grown anaerobically in the light (Ph) decrease to those found in cells grown aerobically in the dark (A), when the former cultures were vigorously oxygenated; simultaneously bacteriochlorophyll (Bchl) synthes...

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Autores principales:	Viale, Alberto Américo, Batlle, Alcira María del Carmen
Publicado:	1987
Materias:	5 aminolevulinate synthase bacteriochlorophyll chloramphenicol porphyrin adaptation article biosynthesis enzymology homeostasis metabolism oxidation reduction reaction Rhodopseudomonas 5-Aminolevulinate Synthetase Adaptation, Physiological Bacteriochlorophylls Chloramphenicol Homeostasis Oxidation-Reduction Porphyrins Support, Non-U.S. Gov't
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n4_p379_Viale http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_Viale
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_0020711X_v19_n4_p379_Viale
record_format	dspace
spelling	paper:paper_0020711X_v19_n4_p379_Viale2025-07-30T17:23:36Z Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation Viale, Alberto Américo Batlle, Alcira María del Carmen 5 aminolevulinate synthase bacteriochlorophyll chloramphenicol porphyrin adaptation article biosynthesis enzymology homeostasis metabolism oxidation reduction reaction Rhodopseudomonas 5-Aminolevulinate Synthetase Adaptation, Physiological Bacteriochlorophylls Chloramphenicol Homeostasis Oxidation-Reduction Porphyrins Rhodopseudomonas Support, Non-U.S. Gov't The high levels of δ-aminolevulinate synthetase (ALA-S) in Rhodopseudomonas palustris cells grown anaerobically in the light (Ph) decrease to those found in cells grown aerobically in the dark (A), when the former cultures were vigorously oxygenated; simultaneously bacteriochlorophyll (Bchl) synthesis abruptly halted leading to diminished steady-state specific Bchl content. When flushing oxygen was interrupted, enzymic activity increased, whether chloramphenicol was present or not in the medium; if the protein synthesis inhibitor was added when oxygenation started, ALA-S declined in the same fashion as in its absence, but thereafter reactivation of the enzyme was lower than before. Succinyl-CoA-synthetase and ALA-dehydratase activities were also measured under the conditions described, and no changes at all have been observed. The existence of different forms of ALA-S in R. palustris depending on growth conditions is postulated along with the formation of low molecular weight factors which can modulate ALA-S activity by binding to the enzyme; a widespread mechanism in the adaptation of micro-organisms to changes in environment. It is also proposed that this particular regulatory phenomenon, could be referred to as a switch off/on mechanism controlling ALA-S activity in R. palustris. © 1987. Fil:Viale, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1987 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n4_p379_Viale http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_Viale
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 bacteriochlorophyll chloramphenicol porphyrin adaptation article biosynthesis enzymology homeostasis metabolism oxidation reduction reaction Rhodopseudomonas 5-Aminolevulinate Synthetase Adaptation, Physiological Bacteriochlorophylls Chloramphenicol Homeostasis Oxidation-Reduction Porphyrins Rhodopseudomonas Support, Non-U.S. Gov't
spellingShingle	5 aminolevulinate synthase bacteriochlorophyll chloramphenicol porphyrin adaptation article biosynthesis enzymology homeostasis metabolism oxidation reduction reaction Rhodopseudomonas 5-Aminolevulinate Synthetase Adaptation, Physiological Bacteriochlorophylls Chloramphenicol Homeostasis Oxidation-Reduction Porphyrins Rhodopseudomonas Support, Non-U.S. Gov't Viale, Alberto Américo Batlle, Alcira María del Carmen Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
topic_facet	5 aminolevulinate synthase bacteriochlorophyll chloramphenicol porphyrin adaptation article biosynthesis enzymology homeostasis metabolism oxidation reduction reaction Rhodopseudomonas 5-Aminolevulinate Synthetase Adaptation, Physiological Bacteriochlorophylls Chloramphenicol Homeostasis Oxidation-Reduction Porphyrins Rhodopseudomonas Support, Non-U.S. Gov't
description	The high levels of δ-aminolevulinate synthetase (ALA-S) in Rhodopseudomonas palustris cells grown anaerobically in the light (Ph) decrease to those found in cells grown aerobically in the dark (A), when the former cultures were vigorously oxygenated; simultaneously bacteriochlorophyll (Bchl) synthesis abruptly halted leading to diminished steady-state specific Bchl content. When flushing oxygen was interrupted, enzymic activity increased, whether chloramphenicol was present or not in the medium; if the protein synthesis inhibitor was added when oxygenation started, ALA-S declined in the same fashion as in its absence, but thereafter reactivation of the enzyme was lower than before. Succinyl-CoA-synthetase and ALA-dehydratase activities were also measured under the conditions described, and no changes at all have been observed. The existence of different forms of ALA-S in R. palustris depending on growth conditions is postulated along with the formation of low molecular weight factors which can modulate ALA-S activity by binding to the enzyme; a widespread mechanism in the adaptation of micro-organisms to changes in environment. It is also proposed that this particular regulatory phenomenon, could be referred to as a switch off/on mechanism controlling ALA-S activity in R. palustris. © 1987.
author	Viale, Alberto Américo Batlle, Alcira María del Carmen
author_facet	Viale, Alberto Américo Batlle, Alcira María del Carmen
author_sort	Viale, Alberto Américo
title	Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_short	Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_full	Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_fullStr	Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_full_unstemmed	Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation
title_sort	porphyrin biosynthesis in rhodopseudomonas palustris-xii. δ-aminolevulinate synthetase switch-off/on regulation
publishDate	1987
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n4_p379_Viale http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n4_p379_Viale
work_keys_str_mv	AT vialealbertoamerico porphyrinbiosynthesisinrhodopseudomonaspalustrisxiidaminolevulinatesynthetaseswitchoffonregulation AT batllealciramariadelcarmen porphyrinbiosynthesisinrhodopseudomonaspalustrisxiidaminolevulinatesynthetaseswitchoffonregulation
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Porphyrin biosynthesis in Rhodopseudomonas palustris-XII. δ-aminolevulinate synthetase switch-off/on regulation

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