The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae
Catabolite repression and derepression on δ‐aminolevulinate synthase (ALA‐S) and δ‐aminolevulinate dehydratase (ALA‐D) in a normal yeast strain, D27, and its derived D27/C6 (HEM R+) were investigated. ALA‐S and ALA‐D activities and intracellular ALA (I‐ALA) at different physiological states of the c...
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1993
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paper:paper_0749503X_v9_n2_p165_Garcia2023-06-08T15:45:41Z The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae catabolite repression and derepression Saccharomyces cerevisiae HEM R+ mutants δ‐aminoleuvulinate dehydratase δ‐Aminolevulinate synthase 5 aminolevulinate synthase porphobilinogen synthase porphyrin article biosynthesis catabolite repression fungus mutant metabolic regulation nonhuman saccharomyces cerevisiae 5-Aminolevulinate Synthetase Cytochromes Enzyme Repression Hydroxymethylbilane Synthase Mutation Porphobilinogen Synthase Porphyrins Saccharomyces cerevisiae Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogen Decarboxylase Fungi Saccharomyces cerevisiae Catabolite repression and derepression on δ‐aminolevulinate synthase (ALA‐S) and δ‐aminolevulinate dehydratase (ALA‐D) in a normal yeast strain, D27, and its derived D27/C6 (HEM R+) were investigated. ALA‐S and ALA‐D activities and intracellular ALA (I‐ALA) at different physiological states of the cells were measured. In YPD medium, under conditions of repression and when glucose was exhausted, both strains behaved identically as if the mutation was not expressed. In YPEt medium, however, both ALA‐S and ALA‐D activities were higher than in YPD, but the I‐ALA content and the enzymic activity profiles shown by the two strains were quite different. It appears, therefore, that the mutation causes a deregulation of ALA‐S, so that its activity is kept at a high level throughout the cell cycle. This would explain the increased levels of cytochromes present in the mutant. This mutation may affect some regulatory aspect of ALA formation and renders an ALA‐S of high activity; moreover, this enzyme species seems to be more stable than in the normal strain. Copyright © 1993 John Wiley & Sons Ltd. 1993 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0749503X_v9_n2_p165_Garcia http://hdl.handle.net/20.500.12110/paper_0749503X_v9_n2_p165_Garcia |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
catabolite repression and derepression Saccharomyces cerevisiae HEM R+ mutants δ‐aminoleuvulinate dehydratase δ‐Aminolevulinate synthase 5 aminolevulinate synthase porphobilinogen synthase porphyrin article biosynthesis catabolite repression fungus mutant metabolic regulation nonhuman saccharomyces cerevisiae 5-Aminolevulinate Synthetase Cytochromes Enzyme Repression Hydroxymethylbilane Synthase Mutation Porphobilinogen Synthase Porphyrins Saccharomyces cerevisiae Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogen Decarboxylase Fungi Saccharomyces cerevisiae |
| spellingShingle |
catabolite repression and derepression Saccharomyces cerevisiae HEM R+ mutants δ‐aminoleuvulinate dehydratase δ‐Aminolevulinate synthase 5 aminolevulinate synthase porphobilinogen synthase porphyrin article biosynthesis catabolite repression fungus mutant metabolic regulation nonhuman saccharomyces cerevisiae 5-Aminolevulinate Synthetase Cytochromes Enzyme Repression Hydroxymethylbilane Synthase Mutation Porphobilinogen Synthase Porphyrins Saccharomyces cerevisiae Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogen Decarboxylase Fungi Saccharomyces cerevisiae The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae |
| topic_facet |
catabolite repression and derepression Saccharomyces cerevisiae HEM R+ mutants δ‐aminoleuvulinate dehydratase δ‐Aminolevulinate synthase 5 aminolevulinate synthase porphobilinogen synthase porphyrin article biosynthesis catabolite repression fungus mutant metabolic regulation nonhuman saccharomyces cerevisiae 5-Aminolevulinate Synthetase Cytochromes Enzyme Repression Hydroxymethylbilane Synthase Mutation Porphobilinogen Synthase Porphyrins Saccharomyces cerevisiae Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogen Decarboxylase Fungi Saccharomyces cerevisiae |
| description |
Catabolite repression and derepression on δ‐aminolevulinate synthase (ALA‐S) and δ‐aminolevulinate dehydratase (ALA‐D) in a normal yeast strain, D27, and its derived D27/C6 (HEM R+) were investigated. ALA‐S and ALA‐D activities and intracellular ALA (I‐ALA) at different physiological states of the cells were measured. In YPD medium, under conditions of repression and when glucose was exhausted, both strains behaved identically as if the mutation was not expressed. In YPEt medium, however, both ALA‐S and ALA‐D activities were higher than in YPD, but the I‐ALA content and the enzymic activity profiles shown by the two strains were quite different. It appears, therefore, that the mutation causes a deregulation of ALA‐S, so that its activity is kept at a high level throughout the cell cycle. This would explain the increased levels of cytochromes present in the mutant. This mutation may affect some regulatory aspect of ALA formation and renders an ALA‐S of high activity; moreover, this enzyme species seems to be more stable than in the normal strain. Copyright © 1993 John Wiley & Sons Ltd. |
| title |
The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae |
| title_short |
The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae |
| title_full |
The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae |
| title_fullStr |
The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae |
| title_full_unstemmed |
The role of ALA‐S and ALA‐D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae |
| title_sort |
role of ala‐s and ala‐d in regulating porphyrin biosynthesis in a normal and a hem r+ mutant strain of saccharomyces cerevisiae |
| publishDate |
1993 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0749503X_v9_n2_p165_Garcia http://hdl.handle.net/20.500.12110/paper_0749503X_v9_n2_p165_Garcia |
| _version_ |
1768542649380241408 |