Toxicogenomic Response of Rhodospirillum rubrum S1H to the Micropollutant Triclosan
نویسندگان
چکیده
منابع مشابه
The Structure of Rhodospirillum rubrum
Cells from serial cultures of R. rubrum, grown anaerobically in the light, were harvested at intervals from (1/2) to 15 days and sectioned for electron microscopy by conventional methods. Cells of this species possess a multilayered outer envelope, and the external cell surface is differentiated into ridges extending parallel or obliquely to the long axis of the cell. Cells from very young cult...
متن کاملPhotosynthesis in Rhodospirillum rubrum
Ribulose 1,5-diphosphate carboxylase has been isolated from autotrophically cultured Rhoclospirillum rubrum. The molecular weight is 120,000. The K, for ribulose 1,5diphosphate is 83 mM, and for CO2 is 59 mM. The enzyme is inhibited by three important metabolites: citrate, an intermediate of the tricarboxylic acid cycle; inorganic phosphate; and 3-phosphoglyceric acid, the product of the reacti...
متن کاملPhotosynthesis in Rhodospirillum rubrum
Ribulose 1,5-diphosphate carboxylase has been isolated from autotrophically cultured Rhoclospirillum rubrum. The molecular weight is 120,000. The K, for ribulose 1,5diphosphate is 83 mM, and for CO2 is 59 mM. The enzyme is inhibited by three important metabolites: citrate, an intermediate of the tricarboxylic acid cycle; inorganic phosphate; and 3-phosphoglyceric acid, the product of the reacti...
متن کاملHomoserine Dehydrogenase of Rhodospirillum rubrum
Homoserine dehydrogenase catalyzes the reductive conversion of aspartate P-semialdehyde to homoserine (l), which has been identified in several microorganisms as a precursor of three other amino acids. On the one hand, homoserine is converted to methionine, and through a separate sequence of reactions is transformed to threonine, a precursor of isoleucine (2). Recent studies (3-7) have provided...
متن کاملHomoserine Dehydrsgenase of Rhodospirillum rubrum
Homoserine dehydrogenase of Rhodospirillum rubrum has been purified by heat treatment, ammonium sulfate fractionation, and by two successive gel filtration steps on Sephadex G-ZOO in the absence and presence of L-threonine, an allosteric inhibitor. The pure protein is free of aspartokinase and aspartate /?-semialdehyde dehydrogenase activities. From the sedimentation velocity centrifugation and...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2010
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.01254-09