Regulation of the Cytoplasmic Inorganic Pyrophosphatase of Rhodospirillum rubrum
نویسندگان
چکیده
منابع مشابه
Regulatory properties of an inorganic pyrophosphatase from the photosynthic bacterium Rhodospirillum rubrum.
In Rhodospirillum rubrum, inorganic pyrophosphatase activity is observed in both the cytoplasmic and membrane fractions. The soluble enzyme accounts for about 80% of the total activity in crude extracts, and is the subject of this report. Zn(2+) is required for both activity and stability of the enzyme, which has a molecular weight of approximately 90,000 (gel-filtration determinations). The su...
متن کاملThe H(+)-pyrophosphatase of Rhodospirillum rubrum is predominantly located in polyphosphate-rich acidocalcisomes.
Acidocalcisomes are acidic, calcium storage compartments with a H(+) pump located in their membrane that have been described in several unicellular eukaryotes, including trypanosomatid and apicomplexan parasites, algae, and slime molds, and have also been found in the bacterium Agrobacterium tumefaciens. In this work, we report that the H(+)-pyrophosphatase (H(+)-PPase) of Rhodospirillum rubrum...
متن کاملThe 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 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 کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1971
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1971.tb01573.x