Pyruvate carboxylase. VII. A possible role for tightly bound manganese.
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چکیده
منابع مشابه
Bacterial acetone carboxylase is a manganese-dependent metalloenzyme.
Bacterial acetone carboxylase catalyzes the ATP-dependent carboxylation of acetone to acetoacetate with the concomitant production of AMP and two inorganic phosphates. The importance of manganese in Rhodobacter capsulatus acetone carboxylase has been established through a combination of physiological, biochemical, and spectroscopic studies. Depletion of manganese from the R. capsulatus growth m...
متن کاملCharacterization and regulation of pyruvate carboxylase of Bacillus licheniformis.
Cell-free extracts of Bacillus licheniformis were found to contain pyruvate carboxylase which catalyzes the reaction between pyruvate and bicarbonate to yield oxalacetate in the presence of adenosine triphosphate (ATP), acetylcoenzyme A (CoA), and manganese. The plot between the reaction velocity of the carboxylation by the partially purified pyruvate carboxylase (25-fold) and the concentration...
متن کاملPig liver pyruvate carboxylase. Purification, properties and cation specificity.
1. Pyruvate carboxylase was purified to apparent homogeneity from pig liver mitochondria and shown to be free of all kinetically contaminating enzymes. 2. The enzyme has a mol. wt. of 520000 and is composed of four subunits, each with a mol. wt. of 130000. 3. The enzyme can exist as the active tetramer, dimer and monomer, although the tetramer appears to be the form in which the enzyme is norma...
متن کاملRelationshiop between phosphorylation and activity of pyruvate dehydrogenase in rat liver mitochondria and the absence of such a relationship for pyruvate carboxylase.
Linn et al. (Linn, T. C., Pettit, F. H., and Reed, L. J. (1969) Proc. Natl. Acad. Sci. U. S. A. 62, 234-241) have shown that purified preparations of pyruvate dehydrogenase complex can be inactivated by phosphorylation and reactivated by dephosphorylation. The present study shows that these processes also take place in rat liver mitochondria. In addition, we have compared such changes with poss...
متن کاملRelationship between Phosphorylation and Activity of Pyruvate Dehydrogenase in Rat Liver Mitochondria and the Absence of Such a Relationship for Pyruvate Carboxylase*
Linn et al. (Linn, T. C., Pettit, F. H., and Reed, L. J. (1969) Proc. Natl. Acad. Sci. U. S. A. 62, 234-241) have shown that purified preparations of pyruvate dehydrogenase complex can be inactivated by phosphorylation and reactivated by dephosphorylation. The present study shows that these processes also take place in rat liver mitochondria. In addition, we have compared such changes with poss...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 241 15 شماره
صفحات -
تاریخ انتشار 1966