Relationshiop between phosphorylation and activity of pyruvate dehydrogenase in rat liver mitochondria and the absence of such a relationship for pyruvate carboxylase. 1978

A B Leiter, and M Weinberg, and F Isohashi, and M F Utter

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D008930 Mitochondria, Liver Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4) Liver Mitochondria,Liver Mitochondrion,Mitochondrion, Liver
D010710 Phosphates Inorganic salts of phosphoric acid. Inorganic Phosphate,Phosphates, Inorganic,Inorganic Phosphates,Orthophosphate,Phosphate,Phosphate, Inorganic
D010750 Phosphoproteins Phosphoprotein
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D011766 Pyruvate Carboxylase A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1. Carboxylase, Pyruvate
D011768 Pyruvate Dehydrogenase Complex A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed) Complex, Pyruvate Dehydrogenase,Dehydrogenase Complex, Pyruvate
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
March 1974, The Journal of biological chemistry,
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
January 1977, Pediatric research,
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
January 1969, The Journal of biological chemistry,
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
November 1973, The Journal of biological chemistry,
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
January 1986, Ukrainskii biokhimicheskii zhurnal (1978),
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
December 1972, European journal of biochemistry,
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
January 2012, Methods in molecular biology (Clifton, N.J.),
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
October 1979, The Journal of biological chemistry,
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
April 1988, European journal of biochemistry,
A B Leiter, and M Weinberg, and F Isohashi, and M F Utter
June 1968, Biochemical and biophysical research communications,
Copied contents to your clipboard!