BIOMAT Database Logo BIOMAT Database Logo

Fructose-1,6-diphosphate binding by two forms of pyruvate kinase purified from human erythrocytes. 1977

H Garreau, and S Columelli, and J Marie, and A Kahn

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D007700 Kinetics The rate dynamics in chemical or physical systems.
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011770 Pyruvate Kinase ATP:pyruvate 2-O-phosphotransferase. A phosphotransferase that catalyzes reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (L, R, M1, and M2). Deficiency of the enzyme results in hemolytic anemia. EC 2.7.1.40. L-Type Pyruvate Kinase,M-Type Pyruvate Kinase,M1-Type Pyruvate Kinase,M2-Type Pyruvate Kinase,Pyruvate Kinase L,R-Type Pyruvate Kinase,L Type Pyruvate Kinase,M Type Pyruvate Kinase,M1 Type Pyruvate Kinase,M2 Type Pyruvate Kinase,Pyruvate Kinase, L-Type,Pyruvate Kinase, M-Type,Pyruvate Kinase, M1-Type,Pyruvate Kinase, M2-Type,Pyruvate Kinase, R-Type,R Type Pyruvate Kinase
D004792 Enzyme Precursors Physiologically inactive substances that can be converted to active enzymes. Enzyme Precursor,Proenzyme,Proenzymes,Zymogen,Zymogens,Precursor, Enzyme,Precursors, Enzyme
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D005636 Fructosephosphates
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining

Related Publications

H Garreau, and S Columelli, and J Marie, and A Kahn
Activation of liver pyruvate kinase by fructose 1,6-diphosphate.
February 1967, The Biochemical journal,
H Garreau, and S Columelli, and J Marie, and A Kahn
Allosteric activation of human erythrocyte pyruvate kinase by fructose-1,6-diphosphate. Kinetic and equilibrium binding studies.
January 1972, Biochimie,
H Garreau, and S Columelli, and J Marie, and A Kahn
Regulation of pyruvate kinase by fructose 1,6-diphosphate in Saccharomyces cerevisiae.
January 1971, European journal of biochemistry,
H Garreau, and S Columelli, and J Marie, and A Kahn
Fructose 1,6-diphosphate, a reactivator of Cu++-inhibited pyruvate kinase from liver.
April 1967, Biochemical and biophysical research communications,
H Garreau, and S Columelli, and J Marie, and A Kahn
Additional kinetic distinctions between normal pyruvate kinase and a mutant isozyme from human erythrocytes. Correction of the kinetic anomaly by fructose-1,6-diphosphate.
March 1971, Blood,
H Garreau, and S Columelli, and J Marie, and A Kahn
A kinetic study of Baker's-yeast pyruvate kinase activated by fructose 1,6-diphosphate.
October 1972, The Biochemical journal,
H Garreau, and S Columelli, and J Marie, and A Kahn
Regulation of M2-type pyruvate kinase from human meningioma by allosteric effectors fructose 1,6 diphosphate and L-alanine.
October 1992, Cancer biochemistry biophysics,
H Garreau, and S Columelli, and J Marie, and A Kahn
Neurospora fructose-1,6-diphosphate aldolase: inhibition by sodium pyruvate.
October 1974, Biochemical and biophysical research communications,
H Garreau, and S Columelli, and J Marie, and A Kahn
[Sensitivity of fructose diphosphate binding sites of yeast pyruvate kinase to pyruvate kinase antibodies].
January 1968, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
H Garreau, and S Columelli, and J Marie, and A Kahn
Interaction between potassium-, ammonium- and fructose-1,6-diphosphate activation of yeast pyruvate kinase.
May 1967, Nature,
Copied contents to your clipboard!