Human erythrocyte pyruvate kinase plays an important role in erythrocyte metabolism. Mutation on the gene results in pyruvate kinase deficiency and is an important cause of hereditary nonspherocytic hemolytic anemia. Because of difficulties in isolating the mutant enzymes from patients, these mutations have not been fully studied. In this study, a complementary DNA (cDNA) encoding the human ery...

Human erythrocyte pyruvate kinase plays an important role in erythrocyte metabolism. Mutation on the gene results in pyruvate kinase deficiency and is an important cause of hereditary nonspherocytic hemolytic anemia. Because of difficulties in isolating the mutant enzymes from patients, these mutations have not been fully studied. In this study, a complementary DNA (cDNA) encoding the human ery...

Pyruvate kinase (EC 2.7.1.40) from oyster tissues occurs in at least two electrophoretically and kinetically distinguishable forms in mantle tissue and in adductor muscle. In mantle, pyruvate kinase activity appears as a single band having a p1 value of 6.35 while adductor pyruvate kinase appears as a “doublet” having p1 values of 5.6 and 6.5. Both forms of the enzyme have an essential requirem...

Glycolysis is a ubiquitous pathway thought to be essential for the production of oil in developing seeds of Arabidopsis thaliana and oil crops. Compartmentation of primary metabolism in developing embryos poses a significant challenge for testing this hypothesis and for the engineering of seed biomass production. It also raises the question whether there is a preferred route of carbon from impo...

Pyruvate dehydrogenase from pig heart exists in active and inactive forms. Interconversion from the active (dephospho) form into the inactive (phospho) form is catalyzed by an ATP-dependent kinase. Conversely the enzyme is reactivated by a phosphatase which removes the phosphate group from the protein. By gradient centrifugation pyruvate dehydrogenase was prepared free of phosphatase but still ...

Pyruvate kinase catalyzes the rate-limiting final step of glycolysis, generating adenosine triphosphate (ATP) and pyruvate. The M2 tumor-specific isoform of pyruvate kinase (PKM2) promotes glucose uptake and lactate production in the presence of oxygen, known as aerobic glycolysis or the Warburg effect. As recently reported in Nature, PKM2, besides its metabolic function, has a nonmetabolic fun...

1. Extracts of Acetobacter xylinum were found to contain the glycolytic enzymes involved in the conversion of triose phosphate into pyruvate. Pyruvate kinase had the lowest relative activity. Phosphofructokinase activity was not detected in the extracts. 2. Only slight differences in the activity of pyruvate kinase were observed between cells grown on glucose and those grown on intermediates of...

The properties of pyruvate kinase from soybean (Glycine max L.) nodule cytosol were examined to determine what influence the N(2) fixation process might have on this supposed key control enzyme. A crude enzyme preparation was prepared by chromatography of cytosol extract on a diethylaminoethyl-cellulose column. ATP and citrate at 5 mm concentrations inhibited pyruvate kinase 27 and 34%, respect...