4-phosphoerythronate and 2-phospholactic-acid

4-phosphoerythronate has been researched along with 2-phospholactic-acid* in 3 studies

Other Studies

3 other study(ies) available for 4-phosphoerythronate and 2-phospholactic-acid

ArticleYear
The Metabolite Repair Enzyme Phosphoglycolate Phosphatase Regulates Central Carbon Metabolism and Fosmidomycin Sensitivity in Plasmodium falciparum.
    mBio, 2019, 12-10, Volume: 10, Issue:6

    Members of the haloacid dehalogenase (HAD) family of metabolite phosphatases play an important role in regulating multiple pathways in

    Topics: Antimalarials; Carbon; Drug Resistance; Fosfomycin; Glycolysis; Humans; Lactates; Malaria, Falciparum; Phosphoric Monoester Hydrolases; Plasmodium falciparum; Sugar Acids

2019
A conserved phosphatase destroys toxic glycolytic side products in mammals and yeast.
    Nature chemical biology, 2016, Volume: 12, Issue:8

    Metabolic enzymes are very specific. However, most of them show weak side activities toward compounds that are structurally related to their physiological substrates, thereby producing side products that may be toxic. In some cases, 'metabolite repair enzymes' eliminating side products have been identified. We show that mammalian glyceraldehyde 3-phosphate dehydrogenase and pyruvate kinase, two core glycolytic enzymes, produce 4-phosphoerythronate and 2-phospho-L-lactate, respectively. 4-Phosphoerythronate strongly inhibits an enzyme of the pentose phosphate pathway, whereas 2-phospho-L-lactate inhibits the enzyme producing the glycolytic activator fructose 2,6-bisphosphate. We discovered that a single, widely conserved enzyme, known as phosphoglycolate phosphatase (PGP) in mammals, dephosphorylates both 4-phosphoerythronate and 2-phospho-L-lactate, thereby preventing a block in the pentose phosphate pathway and glycolysis. Its yeast ortholog, Pho13, similarly dephosphorylates 4-phosphoerythronate and 2-phosphoglycolate, a side product of pyruvate kinase. Our work illustrates how metabolite repair enzymes can make up for the limited specificity of metabolic enzymes and permit high flux in central metabolic pathways.

    Topics: Glycolates; Glycolysis; HCT116 Cells; Humans; Lactates; Pentose Phosphate Pathway; Phosphoric Monoester Hydrolases; Phosphorylation; Pyruvate Kinase; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Substrate Specificity; Sugar Acids

2016
A Guardian Angel Phosphatase for Mainline Carbon Metabolism.
    Trends in biochemical sciences, 2016, Volume: 41, Issue:11

    It is increasingly clear that many metabolic enzymes mistakenly form minor but toxic side-products that must be eliminated to maintain normal fluxes. Collard et al. show that this is true of two iconic glycolytic enzymes, and that a hitherto somewhat mysterious phosphatase rescues central carbon metabolism from their mistakes.

    Topics: Fructosediphosphates; Gluconates; Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+); Glycolysis; Humans; Hydrolysis; Lactates; Phosphoric Monoester Hydrolases; Pyruvate Kinase; RNA, Small Interfering; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Secondary Metabolism; Sugar Acids

2016
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