Pyruvate kinase

About: Pyruvate kinase is a research topic. Over the lifetime, 5683 publications have been published within this topic receiving 180020 citations. The topic is also known as: ATP:pyruvate 2-O-phosphotransferase & phosphoenolpyruvate kinase.

Glycerol kinase: synthesis of dihydroxyacetone phosphate, sn-glycerol-3-phosphate, and chiral analogs

Abstract: Glycerol kinase (8.C. 2.1 .1.30, ATP: glycerol-3-phosphotransferase from S. cereuisiae) catalyzes the phosphorylation by ATP of glycerol, dihydroxyacetone, and certain structural analogues of glycerol. Phosphorylation of racemic mixtures produces chiral organic phosphates with enantiomeric excess (ee) >90-95Vain yields of 75-95Va (based on the quantity of that enantiomer present in the starting racemic mixture). The unphosphorylated enantiomers can be recovered from the reactton mixtures in 30-40Vo yields and 80-90% ee. This paper illustrates the use of glycerol kinase for preparative-scale (10-500 Convenient preparations ofsn-glycerol-3-phosphate (l mol) and dihydroxyacetone phosphate (0.4 mol) are also described. Regeneration of ATP in situ is accomplished using either phosphoenol pyruvate and pyruvate kinase or acetyl phosphate and acetate kinase. PEP was used per equiv of racemic starting material. The

Contribution of Malic Enzyme, Pyruvate Kinase, Phosphoenolpyruvate Carboxylase, and the Krebs Cycle to Respiration and Biosynthesis and to Intracellular pH Regulation during Hypoxia in Maize Root Tips Observed by Nuclear Magnetic Resonance Imaging and

Abstract: In vivo pyruvate synthesis by malic enzyme (ME) and pyruvate kinase and in vivo malate synthesis by phosphoenolpyruvate carboxylase and the Krebs cycle were measured by 13C incorporation from [1-'3C]glucose into glucose-6-phosphate, alanine, glutamate, aspartate, and malate. These metabolites were isolated from maize (Zea mays L.) root tips under aerobic and hypoxic conditions. '3CNuclear magnetic resonance spectroscopy and gas chromatographymass spectrometry were used to discern the positional isotopic distribution within each metabolite. This information was applied to a simple precursor-product model that enabled calculation of specific metabolic fluxes. In respiring root tips, ME was found to contribute only approximately 3% of the pyruvate synthesized, whereas pyruvate kinase contributed the balance. The activity of ME increased greater than 6-fold early in hypoxia, and then declined coincident with depletion of cytosolic malate and aspartate. We found that in respiring root tips, anaplerotic phosphoenolpyruvate carboxylase activity was high relative to ME, and therefore did not limit synthesis of pyruvate by ME. The significance of in vivo pyruvate synthesis by ME is discussed with respect to malate and pyruvate utilization by isolated mitochondria and intracellular pH regulation under hypoxia.