Disease relevance of phosphoenolpyruvate

• The saturation of the pyruvate kinase from Lactobacillus bulgaricus is hyperbolic for ADP and cooperative for the other substrate phospho-enol-pyruvate [1].

High impact information on phosphoenolpyruvate

• The mutant enzyme for which his father was heterozygote was characterized by a decreased affinity for the substrate phospho-enol-pyruvate and a loss of homotropic interactions toward this substrate [2].
• In Pyc- as well as in wild-type cultures, levels of isocitrate lyase, malate synthase and phospho-enol-pyruvate carboxykinase in cell extracts decreased with a decreasing ethanol content in the feed [3].
• 3. S-Adenosyl-L-methionine accumulation into vacuoles does not require glucose, phosphoenolpyruvic acid, ATP, ADP nor any other tri- or di-phosphorylated nucleotides [4].
• The crystal and molecular structure of phosphoenolpyruvic acid [5].
• The rate of hydrolysis was rather insensitive to the depletion of ADP in the assay medium by an ATP regenerating system (phospho-enol-pyruvate (PEP) and pyruvate kinase (PK)) [6].

Biological context of phosphoenolpyruvate

• Substrate cycling between pyruvate kinase, pyruvate carboxylase and phospho-enol-pyruvate kinase increased ATP turnover [7].

Gene context of phosphoenolpyruvate

• Three analogs of phosphoenolpyruvic acid: (Z)-phosphoenol-3-fluoropyruvate, (Z)-phosphoenol-3-bromopyruvate and (Z)-phosphoenol-alpha-ketobutyrate were found to be substrates for yeast pyruvate kinase (ATP: pyruvate (Z)-O-phosphotransferase, EC 2.7.1.40)with maximal velocities much greater than those found for rabbit muscle pyruvate kinase [8].

References