Phosphoenolpyruvic Acid

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phosphoenolpyruvic acid

[¦fäs·fō¦ē‚nȯl·pī′rü·vik ′as·əd]
(biochemistry)
CH2=O(OPO3H2)COOH A high-energy phosphate formed by dehydration of 2-phosphoglyceric acid; it reacts with adenosine diphosphate to form adenosinetriphosphate and enolpyruvic acid.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

Phosphoenolpyruvic Acid

 

(also phosphopyruvic acid), a high-energy compound that is an important metabolic intermediate in animals, plants, and microorganisms. The acid’s structural formula is

Phosphoenolpyruvic acid is formed during glycolysis from 2-phosphoglyceric acid upon the separation of a water molecule from the latter under the action of the enzyme enolase; it is also formed from oxalacetic acid upon decarboxylation, which is accompanied by the transfer of the phosphoryl group (—H2PO3) from nucleoside triphosphates to the pyruvic acid that is being formed.

Phosphoenolpyruvic acid is easily hydrolyzed in aqueous solutions to yield phosphoric and pyruvic acids. It figures in the biosynthesis of adenosine triphosphate, which is formed with the transfer of a phosphoryl group from phosphoenolpyruvic acid to adenosine diphosphate; the transfer results from a reaction catalyzed by the enzyme pyruvate kinase. Phosphoenolpyruvic acid is present in cells in an ionized form known as phosphoenolpyruvate.

The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.
References in periodicals archive ?
Delbaere, "The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF3," Journal of Molecular Biology, vol.
PYCARD, PYD and CARD domain-containing; TLR2, toll-like receptor-2; AdipoR1, adiponectin receptor type 1; Ptpn1, protein tyrosine phosphatase-1; PPAR[gamma], peroxisome proliferator-activated receptor-[gamma]; PEPCK-1, phosphoenolpyruvate carboxykinase; UCP-1, uncoupling protein-1; TBX1, T-box 1; TMEM26, transmembrane protein-26.
Gestational high fat diet programs hepatic phosphoenolpyruvate carboxykinase gene expression and histone modification in neonatal offspring rats.
(18) HWJMSCs population has been found to express the early hepatic markers, such as albumin, alpha-fetoprotein (AFP), cytokeratin-19 (CK-19), some mid- and late- hepatic markers, including CK18 and glucose 6-phosphatase (G6P), (19,20) as well as a low level of hematopoietic markers, such as c-kit and phosphoenolpyruvate carboxykinase (PEPCK).
Regarding energy gain, the shorter and more energetically economical way, probably selected by evolution, includes gluconeogenesis until phosphoenolpyruvate (step D-3 in Figure 1), degraded by the glycolytic pathway.
Previous studies demonstrated that fruits contained a variety of sugar- and acid-metabolizing enzymes including soluble acid invertase, sucrose synthase (SS) in the synthetic or cleavage direction, sucrose phosphate synthase (SPS) (HASHIZUME et al., 2003; ZHANG et al., 2012; YANG et al., 2013), citrate synthase (CS), cis-aconitase (ACO), malate dehydrogenase, isocitrate dehydrogenase (IDH) and phosphoenolpyruvate carboxylase (PEPC) (KUBO et al., 2002; LUO, 2003).
EXAMINING SUGAR TRANSPORT VIA THE PHOSPHOENOLPYRUVATE SUGAR
The reaction was started using 1.0 mM phosphoenolpyruvate. All assays were performed in duplicate at 25[degrees]C.
Pyruvate kinase, phosphoenolpyruvate carboxykinase, cytochrome c oxidase and catalase activities in cadmium exposed Perna viriais subject anoxic and aerobic conditions.
In the liver, only full-length adiponectin activated AMPK and reduced PEPCK (phosphoenolpyruvate carboxykinase) or G6Pase (glucose-6-phosphatase G6Pase) involved in gluconeogenesis and increased fatty-acid oxidation and decreased tissue TG content just as in skeletal muscle [12].
Cretin, "Sorghum phosphoenolpyruvate carboxylase gene family: structure, function and molecular evolution," Plant Molecular Biology, vol.

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