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Human Erythroenzymopathies Of The Anaerobic Embden-Meyerhof Glycolytic And Associated Pathways
Published in Ronald L. Nagel, Genetically Abnormal Red Cells, 2019
Ernst R. Jaffé, William N. Valentine
Phosphoglycerate kinase catalyzes the reversible interconversion of 3-phosphoglycerate (3-PG) and 1,3-diphosphoglycerate (1, 3-DPG), the first ATP-generating step in glycolysis:
Phosphonic Acids And Phosphonates As Antimetabolites
Published in Richard L. Hilderbrand, The Role of Phosphonates in Living Systems, 2018
A number of synthetic efforts have been directed at finding phosphonate analogues of the phosphoglycerates. The first of these107 was concerned with the generation of a nonisosteric system related to 2,3-diphosphoglycerate, that is (Structure 16). Pfeiffer et al.108 have reported the syntheses of both the isosteric (Structure 17) and the nonisosteric (Structure 18) species related to 3-phosphoglycerate. Two other routes were later reported for (17),81,104 one of these proceeding through oxidation of (15).104 Another route,7 basically a modification of that first used,108 allows incorporation of a radioactive label via intermediate cyanohydrin formation using 14-C cyanide.
Anaerobic endurance: the speed endurance sports
Published in Nick Draper, Helen Marshall, Exercise Physiology, 2014
It is at step seven that the first synthesis of ATP occurs within the glycolytic pathway. Phosphoglycerate kinase catalyses the phosphorylation of ADP through the energy released by the removal of the phosphate group from carbon 1 from each 1, 3-bisphosphoglycerate molecule. This results in the creation of an ATP from each of the trioses. The energy balance for glycolysis after step seven is, therefore, a net ATP gain of 0 (two ATP consumed during steps one and three; two ATP produced at step 7). In step eight of glycolysis the remaining phosphate in 3-phosphoglycerate (the product of step seven) is transferred, in a reaction catalysed by phosphoglycerate mutase, from carbon 3 to carbon 2. The product of this reaction is named, not surprisingly, 2-phosphoglycerate.
Interaction of low frequency external electric fields and pancreatic β-cell: a mathematical modeling approach to identify the influence of excitation parameters
Published in International Journal of Radiation Biology, 2018
Sajjad Farashi, Pezhman Sasanpour, Hashem Rafii-Tabar
The glycolysis pathway contains a series of reactions for converting glucose into pyruvate and ATP. In the first step glucose is phosphorylated and converted to glucose-6-phosphate (G6P) which will be isomerised to the fructose-6-phosphate (F6P). The further phosphorylation of F6P by phosphofructokinase-1 enzyme produces fructose 1,6-bisphosphate, which in the next step will be cleaved into glyceraldehyde-3-phosphate (G3P) and dihydroxy acetone phosphate (DHAP) using aldolase enzyme. The DHAP is converted to further G3P by triose-phosphate isomerase. This phase, the procedure is preparatory phase and requires energy consumption. In the next step G3P oxidized to 1,3-bisphosphoglycerate incorporating glyceraldehyde 3-phosphate dehydrogenase. A large amount of energy during the oxidation of an aldehyde group will be released. In this step Nicotinamide adenine dinucleotide (NAD+) will be reduced to NADH, the reduced form of NAD+. The enzyme phosphoglycerate kinase transfers the phosphoryl group of 1,3-bisphosphoglycerate to ADP and producing ATP and 3-phosphoglycerate which the latter will be isomerized to 2-phosphoglycerate using Phosphoglycerate mutase. Using the enzyme enolase, 2-phosphoglycerate will be converted to phosphoenolpyruvate (PEP). Finally, PEP will be converted to pyruvate by pyruvate kinase. In this step one extra ATP molecule will be produced. The glycolysis pathway is depicted in Figure 1.
Targeting endothelial cell metabolism in cancerous microenvironment: a new approach for anti-angiogenic therapy
Published in Drug Metabolism Reviews, 2022
Parisa Mohammadi, Reza Yarani, Azam Rahimpour, Fatemeh Ranjbarnejad, Joana Mendes Lopes de Melo, Kamran Mansouri
Glutamine-derived glutamate can be converted to the other amino acids such as serine which in turn can be interconverted with glycine. Serine and glycine metabolism are important because of their role in one-carbon metabolism (Rohlenova et al. 2018). One-carbon metabolism, mediated by the folate cofactor, is involved in redox homeostasis (via its role in glutathione synthesis) and nucleotide synthesis (purines and thymidine) (Vandekeere et al. 2018; Falkenberg et al. 2019). However, what distinguishes the serine metabolism in ECs is its role in the biosynthesis of heme which plays an important role in maintaining EC homeostasis and survival since it is present in important proteins, especially electron transport chain (ETC) complexes (Vandekeere et al. 2018). Serine can be either taken up or de novo synthesized by ECs. The three-step enzymatic reaction can convert glycolytic intermediate 3-phosphoglycerate (3PG) to serine, with the rate-controlling of phosphoglycerate dehydrogenase (PHGDH) enzyme (Rohlenova et al. 2018). Endothelial deletion of PHGDH causes impaired EC proliferation and survival, partly due to cellular heme depletion which in turn leads to defects in the electron transport chain, ROS accumulation and oxidative stress-induced death (Rohlenova et al. 2018; Vandekeere et al. 2018). Another important role of serine metabolism in ECs is its role in cytosine biosynthesis through heme production because heme is a prosthetic group for dihydroorotate dehydrogenase, a key enzyme of de novo cytosine biosynthesis pathway. This specific role of serine metabolism in ECs may be due to the compartmentalization of related enzymes in mitochondria, where part of heme biosynthesis occurs. However, further studies are required to prove this hypothesis (Vandekeere et al. 2018).
The possible role of methylglyoxal metabolism in cancer
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2021
Khalid O. Alfarouk, Saad S. Alqahtani, Saeed Alshahrani, Jakob Morgenstern, Claudiu T. Supuran, Stephan J. Reshkin
Phosphate acts as a competitive allosteric inhibitor of MGS. Some data concludes that the methylglyoxal pathway supports cells by phosphate and acts as a phosphate sensor18,19. ATP, 3-phosphoglycerate, and phosphoenolpyruvate inhibit MGS15,16. Therefore, it can be concluded that the MG pathway does not co-occur with the pay-off phase of the glycolysis pathway11. Other MGS inhibitors include: phosphoglycolohydroxamic acid20.