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Cellular respiration is the process of oxidizing biological fuels using an inorganic electron acceptor, such as oxygen, to drive production of adenosine triphosphate (ATP), which contains energy. Cellular respiration may be described as a set of metabolic reactions and processes that take place in the cells of organisms to convert chemical ...
One half of each dimer contains the ATP binding site whereas the other half the substrate (fructose-6-phosphate or (F6P)) binding site as well as a separate allosteric binding site. [6] Each subunit of the tetramer is 319 amino acids and consists of two domains: one that binds the substrate ATP, and the other that binds fructose-6-phosphate.
Pyruvate dehydrogenase deficiency (PDCD) can result from mutations in any of the enzymes or cofactors used to build the complex. Its primary clinical finding is lactic acidosis. [18] Such PDCD mutations, leading to subsequent deficiencies in NAD and FAD production, hinder oxidative phosphorylation processes that are key in aerobic respiration.
Glycolysis results in the breakdown of glucose, but several reactions in the glycolysis pathway are reversible and participate in the re-synthesis of glucose (gluconeogenesis). [9] Glycolysis was the first metabolic pathway discovered: As glucose enters a cell, it is immediately phosphorylated by ATP to glucose 6-phosphate in the irreversible ...
This specificity reflects the distinct metabolic roles of the respective coenzymes, and is the result of distinct sets of amino acid residues in the two types of coenzyme-binding pocket. For instance, in the active site of NADP-dependent enzymes, an ionic bond is formed between a basic amino acid side-chain and the acidic phosphate group of NADP +.
Cellular concentrations of free or non-covalently bound flavins in a variety of cultured mammalian cell lines were reported for FAD (2.2-17.0 amol/cell) and FMN (0.46-3.4 amol/cell). [18] FAD has a more positive reduction potential than NAD+ and is a very strong oxidizing agent.
Serine in an amino acid chain, before and after phosphorylation. In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes. [3] [4]
It can also be used to construct the amino acid alanine and can be converted into ethanol or lactic acid via fermentation. Pyruvic acid supplies energy to cells through the citric acid cycle (also known as the Krebs cycle) when oxygen is present (aerobic respiration), and alternatively ferments to produce lactate when oxygen is lacking. [4]