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The following chart shows the solubility of various ionic compounds in water at 1 atm pressure and room temperature (approx. 25 °C, 298.15 K). "Soluble" means the ionic compound doesn't precipitate, while "slightly soluble" and "insoluble" mean that a solid will precipitate; "slightly soluble" compounds like calcium sulfate may require heat to precipitate.
Sodium pyruvate is a salt of the conjugate anion form of pyruvic acid, known as pyruvate. It is commonly added to cell culture media as an additional source of energy, but may also have protective effects against hydrogen peroxide. This was reported by Giandomenico et al. [1] and has been confirmed by several independent groups.
In enzymology, a pyruvate synthase (EC 1.2.7.1) is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR). The relevant equilibrium catalysed by PFOR is: pyruvate + CoA + oxidized ferredoxin acetyl-CoA + CO 2 + reduced ferredoxin
Pyruvate, the conjugate base, CH 3 COCOO −, is an intermediate in several metabolic pathways throughout the cell. Pyruvic acid can be made from glucose through glycolysis , converted back to carbohydrates (such as glucose) via gluconeogenesis , or converted to fatty acids through a reaction with acetyl-CoA . [ 3 ]
In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction pyruvate + phosphate + O 2 ⇌ {\displaystyle \rightleftharpoons } acetyl phosphate + CO 2 + H 2 O 2 The 3 substrates of this enzyme are pyruvate , phosphate , and O 2 , whereas its 3 products are acetyl phosphate , CO 2 , and H 2 O 2 .
Pyruvate, water dikinase in Neisseria meningitidis is 794 amino acids in length and has two active sites: one at at position 422 and position 752. [3] In Pyrococcus furiosus, the pyruvate, water dikinase enzyme has a subunit molecular mass of 92 kDa, and each subunit contains one calcium and one phosphorus atom. [1]
Two Cys-221 (more than 20 Ångstroms away from each site) and His-92 trigger a conformational change, which inhibits or activates the enzyme depending on the substrate availability. If the substrate bound in the active site is pyruvate, the enzyme is activated by a conformational change in this regulatory site. [6]
The oxidative conversion of pyruvate into acetyl-CoA is referred to as the pyruvate dehydrogenase reaction. It is catalyzed by the pyruvate dehydrogenase complex. Other conversions between pyruvate and acetyl-CoA are possible. For example, pyruvate formate lyase disproportionates pyruvate into acetyl-CoA and formic acid. β-Oxidation of fatty acids