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Oxaloacetic acid (also known as oxalacetic acid or OAA) is a crystalline organic compound with the chemical formula HO 2 CC(O)CH 2 CO 2 H. Oxaloacetic acid, in the form of its conjugate base oxaloacetate, is a metabolic intermediate in many processes that occur in animals.
Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.
pyruvic acid, pervasive intermediate in metabolism. oxaloacetic acid, a component of the Krebs cycle. [5] alpha-ketoglutaric acid, a 5-carbon ketoacid derived from glutamic acid. Alpha-ketoglutarate participates in cell signaling by functioning as a coenzyme. [6] It is commonly used in transamination reactions.
The reaction it catalyzes is: pyruvate + HCO − 3 + ATP → oxaloacetate + ADP + P. It is an important anaplerotic reaction that creates oxaloacetate from pyruvate. PC contains a biotin prosthetic group [1] and is typically localized to the mitochondria in eukaryotes with exceptions to some fungal species such as Aspergillus nidulans which have a cytosolic PC.
Citric acid cycle: Through a series of chemical reactions, stored energy is released through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins into adenosine triphosphate (ATP) and carbon dioxide. Fatty acid metabolism. Acetyl-CoA is produced by the breakdown of both carbohydrates (by glycolysis) and lipids (by β ...
CO 2 is initially fixed in the mesophyll cells in a reaction catalysed by the enzyme PEP carboxylase in which the three-carbon phosphoenolpyruvate (PEP) reacts with CO 2 to form the four-carbon oxaloacetic acid (OAA). OAA can then be reduced to malate or transaminated to aspartate.
Oxaloacetic acid + Glutamate ⇌ α-Ketoglutarate + Aspartate (catalyzed by aspartate aminotransferase) When skeletal muscle is at rest (ADP<ATP), the aspartate is no longer needed for the purine nucleotide cycle and can therefore be used with α-ketoglutarate to produce glutamate and oxaloacetic acid (the above reaction reversed).
Tissue transaminase activities can be investigated by incubating a homogenate with various amino/keto acid pairs. Transamination is demonstrated if the corresponding new amino acid and keto acid are formed, as revealed by paper chromatography. Reversibility is demonstrated by using the complementary keto/amino acid pair as starting reactants.