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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.
Oxalate also forms coordination compounds where it is sometimes abbreviated as ox. It is commonly encountered as a bidentate ligand. When the oxalate chelates to a single metal center, it always adopts the planar conformation. As a bidentate ligand, it forms a 5-membered MC 2 O 2 ring. An illustrative complex is potassium ferrioxalate, K 3 [Fe ...
In enzymology, an oxaloacetase (EC 3.7.1.1) is an enzyme that catalyzes the chemical reaction: [1]. oxaloacetate + H 2 O oxalate + acetate. Thus, the two substrates of this enzyme are oxaloacetate and H 2 O, whereas its two products are oxalate and acetate.
At least two pathways exist for the enzyme-mediated formation of oxalate. In one pathway, oxaloacetate, a component of the Krebs citric acid cycle, is hydrolyzed to oxalate and acetic acid by the enzyme oxaloacetase: [36] [O 2 CC(O)CH 2 CO 2] 2− + H 2 O → C 2 O 2− 4 + CH 3 CO − 2 + H +
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.
Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD + to NADH. This reaction is part of many metabolic pathways, including the citric acid cycle.
Both malate and oxaloacetate can be converted into phosphoenolpyruvate, which is the product of phosphoenolpyruvate carboxykinase, the first enzyme in gluconeogenesis. The net result of the glyoxylate cycle is therefore the production of glucose from fatty acids.
Oxamate also plays inhibiting roles with oxaloacetate, an important intermediate for the citric acid cycle. Oxamate competes and binds to the carboxyl transferase domain active site, and reverses the reaction of oxalaoacetate decarboxylation by pyruvate carboxylase .