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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.
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.
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.
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.
Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase (GOT, SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1) that was first described by Arthur Karmen and colleagues in 1954.
Properties section says "The enol forms of oxaloacetic acid are particularly stable, so much so that the two tautomer have different melting points (152 °C for the cis isoform and 184 °C for the trans isoform)." Does this mean the structure shown is the keto form and that there are two enol (iso)forms ?
Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology. [6]
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).