Which enzyme primarily catalyzes the conversion of aspartate to oxaloacetate?

The enzyme that primarily catalyzes the conversion of aspartate to oxaloacetate is an aminotransferase, specifically aspartate transaminase (AST), also known as serum glutamate-oxaloacetate transaminase (SGOT). Aminotransferases facilitate the transfer of an amino group from an amino acid to a keto acid, which is a key step in amino acid metabolism. In this case, aspartate donates its amino group to alpha-ketoglutarate, resulting in the production of oxaloacetate and glutamate.

This conversion is an important aspect of various metabolic pathways, including gluconeogenesis and the urea cycle, as it allows for the interconversion of amino acids and intermediates of the citric acid cycle. The functions of aminotransferases are crucial in maintaining amino acid profiles in the body and contributing to energy production through the metabolism of amino acids.

Other options, such as alanine transaminase, malate dehydrogenase, and lactate dehydrogenase, serve different roles in metabolic pathways. Alanine transaminase specifically transfers an amino group from alanine to alpha-ketoglutarate to form pyruvate and glutamate, while mal