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α-Ketoglutarate is a component of the citric acid cycle, a cyclical metabolic pathway located in the mitochondria.This cycle supplies the energy that cells need by sequentially metabolizing (indicated by →) citrate through seven intermediate metabolites and then converting the eighth intermediate metabolite, oxaloacetate, back to citrate: [2]
Alanine can be synthesized from pyruvate and branched chain amino acids such as valine, leucine, and isoleucine. Alanine is produced by reductive amination of pyruvate, a two-step process. In the first step, α-ketoglutarate, ammonia and NADH are converted by glutamate dehydrogenase to glutamate, NAD + and water.
The alanine amino acid acts as a shuttle - it leaves the cell, entering the blood stream and traveling to hepatocytes in the liver, where essentially this entire process is reversed. Alanine undergoes a transamination reaction with free α-ketoglutarate to yield glutamate, which is then deaminated to form pyruvate and, ultimately, free ammonium ...
Alanine is produced by the transamination of one molecule of pyruvate using two alternate steps: 1) conversion of glutamate to α-ketoglutarate using a glutamate-alanine transaminase, and 2) conversion of valine to α-ketoisovalerate via Transaminase C. Not much is known about the regulation of alanine synthesis.
The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced through metabolism of fuels. Being a major degradative aminoacid pathway, lysine , proline and threonine are the only three amino acids that do not always undergo transamination and rather use respective dehydrogenase.
2. Glutamate can be excreted or can be further metabolized to α-ketoglutarate. For the conversion of glutamate to α-ketoglutarate three different reactions are possible: Catalyzing enzymes: glutamate dehydrogenase (GlDH), EC 1.4.1.2; glutamate pyruvate transaminase (GPT), also called alanine transaminase (ALT), EC 2.6.1.2
Alanine transaminase (ALT), also known as alanine aminotransferase (ALT or ALAT), formerly serum glutamate-pyruvate transaminase (GPT) or serum glutamic-pyruvic transaminase (SGPT), is a transaminase enzyme (EC 2.6.1.2) that was first characterized in the mid-1950s by Arthur Karmen and colleagues. [1]
Enzyme-bound pyridoxamine in turn reacts with pyruvate, oxaloacetate, or alpha-ketoglutarate, giving alanine, aspartic acid, or glutamic acid, respectively. Many transamination reactions occur in tissues, catalysed by transaminases specific for a particular amino/keto acid pair.
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