alanineglyoxylate

Alanineglyoxylate is not a standard chemical name, but is sometimes used informally to refer to the pair of substrates involved in the alanine–glyoxylate transamination reaction. The key enzyme is alanine-glyoxylate aminotransferase (AGT), which catalyzes the transfer of an amino group from alanine to glyoxylate, producing glycine and pyruvate.

The reaction can be written as: alanine + glyoxylate ↔ pyruvate + glycine. The process is a pyridoxal phosphate (PLP)–dependent transamination that helps connect amino acid metabolism with glycolytic intermediates. This detoxification pathway is important because glyoxylate is reactive and potentially toxic; converting it to the nonreactive amino acid glycine and generating pyruvate helps maintain cellular balance.

Physiological relevance varies by organism but is especially noted in humans, plants, and microbes. In humans, alanine-glyoxylate aminotransferase is primarily associated with peroxisomal enzymes in liver tissues. Genetic defects in AGT can lead to primary hyperoxaluria type 1, a disorder characterized by oxalate overproduction, kidney stone formation, and renal damage. Treatments focus on reducing oxalate burden and may include pyridoxine supplementation in responsive variants, hydration strategies, and, in severe cases, liver transplantation or gene therapy approaches under investigation.

In summary, alanineglyoxylate commonly refers to the substrate pair for the AGT-catalyzed transamination, a pathway that links amino acid metabolism to glyoxylate detoxification, with clinical significance in human metabolic disease.