aminotransferaatioiden

Aminotransferaatioiden, also known as transamination, is a fundamental biochemical reaction catalyzed by enzymes called aminotransferases or transaminases. These enzymes are crucial for the metabolism of amino acids. In a typical aminotransference reaction, an amino group is transferred from an amino acid to a keto acid. This process involves the formation of a Schiff base intermediate with the enzyme's prosthetic group, pyridoxal phosphate (PLP).

The general reaction can be represented as: Amino acid 1 + Keto acid 2 <=> Keto acid 1 + Amino acid 2. This reversible reaction plays a vital role in both the synthesis and degradation of amino acids. For instance, transamination is essential for generating non-essential amino acids from their corresponding keto acid precursors. Conversely, it is a key step in the catabolism of amino acids, where the amino group is ultimately removed to be processed, often leading to the formation of urea.

Aminotransferases are found in virtually all organisms, from bacteria to humans, and are particularly abundant in the liver, kidneys, and muscles. Specific examples of important aminotransferases include aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Elevated levels of these enzymes in the blood serum are often indicative of tissue damage, particularly in the liver, making them common biomarkers in clinical diagnostics. Their role in interconverting amino acids and keto acids highlights their central position in nitrogen metabolism.