The catabolism of amino acids to a wide range of volatile flavour compounds is amongst the most important series of reactions in the development of cheese flavour. The key enzymes in the degradation of free amino acids appear to be aminotransferases (ATases) from lactic acid bacteria. ATases are intracellular enzymes whose physiological role is in the interconversion of amino acids. These enzymes require pyridoxal-5'-phosphate (PLP) as a co-factor and catalyse the transfer of the amino group of a donor amino acid (leucine in the example below) to an acceptor molecule, usually alpha-ketoglutarate, forming a product alpha-keto acid corresponding to the donor amino acid (alpha-ketoisocaproate in this example) and glutamic acid. The catalytic mechanism of ATases involves two steps: firstly, the amino group of the donor amino acid is transferred to PLP to yield the product alpha-keto acid and enzyme-bound pyridoxamine-5'-phosphate. Secondly, the amino group is transferred from pyridoxamine-5'-phosphate to the acceptor alpha-keto acid, thus regenerating PLP. The alpha-keto acids formed by ATase action are unstable and degrade to a wide range of compounds via enzymatic and/or chemical pathways.