Aspartate aminotransferases

Aspartate aminotransferases (EC 2.6.1.1) are enzymes that catalyse the transfer of amino groups, converting L-aspartic acid and 2-oxoglutarate into L-glutamate and oxaloacetate. They also act on L-tyrosine, L-phenylalanine, and L-tryptophan, giving them a broad role in amino acid metabolism. In food biochemistry these transaminases matter for flavour development during fermentation and ripening: amino acid conversions generate keto acids and other intermediates that become precursors of aroma compounds in cheese, wine, beer, and cured meats. They are also clinical markers in medicine, but in food science their interest lies in how controlled enzyme activity shapes the flavour complexity of fermented products.