The introduction of a stereogenic centre to produce an "unnatural" amino acid can be accomplished in a variety of ways ranging from asymmetric hydrogenation to biotransformations based on transaminase enzymes. Our transaminase approach can be used to access a wide variety of L- and D-amino acids from an alpha-keto acid substrate. It is run as a whole cell biotransformation and uses coupled enzyme systems. In addition, formation of amino acids with small side chains, such as 2-aminobutyrate, can cause significant isolation problems due to the presence of small amounts of other amino acids, such as alanine. The improvements we have made to the approach are illustrated with 2-aminobutyrate as the example. Aspartic acid is used as the amino donor and gives rise to the formation of pyruvate, a substrate for the transaminase enzymes. We have now developed an alternative approach where lysine is used as the amino donor to allow formation of a cyclic by-product that is removed from the equilibrium.