Cheanyeh Cheng - Enzyme-Based Organic Synthesis

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The use of transaminases, or aminotransferases, as a catalyst for the organic synthesis of chiral amino compounds from the corresponding keto acids, ketones, or aldehydes has been known a very powerful method since last decade. Their immense potential in the industrial applications can be due to not only their concise reaction, excellent enantioselectivity and environmental friendliness but also their easy combination with other existing enzymatic or chemical methods. The catalytic process for the transfer of an amino group from the amino donor to the amino group acceptor in general involves two steps: (i) the release of an amino group from the amino donor (deamination) and (ii) the addition of the amino group to the amino acceptor (amination). For this kind of transamination reaction, a vitamin B 6‐based pyridoxal 5′‐phosphate (PLP) is required as a cofactor for transaminase to act as an intermediate amine acceptor and electron sink. Since the cofactor releases the amino group and restores its initial state at the end of the transamination, there is no need to carry out additional cofactor regeneration for the enzyme [1, 2]. However, the use of transaminases in organic synthesis still suffers from the problem of unfavorable reversible reaction equilibrium. This problem is especially serious when an amino acid is used as amino donor in the asymmetric synthesis of amines.