Transaminase enzyme | Johnson Matthey
Transaminase enzyme technology
Johnson Matthey’s transaminase enzymes can be used to produce aromatic and aliphatic primary amines through the formal reductive amination of ketones, yielding the corresponding (R)- or (S)-amines.
A transaminase enzyme requires an amino donor and PLP as cofactor for catalysing the reaction. Reactions can be run with an amine donor as simple as isopropylamine, where the equilibrium can be driven under reduced pressure, or using multienzymatic systems employing alanine as an amino donor. Both strategies have their specific advantages and can be chosen based on the requirements of the biocatalytic process.
Advantages of using transaminase enzymes:
- TAs enzymes exhibit high chemo-, regio- and enantioselectivity, producing chiral amines with high enantiomeric excess in aqueous media, under mild temperature and pressure conditions.
- Uses pyridoxal phosphate (PLP) as a cofactor, which is relatively stable and easier to handle compared to the nicotinamide cofactors (NADH or NADPH). This can simplify the reaction setup and reduce costs.
- A transaminase enzyme typically has a broader substrate scope compared to amine dehydrogenases and imine reductases.
- Tuneable activity and selectivity by using enzyme engineering.
