ω-Transaminases have been increasingly used as efficient biocatalysts due to their ability to produce a wide range of optically pure amine compounds. Several approaches have been adopted, including screening, engineering, and development of new techniques in reaction systems for different aspects of the enzymes. This review summarizes the various methodologies and approaches adopted to produce enantiomerically pure amines and unnatural amino acids using ω-transaminases.
In the past decade it has become clear that many microbes harbor enzymes that employ an unusual flavin cofactor, the F420 deazaflavin cofactor. Herein we show that F420-dependent reductases (FDRs) can successfully perform enantio-, regio- and chemoselective ene-reductions. For the first time, we have demonstrated that F420H2-driven reductases can be used as biocatalysts for the reduction of α,β-unsaturated ketones and aldehydes with good conversions (>99%) and excellent regioselectivities and enantiomeric excesses (>99% ee). Noteworthily, FDRs typically display an opposite enantioselectivity when compared to the well established FMN-dependent Old Yellow Enzymes (OYEs).
In this study, we developed a one-pot one-step deracemization method for the production of various enantiomerically pure amines using two opposite enantioselective ω-TAs. Using this method, various aromatic amines were successfully converted to their (R)-forms (>99%) with good conversion.
A novel thermostable ω-transaminase from Thermomicrobium roseum showing broad substrate specificity and high enantioselectivity was identified, expressed and biochemically characterized and it could produce chiral amines at high temperature.
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