Chiral amines are important structural features of many
pharmaceutical
and agrochemical compounds; accordingly, numerous synthetic methods
have been developed to enable the installation of this functional
group. Of the many available methods, amine transaminases have gained
attention as stereoselective, efficient, and green catalysts. As selection
of transaminases for a given transformation most often cannot be performed
a priori, high-throughput screens are often used to identify a suitable
catalyst. One concern with high-throughput screening is that while
the transaminase may accept a particular substrate, it is possible
that the amine donor may not be compatible with the enzyme in question.
Here, we compare five common and diverse amine donors and identify
those that have the broadest compatibility with various amine transaminases.
Findings were used to further probe larger enzyme panels and reveal
preferences that engineered and wild-type enzymes have for differing
amine donors. In the process of exploring amine donors, we also define
a concise set of transaminases that catalyze the production of substituted
benzylamines.