Protein Engineering for Enhanced Acyltransferase Activity, Substrate
Scope, and Selectivity of the Mycobacterium smegmatis Acyltransferase MsAcT
Posted on 2020-06-26 - 12:37
The
highly efficient and versatile acyltransferase MsAcT from Mycobacterium smegmatis catalyzes aqueous acyl transfer
reactions, enabling applications in environmentally friendly processes
and enzyme cascades. We rationally designed several variants with
up to 30-fold increased acyl transfer to hydrolysis ratios while mostly
retaining initial activity. Variants exhibiting broader acyl-donor
substrate scope and higher or inverted enantioselectivity were also
designed. Alterations of the catalytic His-Asp pair decreased the
activation of hydrolytic water, thereby increasing acyl transfer to
hydrolysis ratios. This study demonstrates that targeting the disruption
of water networks and manipulating the activation of nucleophiles
are promising strategies for engineering promiscuous acyltransferase
activities.
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Godehard, Simon
P.; Badenhorst, Christoffel P.
S.; Müller, Henrik; Bornscheuer, Uwe T. (2020). Protein Engineering for Enhanced Acyltransferase Activity, Substrate
Scope, and Selectivity of the Mycobacterium smegmatis Acyltransferase MsAcT. ACS Publications. Collection. https://doi.org/10.1021/acscatal.0c01767