A Single Mutation Increases the Thermostability and Activity of Aspergillus terreus Amine Transaminase.

ABSTRACT: Enhancing the thermostability of (R)-selective amine transaminases (AT-ATA) will expand its application in the asymmetric synthesis of chiral amines. In this study, mutual information and coevolution networks of ATAs were analyzed by the Mutual Information Server to Infer Coevolution (MISTIC). Subsequently, the amino acids most likely to influence the stability and function of the protein were investigated by alanine scanning and saturation mutagenesis. Four stabilized mutants (L118T, L118A, L118I, and L118V) were successfully obtained. The best mutant, L118T, exhibited an improved thermal stability with a 3.7-fold enhancement in its half-life (t_1/2) at 40 °C and a 5.3 °C increase in T₅₀¹⁰ compared to the values for the wild-type protei

SUBMITTER: Zhu WL 

PROVIDER: S-EPMC6479498 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature