Structure and evolution of alanine/serine decarboxylases and the engineering of theanine production.

ABSTRACT: Ethylamine (EA), the precursor of theanine biosynthesis, is synthesized from alanine decarboxylation by alanine decarboxylase (AlaDC) in tea plants. AlaDC evolves from serine decarboxylase (SerDC) through neofunctionalization and has lower catalytic activity. However, lacking structure information hinders the understanding of the evolution of substrate specificity and catalytic activity. In this study, we solved the X-ray crystal structures of AlaDC from Camellia sinensis (CsAlaDC) and SerDC from Arabidopsis thaliana (AtSerDC). Tyr³⁴¹ of AtSerDC or the corresponding Tyr³³⁶ of CsAlaDC is essential for their enzymatic activity. Tyr¹¹¹ of AtSerDC and the corresponding Phe¹⁰⁶ of CsAlaDC determine their substrate specificity. Both CsAlaD

SUBMITTER: Wang H 

PROVIDER: S-EPMC11407765 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature