Aminomutation catalyzed by CO2self-sufficient cascade amino acid decarboxylases

Abstract

AbstractMolecular editing of an amino group from α-position of amino acids to its β-position is of scientific interest and could be economically appealing. Here we reconstructed anin vitrobiotransformation pathway composed of two cascade decarboxylases, i.e., aspartate β-decarboxylase and aspartate α-decarboxylase, and implemented molecular editing to change α-alanine into β-alanine. In it, we discovered a new reaction of aspartate β-decarboxylase that can fix CO2directly. This cascade enzymatic pathway enabled an aminomutation reaction with 100% carbon atom economy. This work presented the first CO2-fixing biological reaction catalyzed by the amino acid decarboxylases and demonstrated a new means for the molecular editing of α-amino acids.