Aminomutation catalyzed by CO2 self-sufficient cascade amino acid decarboxylases
Song, Z.; Li, Y.; Li, Y.; Cui, X.; Zhong, J.; Zhang, Y.-H. P. J.
Show abstract
Molecular editing of an amino group from -position of amino acids to its {beta}-position is of scientific interest and could be economically appealing. Here we reconstructed an in vitro biotransformation pathway composed of two cascade decarboxylases, i.e., aspartate {beta}-decarboxylase and aspartate -decarboxylase, and implemented molecular editing to change -alanine into {beta}-alanine. In it, we discovered a new reaction of aspartate {beta}-decarboxylase that can fix CO2 directly. 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 -amino acids.
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