Aminomutation catalyzed by CO2 self-sufficient cascade amino acid decarboxylases

Song, Z.; Li, Y.; Cui, X.; Zhong, J.; Zhang, Y.-H. P. J.

doi:10.1101/2023.08.12.552924

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bioRxiv · 10.1101/2023.08.12.552924

Aminomutation catalyzed by CO2 self-sufficient cascade amino acid decarboxylases

Song, Z.·Li, Y.·Cui, X.·Zhong, J.·Zhang, Y.-H. P. J.

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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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Song, Z., Li, Y., Cui, X., Zhong, J., Zhang, Y.-H. P. J.. 2023-08-12. Aminomutation catalyzed by CO2 self-sufficient cascade amino acid decarboxylases. https://doi.org/10.1101/2023.08.12.552924

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