bioRxiv Science⌕ Search

Biology subjects

Zhang, Y.-H. P. J.

Publications and source records attributed to Zhang, Y.-H. P. J..

2 recordsLinked to original sources

Aminomutation catalyzed by CO2 self-sufficient cascade amino acid decarboxylases

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.

biochemistry↗

Designing a Minimal Artificial Glycolytic Pathway

The canonical glycolysis generates two molecules of acetyl-coenzyme A (acetyl-CoA) from one glucose through eleven cascade biochemical reactions. Here, we designed and constructed a Minimal Artificial Glycolytic (MAG) pathway consisting of only three types of biochemical reactions, with phosphoketolase as the core, combined with phosphatase and isomerase as auxiliary enzymes. It could theoretically achieve a 100% carbon yield to acetyl-CoA from any monosaccharide by integrating one-carbon condensation reaction. We tested the MAG pathway in vitro and in vivo, demonstrating the catabolism of typical C1-C6 carbohydrates to acetyl-CoA with yields from 82% to 95%. This novel glycolytic pathway provides a promising route for biomanufacturing with stoichiometric productivity from multiple carbon sources in the future.

synthetic biology↗