Abstract
The carbon-carbon bond formation has always been one of the most important reactions in C1 resource utilization. Compared to traditional organic synthesis methods, biocatalytic C-C bond formation offers a green and potent alternative for C1 transformation. In recent years, with the development of synthetic biology, more and more carboxylases and C-C ligases have been mined and designed for the C1 transformation in vitro and C1 assimilation in vivo. This article presents an overview of C-C bond formation in biocatalytic C1 resource utilization is first provided. Sets of newly mined and designed carboxylases and ligases capable of catalyzing C-C bond formation for the transformation of CO2, formaldehyde, CO, and formate are then reviewed, and their catalytic mechanisms are discussed. Finally, the current advances and the future perspectives for the development of catalysts for C1 resource utilization are provided.
Highlights
It has been estimated that more than 35% of industrial chemicals will be produced by bio-manufacturing until 2030 [1]
In addition to Calvin–Benson–Bassham (CBB) cycle, there are three major pathways that operate in methanotrophs or methylotrophic yeast for assimilation of methane or methanol, which are first oxidized to formaldehyde, and is assimilated via the ribulose monophosphate (RuMP) cycle, serine cycle, or xylulose monophosphate pathway (XuMP) [3]
It has been shown thatcarboxylases involved in the secondary metabolism are generally reversible and promiscuous [17], several C-C ligases, such as aldolases and thiamine diphosphate (ThDP)-dependent enzymes [18], can receive formaldehyde as a receptor
Summary
It has been estimated that more than 35% of industrial chemicals will be produced by bio-manufacturing until 2030 [1]. Carboxylases and C-C ligases from naturally occurring C1 assimilation pathways are highly specialized, and restricted their use for the C1 biotransformation in vitro. It has been shown that (de)carboxylases involved in the secondary metabolism are generally reversible and promiscuous [17], several C-C ligases, such as aldolases and thiamine diphosphate (ThDP)-dependent enzymes [18], can receive formaldehyde as a receptor. These newly mined (de)carboxylases and C-C ligases greatly expand the scope of C1 resource utilization in vitro.
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