Recombinant E.coli UGT72E2 protein

UGT72E2 is a member of the uridine diphosphate (UDP)-glycosyltransferase (UGT) family, a group of enzymes widely present in plants that catalyze the transfer of sugar moieties from activated donors to various acceptor molecules. Specifically, UGT72E2 is a plant-derived enzyme initially identified in *Arabidopsis thaliana* and has garnered interest for its role in modifying secondary metabolites, particularly phenylpropanoids. This class of compounds includes lignin precursors, flavonoids, and other phenolic derivatives, which are critical for plant structural integrity, stress responses, and interactions with the environment. UGT72E2 is known to glycosylate monolignols, such as coniferyl alcohol, influencing lignin biosynthesis and potentially altering cell wall composition. Such activity positions it as a target for bioengineering efforts to modify lignin content in crops, which could enhance biomass digestibility for biofuel production or improve agricultural sustainability.

Recombinant UGT72E2 protein is produced via heterologous expression systems, typically in *Escherichia coli* or yeast, to enable large-scale purification and functional characterization. The recombinant form retains the enzymatic activity of its native counterpart, allowing researchers to study substrate specificity, kinetic parameters, and structural features. Its crystal structure and catalytic mechanism have been partially elucidated, revealing conserved motifs critical for UDP-glucose binding and sugar transfer. Beyond lignin metabolism, UGT72E2's ability to glycosylate diverse substrates has implications for synthesizing bioactive glycosides in vitro, with potential applications in pharmaceuticals or nutraceuticals. Studies on UGT72E2 also contribute to understanding the evolutionary diversification of UGTs in tailoring plant specialized metabolism. Overall, this recombinant enzyme serves as a versatile tool for both fundamental research and biotechnological innovation.