Nature Sub-Journal: Defines the structure of the substrate-bound iron 2-oxoglutarate (Fe/2OG) enzyme

Researchers from North Carolina State University and the University of Texas at Austin defined the structure of the substrate-bound iron 2-oxoglutarate (Fe/2OG) enzyme to explore whether these enzymes could be used to create a wide array of molecules

The Fe/2OG family of enzymes is naturally occurring – from bacteria to plants and animals, they are everywhere

Wei-chen Chang, an associate professor of chemistry at North Carolina State University and one of the corresponding authors of a paper describing the work, said: "The final goal is to understand how enzymes in this family produce specific molecules so that we can potentially take advantage of natural processes

By focusing on how the enzyme binds to a particular substrate, researchers can determine which other substrates the enzyme can use, a more efficient way to identify potential reactions and products than experiments

The research team mainly studied two Fe/2OG enzymes, PvcB and PlsnB, and compared their structure and products

"Typically, fe/2OG enzymes catalyze or produce new products in such a way that the enzyme binds to the substrate, introduces an oxygen atom from the molecule oxygen (O2) into the substrate, and oxygen drives the reaction

"But for these enzymes, the conversion or reaction is not driven by hydroxylation, but by a reaction cation that triggers subsequent desaturation, introducing new bonds

The two Fe/2OG enzymes studied (PIsnB and PvcB) use completely different desaturations to produce different products from the same substrate

"Now that we know how these enzymes catalyze conversion and have found binding sites, we have a basis

The study was published in the journal Nature Communications and was supported

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