Fe(II)/α-ketoglutarate-dependent oxygenases offer a powerful and efficient solution for site-selective C-H hydroxylation—a transformation that’s often difficult and complex to achieve in synthetic chemistry.

KGOs have been shown to catalyze other reactions like demethylations and ring formations.

KGOs naturally occur intracellularly and play a crucial role in metabolic processes, functioning within cells to drive essential biochemical reactions. Natively active on metabolites, these enzymes enable precise and efficient modifications, offering valuable applications in both natural and industrial settings. As their outstanding feature KGOs are able to halogenate (Cl, Br, I).

Reactions on

metabolites

antibiotics

nucleotides

amino acids

nucleosides

Special feature

halogenation

Biocatalytic reactions involving unspecific oxygenases are scalable! The enzymes only require α-ketoglutarate as oxygen donor which can be continuously supplemented or regenerated during the reaction via an enzymatic side reaction.

And we scale with you: We can supply our KGOs up to 100 kg scale.

Our KGOs offer unmatched stability and simplicity for your processes, requiring no heme cofactors for activity.
Unlike complex P450 enzymes, KGOs are streamlined and efficient, with no intricate domain structures that can lead to instability. This means they are robust under diverse conditions, making them ideal for reliable, scalable applications in even the most demanding workflows.