Beilstein J. Org. Chem.2024,20, 589–596, doi:10.3762/bjoc.20.51
the individual enzyme activities is lacking. In this study, we verify the activity for one enzyme in this pathway. We show that Hyg17 is a myo-inositoldehydrogenase that has a unique substrate scope when compared to other myo-inositol dehydrogenases. Furthermore, we analyze sequences from the protein
family containing Hyg17 and discuss genome mining strategies that target this protein family to identify biosynthetic clusters for natural product discovery.
Keywords: aminocyclitol; biosynthesis; hygromycin A; inositoldehydrogenase; myo-inositol; Introduction
Hygromycin A is a natural product that
annotations and in vivo studies [8]. However, validation by in vitro approaches or biochemical analysis of the individual enzymes is lacking. Here, we verify that Hyg17 is a myo-inositoldehydrogenase and show that it has a distinct substrate scope. In addition, we use sequence similarity networks to compare
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Graphical Abstract
Figure 1:
Proposed biosynthetic pathway for the aminocyclitol from hygromycin A.