Alder Ensberg Rose Hills
Characterization and Engineering of a Radical Amino Acid Hydroxylase
Fe(II)/ɑ-ketoglutarate (FeII/αKG) dependent halogenases are a class of enzymes that stand out in their ability to add halogens to otherwise hard-to-distinguish C-H bonds in organic compounds. This provides potential for widespread utility in many contexts, such as agriculture, medicine, and industry. However, these enzymes tend to act on only a few specific amino acids, limiting their utility. The Chang Group has previously identified a hydroxylase from the bacteria Streptomyces bunogensis known as MN3 and shown it to accept the amino acid arginine, setting it apart from other enzymes in the family which only accept lysine. I aim to gain and document a more thorough understanding of the interaction between arginine and MN3; to test the substrate scope of MN3; to engineer the reaction pathway of MN3 in order to allow it to halogenate arginine and possibly other substrates; and to solve the X-ray crystal structure of MN3 in order to gain a full understanding of its divergence from other enzymes in its family.