6nie
From Proteopedia
BesD with Fe(II), chloride, and alpha-ketoglutarate
Structural highlights
Function[BESD_STREN] Involved in the biosynthesis of terminal alkyne-containing amino acids produced as antibiotics by S.cattleya. Catalyzes the chlorination of L-lysine at the C4 position, leading to the production of 4-chloro-L-lysine.[1] Publication Abstract from PubMedThe integration of synthetic and biological catalysis enables new approaches to the synthesis of small molecules by combining the high selectivity of enzymes with the reaction diversity offered by synthetic chemistry. While organohalogens are valued for their bioactivity and utility as synthetic building blocks, only a handful of enzymes that carry out the regioselective halogenation of unactivated [Formula: see text] bonds have previously been identified. In this context, we report the structural characterization of BesD, a recently discovered radical halogenase from the Fe(II)/alpha-ketogluturate-dependent family that chlorinates the free amino acid lysine. We also identify and characterize additional halogenases that produce mono- and dichlorinated, as well as brominated and azidated, amino acids. The substrate selectivity of this new family of radical halogenases takes advantage of the central role of amino acids in metabolism and enables engineering of biosynthetic pathways to afford a wide variety of compound classes, including heterocycles, diamines, alpha-keto acids and peptides. A family of radical halogenases for the engineering of amino-acid-based products.,Neugebauer ME, Sumida KH, Pelton JG, McMurry JL, Marchand JA, Chang MCY Nat Chem Biol. 2019 Oct;15(10):1009-1016. doi: 10.1038/s41589-019-0355-x. Epub, 2019 Sep 23. PMID:31548692[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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