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By St. John C.E.

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J. Schofield, Curr. Opin. Struct. , 2012, 22, 1–10. D. A. Proshlyakov and R. P. Hausinger, in Iron-containing Enzymes: Versatile Catalysts of Hydroxylation Reactions in Nature, ed. D. Kumar and S. P. , 2011, pp. 67–87. P. K. Grzyska, E. H. Appelman, R. P. Hausinger and D. A. Proshlyakov, Proc. Natl. Acad. Sci. , 2010, 107, 3982–3987. R. W. Welford, J. M. Kirkpatrick, L. A. McNeill, M. Puri, N. J. Oldham and C. J. , 2005, 579, 5170–5174. A. G. Prescott and M. D. Lloyd, Nat. Prod. , 2000, 17, 367–383.

15F), followed by dehydration using CurC, decarboxylation via a CurF domain, and mono- or dichloro l-2-aminobutyryl group in cytotrienin synthesis. (D) Trichlorination of leucine by BarB1 and BarB2 to make barbamide. (E) CmaB- or KtzD-dependent hydroxylation of isoleucyl groups for subsequent cyclization to coronamic acids. (F) CurA chlorination of a 3-hydroxy-3-methylglutaryl group as part of curacin A synthesis. (G) KthP halogenation of a piperazyl group during formation of kutznerides. (H) Hydroxylation of a histidyl group during synthesis of bleomycin, tallysomycin and zorbamycin (yellow highlight is a single bond in the case of zorbamycin).

The gene encoding PhnY was identified from a screen of ocean-derived metagenomic DNA that allowed E. coli cells deficient in C–P lyase (Δphn) to grow on 2-aminoethylphosphonic acid as the sole source of phosphorus. 12E)297 much like the reaction of TauD; however, the hydroxylated phosphonate is stable – unlike the hydroxylated sulfonate. 300 Another enzyme participating in the synthesis of dehydrophos by S. 7 2OG-Dependent  Oxygenases Involved in Antibiotic Biosynthesis Several 2OG-dependent oxygenases described earlier function in the synthesis of antibiotics, but their actions typically involve provision of small precursor molecules that become incorporated into the final compounds.

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