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Halogenation is a frequent modification of secondary metabolites and can play a significant role in establishing the bioactivity of a compound. Enzymatic halogenation through oxidative mechanisms is the most common route to these metabolites, though direct halogenation via halide anion incorporation is also known to proceed through both enzymatic and nonenzymatic pathways. In this article, we review the current state of knowledge regarding the mechanisms of these transformations, highlight applications of this knowledge, and propose future opportunities and challenges for the field. [Copyright &y& Elsevier]

The article presents a study which examines the biosynthesis of Allocoronamic Acyl Thioster by an Fe''-dependent Halogenase and a Cyclopropane-Forming Flavoprotein. It notes that the four-protein cassette KtzABCD was used as flavoprotein to test if it can yield cyclopropyl-containing amino acid. Moreover, it mentions that the KtzABCD was cloned in Escherichia coli expression. It also concludes that the KtzABCD proteins synthesis rendered alloCMA as product of the enzymes.