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    Flavin-dependent dehalogenases use flavin as a cofactor to catalyze carbon-halogen (C-X) bond cleavage from halogenated compounds which are mainly distributed as persistent environmental pollutants via anthropogenic activities. The accumulation of these compounds results in adaptation of bacteria to evolve metabolic pathways to metabolize the agents for four decades. Flavin-dependent enzymes have been evolved to catalyze dehalogenation in addition to its basal function. Apart from bacterial biodegradation, flavin-dependent dehalogenases also naturally appear in cellular metabolisms of higher organisms such as in human thyroid hormone. Although the removal of halogen is required in various applications, the usage of dehalogenases remains limited. In-depth understanding of their enzymatic mechanisms is useful for development of dehalogenases applications. Three main types of flavin-dependent dehalogenases are classified based on their reaction mechanisms reported to date: (1) flavin-dependent O2-utilizing dehalogenases; (2) flavin-dependent reductive dehalogenases; and (3) non-redox flavin-dependent dehalogenases. In this chapter, the catalytic properties, substrate scope, protein structures, enzymatic mechanisms, enzyme engineering, and also development of enzymes for novel applications are discussed. © 2020 Elsevier Inc. All rights reserved.


    Panu Pimviriyakul, Pimchai Chaiyen. Flavin-dependent dehalogenases. The Enzymes. 2020;47:365-397

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    PMID: 32951828

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