Enzymatic Halogenation of Tryptophan on a Gram Scale

Frese M, Sewald N (2015)
Angewandte Chemie International Edition 54(1): 298-301.

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Abstract
Halogenated arenes are important building blocks in medicinal and agrochemistry. Chemical electrophilic aromatic halogenation requires molecular halogen, whereas FAD-dependent halogenases form halogenated arenes with high regioselectivity while only halide salts and O-2 are required. This reaction proceeds at room temperature in aqueous media. However, enzymatic halogenation is considered inefficient, mainly because halogenases are not stable. Thus, the preparative application remained elusive. We were able to show that the long-term stability and, hence, the preparative efficiency of the tryptophan-7-halogenase RebH can be significantly improved by immobilization together with the other enzymes required for cofactor regeneration. We established a facile scalable method suitable for the halogenation of tryptophan and its derivatives on a gram scale using a solid, multifunctional, and recyclable biocatalyst; this immobilization strategy might also be applicable for other FAD-dependent halogenases.
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Frese M, Sewald N. Enzymatic Halogenation of Tryptophan on a Gram Scale. Angewandte Chemie International Edition. 2015;54(1):298-301.
Frese, M., & Sewald, N. (2015). Enzymatic Halogenation of Tryptophan on a Gram Scale. Angewandte Chemie International Edition, 54(1), 298-301. doi:10.1002/anie.201408561
Frese, M., and Sewald, N. (2015). Enzymatic Halogenation of Tryptophan on a Gram Scale. Angewandte Chemie International Edition 54, 298-301.
Frese, M., & Sewald, N., 2015. Enzymatic Halogenation of Tryptophan on a Gram Scale. Angewandte Chemie International Edition, 54(1), p 298-301.
M. Frese and N. Sewald, “Enzymatic Halogenation of Tryptophan on a Gram Scale”, Angewandte Chemie International Edition, vol. 54, 2015, pp. 298-301.
Frese, M., Sewald, N.: Enzymatic Halogenation of Tryptophan on a Gram Scale. Angewandte Chemie International Edition. 54, 298-301 (2015).
Frese, Marcel, and Sewald, Norbert. “Enzymatic Halogenation of Tryptophan on a Gram Scale”. Angewandte Chemie International Edition 54.1 (2015): 298-301.
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Francis D, Winn M, Latham J, Greaney MF, Micklefield J., Chembiochem 18(4), 2017
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Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse.
Agarwal V, Miles ZD, Winter JM, Eustáquio AS, El Gamal AA, Moore BS., Chem Rev 117(8), 2017
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Directed Evolution of RebH for Catalyst-Controlled Halogenation of Indole C-H Bonds.
Andorfer MC, Park HJ, Vergara-Coll J, Lewis JC., Chem Sci 7(6), 2016
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A High-Throughput Fluorescence Assay to Determine the Activity of Tryptophan Halogenases.
Schnepel C, Minges H, Frese M, Sewald N., Angew Chem Int Ed Engl 55(45), 2016
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Menon BR, Latham J, Dunstan MS, Brandenburger E, Klemstein U, Leys D, Karthikeyan C, Greaney MF, Shepherd SA, Micklefield J., Org Biomol Chem 14(39), 2016
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Payne JT, Poor CB, Lewis JC., Angew Chem Int Ed Engl 54(14), 2015
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Shepherd SA, Karthikeyan C, Latham J, Struck AW, Thompson ML, Menon BRK, Styles MQ, Levy C, Leys D, Micklefield J., Chem Sci 6(6), 2015
PMID: 29511510
Halogenase Engineering for the Generation of New Natural Product Analogues.
Brown S, O'Connor SE., Chembiochem 16(15), 2015
PMID: 26256103

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