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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes Binuraj R. K. Menon , Jonathan Latham , Mark S. Dunstan , Eileen Brandenburger , Ulrike Klemstein , David Leys , Chinnan Karthikeyan , Michael F. Greaney , Sarah A. Shepherd , Jason Micklefield Org. Biomol. Chem. 14, 9354 - 9361 DOI: 10.1039/C6OB01861K Diamond Proposal Number(s): [8997] Open Access Show Abstract ▼ Abstract: Flavin-dependent halogenase (Fl-Hal) enzymes have been shown to halogenate a range of synthetic as well as natural aromatic compounds. The exquisite regioselectively of Fl-Hal enzymes can provide halogenated building blocks which are inaccessible using standard halogenation chemistries. Consequently, Fl-Hal are potentially useful biocatalysts for the chemoenzymatic synthesis of pharmaceuticals and other valuable products, which are derived from haloaromatic precursors. However, the application of Fl-Hal enzymes, in vitro, has been hampered by their poor catalytic activity and lack of stability. To overcome these issues, we identified a thermophilic tryptophan halogenase (Th-Hal), which has significantly improved catalytic activity and stability, compared with other Fl-Hal characterised to date. When used in combination with a thermostable flavin reductase, Th-Hal can efficiently halogenate a number of aromatic substrates. X-ray crystal structures of Th-Hal, and the reductase partner (Th-Fre), provide insights into the factors that contribute to enzyme stability, which could guide the discovery and engineering of more robust and productive halogenase biocatalysts.	Sep 2016

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I04-Macromolecular Crystallography

Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes

Binuraj R. K. Menon , Jonathan Latham , Mark S. Dunstan , Eileen Brandenburger , Ulrike Klemstein , David Leys , Chinnan Karthikeyan , Michael F. Greaney , Sarah A. Shepherd , Jason Micklefield

Org. Biomol. Chem. 14, 9354 - 9361

DOI: 10.1039/C6OB01861K

Diamond Proposal Number(s): [8997]