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Instruments / Technical Area	Publication Details	Published	Actions
I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	Discovery of a fungal copper radical oxidase with high catalytic efficiency towards 5-hydroxymethylfurfural and benzyl alcohols for bioprocessing Yann Mathieu , Wendy A. Offen , Stephanie M. Forget , Luisa Ciano , Alexander Holm Viborg , Elena Blagova , Bernard Henrissat , Paul H. Walton , Gideon J. Davies , Harry Brumer Acs Catalysis DOI: 10.1021/acscatal.9b04727 Diamond Proposal Number(s): [13587, 18598] Show Abstract ▼ Abstract: Alternatives to petroleum-based chemicals are highly sought-after for on-going efforts to reduce the damaging effects of human activity on the environment. Copper radical oxidases from Auxiliary Activity Family 5/Subfamily 2 (AA5_2) are attractive biocatalysts because they oxidize primary alcohols in a chemo-selective manner without complex organic cofactors. However, despite numerous studies on canonical galactose oxidases (GalOx, EC 1.1.3.9) and engineered variants, and the recent discovery of a Colletotrichum graminicola copper radical alcohol oxidase (AlcOx, EC 1.1.3.13), the catalytic potentials of very few AA5_2 members have been characterized. Guided by sequence similarity network and phylogenetic analyses, in this study we targeted a distinct paralog from the fungus C. graminicola as a representative member of a large uncharacterized subgroup of AA5_2. Through recombinant production and detailed kinetic analysis, we demonstrated that this enzyme is weakly active towards carbohydrates, but efficiently catalyzes the oxidation of aryl alcohols to the corresponding aldehydes. As such, this represents the initial characterization of a demonstrable aryl alcohol oxidase (AAO, EC 1.1.3.7) in AA5, an activity which is classically associated with flavin-dependent glucose-methanol-choline (GMC) oxidoreductases of Auxiliary Activity Family 3 (AA3). X-ray crystallography revealed a distinct multidomain architecture comprising an N-terminal PAN domain abutting a canonical AA5 seven-bladed propeller catalytic domain. Of direct relevance to biomass processing, the wild-type enzyme exhibits the highest activity on the primary alcohol of 5-hydroxymethylfurfural (HMF), a product of significant interest in the lignocellulosic bio-refinery concept. Thus, the chemoselective oxidation of HMF to 2,5-diformylfuran (DFF) by C. graminicola aryl alcohol oxidase (CgrAAO) from AA5 provides a fundamental building block for chemistry via biotechnology.	Feb 2020
I02-Macromolecular Crystallography	Structural and functional characterization of three novel fungal amylases with enhanced stability and pH tolerance Christian Roth , Olga V. Moroz , Johan P. Turkenburg , Elena Blagova , Jitka Waterman , Antonio Ariza , Li Ming , Sun Tianqi , Carsten Andersen , Gideon J. Davies , Keith S. Wilson International Journal Of Molecular Sciences 20 DOI: 10.3390/ijms20194902 Diamond Proposal Number(s): [1221, 9948] Open Access Show Abstract ▼ Abstract: Amylases are probably the best studied glycoside hydrolases and have a huge biotechnological value for industrial processes on starch. Multiple amylases from fungi and microbes are currently in use. Whereas bacterial amylases are well suited for many industrial processes due to their high stability, fungal amylases are recognized as safe and are preferred in the food industry, although they lack the pH tolerance and stability of their bacterial counterparts. Here, we describe three amylases, two of which have a broad pH spectrum extending to pH 8 and higher stability well suited for a broad set of industrial applications. These enzymes have the characteristic GH13 α-amylase fold with a central (β/α)8-domain, an insertion domain with the canonical calcium binding site and a C-terminal β-sandwich domain. The active site was identified based on the binding of the inhibitor acarbose in form of a transglycosylation product, in the amylases from Thamnidium elegans and Cordyceps farinosa. The three amylases have shortened loops flanking the nonreducing end of the substrate binding cleft, creating a more open crevice. Moreover, a potential novel binding site in the C-terminal domain of the Cordyceps enzyme was identified, which might be part of a starch interaction site. In addition, Cordyceps farinosa amylase presented a successful example of using the microseed matrix screening technique to significantly speed-up crystallization.	Oct 2019

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