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4 citations found for Stubbs, A.

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Crystal structures of the H. pylori methylthioadenosine nucleosidase (MTAN) HpyMqnB have been solved in native and complexed forms, shedding light on substrate binding and the reaction mechanism.

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The structure of a fungal α-L-arabinofuranosidase has been determined using sulfur SAD data collected in vacuo using beamline I23 at Diamond Light Source. Complexes with L-arabinose, an iminosugar and two covalent inhibitors confirm the identity of the catalytic nucleophile and provide a detailed map of enzyme–substrate interactions that are conserved between bacteria and fungi.

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The three-dimensional structure of a fungal arabinofuranosidase from CAZY family GH62 has been solved at 1.25 Å resolution in complex with the bespoke arabinofuranosidase inhibitor AraDNJ, shedding light on the activity of this catalyst in the enzymatic deconstruction of arabinoxylans.

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In the asymmetric unit of the title salt, C14H18N2O2+·2CF3O3S, the components are linked by two N—H...O and one C—H...O hydrogen bonds. The dipyridinium salt demonstrates a skew conformation based upon C—O—C—C torsion angles of 61.5 (3) and 15.1 (4)°. A C—O—C angle of 119.3 (2)° and C—O bond distances of 1.364 (3) and 1.389 (3) Å are consistent with other dipyridyl ethers. The planes of the pyridyl rings exhibit a twist angle of 67.89 (8)°. One of the tri­fluoro­methane­sulfonate ions shows disorder of the F atoms [in a 0.52 (7):0.48 (7) occupancy ratio] and an O atom [0.64 (8):0.36 (8) occupancy ratio]. In the crystal, the components are linked by C—H...O inter­actions, which form chains along [101].

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