Johan P. Turkenburg

TL;DR: In inhibition and structural studies on the deoxyuridine nucleotidohydrolase from the malaria parasite Plasmodium falciparum, the data show that PfdUTPase may be considered as an antimalarial drug target.

TL;DR: This study provides a template for the production of tailored industrial catalysts based on the structure of Bacillus subtilis endo-arabinanase 43A and a rational design approach that led to the conversion of the Cellvibrio enzyme from an exo to an endo mode of action.

TL;DR: The structure of an active site mutant in complex with the reaction product, acetate, reveals details of the putative oxyanion binding site, and suggests that substrates bind predominantly through non-specific contacts with protein hydrophobic residues.

TL;DR: Of the mutations that confer the ability to catalyse the oxidation of secondary amines in MAO-N-D3, Asn336Ser reduces steric bulk behind Trp430 of the aromatic cage and Ile246Met confers greater flexibility within the substrate binding site, and two additional mutations appear to influence the active-site environment remotely through changes in tertiary structure that perturb the side chain of Phe382.

TL;DR: It is shown that family GH97 has diverged significantly, as it contains both inverting and retaining α-glycosidases, and 1H NMR analysis shows an inversion mechanism for BtGH97a, whereas another GH97 enzyme from B. thetaiotaomicron, Bt GH97b, functions as a retaining β-galactosidase.