J
Johan P. Turkenburg
Researcher at University of York
Publications - 126
Citations - 8279
Johan P. Turkenburg is an academic researcher from University of York. The author has contributed to research in topics: Hydrolase & Glycoside hydrolase. The author has an hindex of 41, co-authored 124 publications receiving 7492 citations. Previous affiliations of Johan P. Turkenburg include New York University & Newcastle University.
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Journal ArticleDOI
Evidence that Family 35 Carbohydrate Binding Modules Display Conserved Specificity But Divergent Function.
Cedric Montanier,Alicia Lammerts van Bueren,Claire Dumon,James E. Flint,Márcia A. S. Correia,José A. M. Prates,Susan J. Firbank,Richard J. Lewis,Gilles Grondin,Mariana Gabriela Ghinet,Tracey M. Gloster,Cécile Hervé,J. Paul Knox,Brian G. Talbot,Johan P. Turkenburg,Janne Kerovuo,Ryszard Brzezinski,Carlos M. G. A. Fontes,Gideon J. Davies,Alisdair B. Boraston,Harry J. Gilbert +20 more
TL;DR: The biological role of CBM35s is not dictated solely by their carbohydrate specificities but also by the context of their target ligands, which reveals an unusual mechanism for bacterial cell wall enzyme attachment.
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Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases.
Edward J. Taylor,Tracey M. Gloster,Johan P. Turkenburg,Florence Vincent,A. Marek Brzozowski,Claude Dupont,François Shareck,Maria S.J. Centeno,José A. M. Prates,Vladimír Puchart,Luís M. A. Ferreira,Carlos M. G. A. Fontes,Peter Biely,Gideon J. Davies +13 more
TL;DR: The structures of two distinct acetylxylan esterases, those from Streptomyces lividans and Clostridium thermocellum, in native and complex forms are reported, showing that the enzymes are sugar-specific and metal ion-dependent and possess a single metal center with a chemical preference for Co2+.
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Structure and molecular model refinement of Aspergillus oryzae (TAKA) α‐amylase: an application of the simulated‐annealing method
H. J. Swift,Leo Brady,Zygmunt S. Derewenda,Eleanor J. Dodson,G.G. Dodson,Johan P. Turkenburg,Anthony J. Wilkinson +6 more
TL;DR: The solution of the structure of this enzyme in a different crystal form, with only one molecule in the asymmetric unit is reported, using a model of acid alpha-amylase from a related fungus A. niger.
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Convergent Evolution Sheds Light on the Anti-Beta-Elimination Mechanism Common to Family 1 and 10 Polysaccharide Lyases
TL;DR: Common coordination of the −1 and +1 subsite saccharide carboxylate groups by a protein-liganded Ca2+ ion, the positioning of an arginine catalytic base in close proximity to the α-carbon hydrogen and numerous other conserved enzyme–substrate interactions suggest a generic polysaccharide anti-β-elimination mechanism.
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Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum
Edward J. Taylor,Nicola Smith,Johan P. Turkenburg,Simone D'Souza,Harry J. Gilbert,Gideon J. Davies +5 more
TL;DR: The paucity of direct hydrogen bonds with the aglycone moiety and the flexible conformation adopted by Trp(178), which stacks against the sugar at the +1 subsite, provide a structural explanation for the plasticity in substrate specificity displayed by the clostridial arabinofuranosidase.