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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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The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily.

TL;DR: Models of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggest possible mechanistic roles for Glu-244, Asp-154, His-122, his-45, and His-145.
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Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis.

TL;DR: Crystals of recombinant Haemophilus influenzae DapF that diffract to beyond 2 A resolution have been obtained which facilitated the solution of the structure by molecular replacement at a resolution approximately 1 A higher than that previously determined.
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Structural and functional insights into asymmetric enzymatic dehydration of alkenols

TL;DR: The structure and substrate specificity of the bifunctional linalool dehydratase isomerase (LinD) from the bacterium Castellaniella defragrans is reported, which facilitates the development of hydrating catalysts, enriching the toolbox for novel bond-forming biocatalysis.
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The structural characterization of a prophage-encoded extracellular DNase from Streptococcus pyogenes

TL;DR: The X-ray structure of Spd1, a type I, nonspecific ββα/metal-dependent nuclease from Streptococcus pyogenes, which is encoded by the SF370.1 prophage, is presented and the possibility of a catalytically blocked dimeric form of the protein is alludes to.
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A family of native amine dehydrogenases for the asymmetric reductive amination of ketones

TL;DR: The discovery of a family of native NAD(P)H-dependent amine dehydrogenases competent for the asymmetric reductive amination of aliphatic and alicyclic ketones is reported, adding significantly to the biocatalytic toolbox available for chiral amine synthesis.