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Stephen Bornemann

Researcher at Norwich Research Park

Publications -  74
Citations -  2809

Stephen Bornemann is an academic researcher from Norwich Research Park. The author has contributed to research in topics: Chorismate synthase & Oxalate. The author has an hindex of 30, co-authored 74 publications receiving 2598 citations. Previous affiliations of Stephen Bornemann include Norwich University & John Innes Centre.

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Three Isoforms of Isoamylase Contribute Different Catalytic Properties for the Debranching of Potato Glucans

TL;DR: The data suggest that Stisa1 and Stisa2 act together to debranch soluble glucan during starch synthesis, and the catalytic specificity of Stisa3 is distinct from that of the multimeric enzyme, indicating that it may play a different role in starch metabolism.
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Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an [alpha]-glucan pathway

TL;DR: The unique combination of maltose 1-phosphate toxicity and gene essentiality within a synthetic lethal pathway validates GlgE as a distinct potential drug target that exploits new synergistic mechanisms to induce death in M. tuberculosis.
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Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme.

TL;DR: The barley (Hordeum vulgare) seedling root enzyme was purified to homogeneity and shown by metal analysis and EPR spectroscopy to contain Mn(II) at up to 0.80 atom per subunit.
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Oxalate decarboxylase requires manganese and dioxygen for activity. Overexpression and characterization of Bacillus subtilis YvrK and YoaN.

TL;DR: The structure of YvrK was modeled on the basis of homology with oxalate oxidase, canavalin, and phaseolin, and its hexameric oligomerization was predicted by analogy with proglycinin and homogentisate 1,2-dioxygenase, and only one could be fully occupied by manganese.
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Calcium/Calmodulin-Dependent Protein Kinase Is Negatively and Positively Regulated by Calcium, Providing a Mechanism for Decoding Calcium Responses during Symbiosis Signaling

TL;DR: A model for decoding calcium oscillations that uses differential calcium binding affinities to create a robust molecular switch that is responsive to calcium concentrations associated with both the basal state and with oscillations is provided.