Ken Scott
University of Auckland
25 Papers
163 Citations
Ken Scott is an academic researcher from University of Auckland. The author has contributed to research in topics: Binding site & Peptide sequence. The author has an hindex of 13, co-authored 25 publications.
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Papers
DING proteins; novel members of a prokaryotic phosphate-binding protein superfamily which extends into the eukaryotic kingdom.
TL;DR: Though it has been claimed that all such proteins may originate from pseudomonads, many eukaryotic DING proteins have unique features which are incompatible with a bacterial origin, and there are two subsets of these proteins; AP proteins, which are alkaline phosphatases, and Dinging proteins, named for their N-terminal sequence, which is phosphate-binding proteins.
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Elucidation of the phosphate binding mode of DING proteins revealed by subangstrom X-ray crystallography.
Dorothee Liebschner,Mikael Elias,Sebastien Moniot,Bertrand Fournier,Ken Scott,Christian Jelsch,Benoit Guillot,Claude Lecomte,Eric Chabrière +8 more
TL;DR: PfluDING structures reveal that only dibasic phosphate binds to the protein at both acidic and basic phosphate, suggesting that the protein binding site environment stabilizes the HPO(4)(2-) form of phosphate.
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Purification and characterisation of a protease (tamarillin) from tamarillo fruit.
TL;DR: De novo sequencing strongly indicated that the protease from tamarillo fruit was a subtilisin-like alkaline serine protease, named 'tamarillin', suggesting that some cysteine residues may be located close to the active site.
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Protease activity of enzyme extracts from tamarillo fruit and their specific hydrolysis of bovine caseins
TL;DR: The characterisation of a serine protease isolated from tamarillo fruit and its milk casein hydrolysis activity were investigated and the purified protease was named "tamarillin" and revealed proteolytic activity toward purified α-, β- and κ-casein.
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Genetic characterization of psp encoding the DING protein in Pseudomonas fluorescens SBW25.
TL;DR: It is proposed that Psp is involved in extracellular scavenging of phosphates, which is subsequently taken up by the cell-bound Pst transport system, whose expression is elevated on plant surfaces.
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