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Norbert Sträter
Researcher at Leipzig University
Publications - 141
Citations - 7697
Norbert Sträter is an academic researcher from Leipzig University. The author has contributed to research in topics: Chemistry & Active site. The author has an hindex of 36, co-authored 127 publications receiving 6894 citations. Previous affiliations of Norbert Sträter include Free University of Berlin & Harvard University.
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Recent Advances in Zinc Enzymology
TL;DR: Zinc enzymology is, compared to some other current areas of metallobiochemistry, a maturing field, but in addition to further developments of structure-function relationships it has also provided a number of surprising new results and ideas in the last few years.
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Cellular function and molecular structure of ecto-nucleotidases
TL;DR: The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.
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Two-Metal Ion Catalysis in Enzymatic Acyl- and Phosphoryl-Transfer Reactions
TL;DR: A remarkable diversity is also seen in the structures of the active sites of these di- and trinuclear metalloenzymes, even for enzymes that catalyze very similar reactions, including hydrolytic cleavage of phosphomono-, -di- and -triester bonds, phosphoanhydride bonds as well as of peptide bonds or urea.
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Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.
TL;DR: The active-site structure of the homodimeric 111-kilodalton KBPAP is consistent with previous proposals regarding the mechanism of phosphate ester hydrolysis involving nucleophilic attack on the phosphate group by an Fe(III)-coordinated hydroxide ion.
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Mechanism of Fe III –Zn II purple acid phosphatase based on crystal structures
TL;DR: All three structures reported herein support a mechanism of phosphate ester hydrolysis involving interaction of the substrate with Zn(II) followed by a nucleophilic attack on the phosphorus by an Fe(III)-coordinated hydroxide ion.