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Robert Huber

Researcher at Technische Universität München

Publications -  742
Citations -  76282

Robert Huber is an academic researcher from Technische Universität München. The author has contributed to research in topics: Active site & Protein structure. The author has an hindex of 139, co-authored 671 publications receiving 73557 citations. Previous affiliations of Robert Huber include Munich University of Applied Sciences & Russian Academy of Sciences.

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Biochemical characterization of Bacillus subtilis type II isopentenyl diphosphate isomerase, and phylogenetic distribution of isoprenoid biosynthesis pathways.

TL;DR: Type II isomerase is essential in some important human pathogens including Staphylococcus aureus and Enterococcus faecalis where it may represent a novel target for anti-infective therapy and in 283 completed and unfinished prokaryotic genomes revealed 10 different classes.
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Crystal Structure of the Dinuclear Zinc Aminopeptidase PepV from Lactobacillus delbrueckii Unravels Its Preference for Dipeptides

TL;DR: PepV from Lactobacillus delbrueckii, a dinuclear zinc peptidase, has been characterized as an unspecific amino dipeptidase as well as a "catalytic domain" and a "lid domain" which together form an internal active site cavity that traps the inhibitor.
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Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5′-phosphate-dependent protein acting as a haemolytic enzyme

TL;DR: Analysis of the cystalysin–L‐aminoethoxyvinylglycine (AVG) complex revealed a ‘dead end’ ketimine PLP derivative, resulting in a total loss of enzyme activity, which may provide the chemical basis for rational drug design.
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Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation.

TL;DR: It is concluded that the endopeptidase uses the metal in the large subunit of [NiFe]-hydrogenases as a recognition motif.
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Crystal structure of the cystine C-S lyase from Synechocystis: Stabilization of cysteine persulfide for FeS cluster biosynthesis

TL;DR: Binding and stabilization of the cysteine persulfide represent an alternative to the generation of a protein-bound Persulfide by NifS-like proteins and point to the general importance of persulfidic compounds for FeS cluster assembly.