Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Mandana Gruber-Khadjawi"'
Autor:
Tea Pavkov-Keller, Kerstin Steiner, Mario Faber, Martin Tengg, Helmut Schwab, Mandana Gruber-Khadjawi, Karl Gruber
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0171056 (2017)
Friedel-Crafts alkylation of aromatic systems is a classic reaction in organic chemistry, for which regiospecific mono-alkylation, however, is generally difficult to achieve. In nature, methyltransferases catalyze the addition of methyl groups to a w
Externí odkaz:
https://doaj.org/article/9fad6ec7b63d4975b0e90a7b5e97f40b
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 10, Iss 16, Pp 58-62 (2014)
Hydroxynitrile lyases (HNLs) are powerful carbon–carbon bond forming enzymes. The reverse of their natural reaction – the stereoselective addition of hydrogen cyanide (HCN) to carbonyls – yields chiral cyanohydrins, versatile building blocks fo
Externí odkaz:
https://doaj.org/article/810ee9088aa546be957f0eb23a1a6d0d
Publikováno v:
Organic & Biomolecular Chemistry. 15:7917-7924
Various bioactive natural products, like the aminocoumarin antibiotics novobiocin and coumermycin, exhibit an aromatic C-methyl group adjacent to a glycosylated phenolic hydroxyl group. Therefore, tailoring of basic phenolic scaffolds to contain the
Autor:
Patrik Fladischer, Niklaus Anderhuber, Juergen Mairhofer, Gerald Striedner, Mandana Gruber-Khadjawi, Birgit Wiltschi
Publikováno v:
Journal of Biotechnology. 235:100-111
The residue-specific labeling of proteins with non-canonical amino acids (ncAA) is well established in shake flask cultures. A key aspect for the transfer of the methodology to larger scales for biotechnological applications is the cost of the supple
Autor:
Katharina Plasch, Mandana Gruber-Khadjawi, Helmut Schwab, Martin Tengg, Felix Anderl, Lisa Offner, Hansjörg Weber, Harald Stecher
Publikováno v:
ChemCatChem. 8:1354-1360
Autor:
Bettina Kothbauer, Helmut Schwab, Tea Pavkov-Keller, Karl Gruber, Mandana Gruber-Khadjawi, Romana Wiedner, Kerstin Steiner
Publikováno v:
ChemCatChem. 7:325-332
Hydroxynitrile lyases (HNLs) catalyse the reversible cleavage of cyanohydrins to carbonyl compounds and HCN. The recent discovery of bacterial HNLs with a cupin fold gave rise to a new promising class of these enzymes. They are interesting candidates
Autor:
Helmar Wiltsche, Mandana Gruber-Khadjawi, Helmut Schwab, Romana Wiedner, Myria Bekerle-Bogner, Kerstin Steiner
Publikováno v:
ChemCatChem. 8:2214-2216
The nitroaldol (Henry) reaction is a valuable C−C bond-forming reaction resulting in β-nitro alcohols, which are important building blocks for the synthesis of bioactive compounds. Metal-dependent bacterial hydroxynitrile lyases with a cupin fold
Autor:
Elisa Lanfranchi, Tea Pavkov-Keller, Eva-Maria Koehler, Matthias Diepold, Kerstin Steiner, Barbara Darnhofer, Jürgen Hartler, Tom Van Den Bergh, Henk-Jan Joosten, Mandana Gruber-Khadjawi, Gerhard G. Thallinger, Ruth Birner-Gruenberger, Karl Gruber, Margit Winkler, Anton Glieder
Publikováno v:
Scientific Reports
Homology and similarity based approaches are most widely used for the identification of new enzymes for biocatalysis. However, they are not suitable to find truly novel scaffolds with a desired function and this averts options and diversity. Hydroxyn
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 10, Iss 16, Pp 58-62 (2014)
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal
Hydroxynitrile lyases (HNLs) are powerful carbon–carbon bond forming enzymes. The reverse of their natural reaction – the stereoselective addition of hydrogen cyanide (HCN) to carbonyls – yields chiral cyanohydrins, versatile building blocks fo
Publikováno v:
ChemCatChem. 5:1248-1272
Carbon-carbon bond formation is among the most challenging transformations in the organic synthetic chemistry. Enzymes capable to perform this reaction are of great interest. The enzymes for stereoselective CC bond formations have been investigated v