Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Andrzej Franciszek Lyskowski"'
Autor:
Andrzej Franciszek Lyskowski, Karl Gruber, Helmut Schwab, Ulf Hanefeld, Kerstin Steiner, Ivan Hajnal
Publikováno v:
FEBS Journal, 280, 5815-28
FEBS Journal, 280, 22, pp. 5815-28
FEBS Journal, 280, 22, pp. 5815-28
Item does not contain fulltext Hydroxynitrile lyases (HNLs), which catalyse the decomposition of cyanohydrins, are found mainly in plants. In vitro, they are able to catalyse the synthesis of enantiopure cyanohydrins, which are versatile building blo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38f0bfeaaaa52d45aab574a94697eec8
https://doi.org/10.1111/febs.12501
https://doi.org/10.1111/febs.12501
Autor:
Bernd Nidetzky, Regina Kratzer, Andrzej Franciszek Lyskowski, Barbara Petschacher, Karl Gruber, Georg Steinkellner, Norbert Klempier, Sigrid Egger, Margit Winkler, Birgit Wilding
Publikováno v:
Chemistry - A European Journal. 19:7007-7012
Nitrile reductase QueF catalyzes the reduction of 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one (preQ0) to 2-amino-5-aminomethylpyrrolo[2,3-d]pyrimidin-4-one (preQ1) in the biosynthetic pathway of the hypermodified nucleoside queuosine. It is the only
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7c145028b40ecd004e454ceed9e9032
https://doi.org/10.1002/chem.201300163
https://doi.org/10.1002/chem.201300163
Autor:
Christoph Kratky, Karl Gruber, Andrzej Franciszek Lyskowski, Marc-Olivier Ebert, Philip A. Butler, Bernhard Kräutler
Publikováno v:
Angewandte Chemie. 118:1004-1008
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4586930d506c32c43f6a3a61330a6172
https://doi.org/10.1002/ange.200502638
https://doi.org/10.1002/ange.200502638
Autor:
Marc-Olivier Ebert, Karl Gruber, Bernhard Kräutler, Christoph Kratky, Philip A. Butler, Andrzej Franciszek Lyskowski
Publikováno v:
Angewandte Chemie International Edition. 45:989-993
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0dd435418bac0dfceac97a58ae8948a
https://doi.org/10.1002/anie.200502638
https://doi.org/10.1002/anie.200502638
Autor:
Christiane Wuensch, Andrzej Franciszek Lyskowski, Silvia M. Glueck, Georg Steinkellner, Kurt Faber, Johannes Gross, Karl Gruber
Publikováno v:
ChemInform. 45
Several decarboxylases are tested for exclusively selective ortho-carboxylation of phenols under ambient reaction conditions using bicarbonate as CO2 source.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8a56c4fcbf8e496b1298e453c114a71
https://doi.org/10.1002/chin.201438076
https://doi.org/10.1002/chin.201438076
Autor:
Kerstin Steiner, Tea Pavkov-Keller, Alexandra Binter, Peter Macheroux, Kurt Faber, Monika Oberer, Helmut Schwab, Orsolya Schwamberger, Karl Gruber, Christoph K. Winkler, Georg Steinkellner, Christian Gruber, Andrzej Franciszek Lyskowski
Publikováno v:
Nature Communications
'Nature Communications ', vol: 5, pages: 4150-1-4150-9 (2014)
'Nature Communications ', vol: 5, pages: 4150-1-4150-9 (2014)
The exploitation of catalytic promiscuity and the application of de novo design have recently opened the access to novel, non-natural enzymatic activities. Here we describe a structural bioinformatic method for predicting catalytic activities of enzy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e71d35171d73fa21cab45954310b663a
https://doi.org/10.1038/ncomms5150
https://doi.org/10.1038/ncomms5150
Autor:
Peter Macheroux, Martin Puhl, Andreas Winkler, Andrzej Franciszek Lyskowski, Toni M. Kutchan, Karl Gruber, Sabrina Riedl
Publikováno v:
Nature Chemical Biology 4, 739-741 (2008). doi:10.1038/nchembio.123
Berberine bridge enzyme catalyzes the conversion of (S)-reticuline to (S)-scoulerine by formation of a carbon-carbon bond between the N-methyl group and the phenolic ring. We elucidated the structure of berberine bridge enzyme from Eschscholzia calif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbea24eb489242beaea0eecfb55db956
https://doi.org/10.1038/nchembio.123
https://doi.org/10.1038/nchembio.123
Autor:
Katharina Schmölzer, Doris Ribitsch, Sabine Zitzenbacher, Tibor Czabany, Andrzej Franciszek Lyskowski, Deja Kokot, Bernd Nidetzky, Christiane Luley-Goedl, Helmut Schwab
Publikováno v:
Glycobiology. 23(11)
A new multifunctional α2,3-sialyltransferase has been discovered in Pasteurella dagmatis. The enzyme, in short PdST, was identified from the P. dagmatis genome by sequence similarity with sialyltransferases of glycosyltransferase family GT-80. In ad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85771e0d0a71bbed8f1a7f49ddd7c733
https://pubmed.ncbi.nlm.nih.gov/23969291
https://pubmed.ncbi.nlm.nih.gov/23969291
Autor:
Andrzej Franciszek Lyskowski, Mandana Gruber-Khadjawi, Martin Tengg, Georg Steinkellner, Karl Gruber, Helmut Schwab
Recombinant {"type":"entrez-protein","attrs":{"text":"Q9F8T9","term_id":"75413747","term_text":"Q9F8T9"}}Q9F8T9 protein from Streptomyces rishiriensis (CouO), an S-adenosyl-l-methionine-dependent C-methyltransferase, has been successfully cloned, e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::829434f241ddb92eb9ced3b41fd01c95
https://europepmc.org/articles/PMC3370914/
https://europepmc.org/articles/PMC3370914/
Autor:
Karl Gruber, Thérésa Bridget Fitzpatrick, Christoph Kratky, Alexander Morokutti, Peter Macheroux, Andrzej Franciszek Lyskowski, Sonja Sollner, Eva Maria Pointner
Publikováno v:
Biochemistry, Vol. 44, No 42 (2005) pp. 13724-33
YcnD from the gram-positive bacterium Bacillus subtilis is a member of a family of bacterial proteins that act as NADH- and/or NADPH-dependent oxidoreductases. Here, we report for the first time on the biochemical characterization of the purified pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91c6f5ad04ea7c97deb4aba059e5d6d2
https://archive-ouverte.unige.ch/unige:89529
https://archive-ouverte.unige.ch/unige:89529