Výsledky vyhledávání - "Alexandra, Binter"

Asymmetric Reductive Carbocyclization Using Engineered Ene Reductases

Autor: Alexandra Binter, Peter Macheroux, Marina Toplak, Rolf Breinbauer, Karl Gruber, Kathrin Heckenbichler, Anna Katharina Schweiger, Lea A. Brandner

Publikováno v: Angewandte Chemie (International Ed. in English)

Ene reductases from the Old Yellow Enzyme (OYE) family reduce the C=C double bond in α,β‐unsaturated compounds bearing an electron‐withdrawing group, for example, a carbonyl group. This asymmetric reduction has been exploited for biocatalysis.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccb052433a94aff7969dc86895312449
https://pubmed.ncbi.nlm.nih.gov/29689601

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Catalytic competence, structure and stability of the cancer-associated R139W variant of the human NAD(P)H:quinone oxidoreductase 1 (NQO1)

Autor: Wolf-Dieter, Lienhart, Emilia, Strandback, Venugopal, Gudipati, Karin, Koch, Alexandra, Binter, Michael K, Uhl, David M, Rantasa, Benjamin, Bourgeois, Tobias, Madl, Klaus, Zangger, Karl, Gruber, Peter, Macheroux

Publikováno v: The FEBS journal

The human NAD(P)H:quinone oxidoreductase 1 (NQO1; EC 1.6.99.2) is an essential enzyme in the antioxidant defence system. Furthermore, NQO1 protects tumour suppressors like p53, p33ING1b and p73 from proteasomal degradation. The activity of NQO1 is al

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3840177ca00e847092040aeff823d433
https://pubmed.ncbi.nlm.nih.gov/28236663

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Structural and Functional Characterization of NikO, an Enolpyruvyl Transferase Essential in Nikkomycin Biosynthesis

Autor: Alexandra Binter, Peter Macheroux, Cristian Ginj, Karl Gruber, Gustav Oberdorfer

Publikováno v: Journal of Biological Chemistry. 287:31427-31436

Nikkomycins are peptide-nucleoside compounds with fungicidal, acaricidal, and insecticidal properties because of their strong inhibition of chitin synthase. Thus, they are potential antibiotics especially for the treatment of immunosuppressed patient

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0004131b671cf8e0133c123e0de5474a
https://doi.org/10.1074/jbc.m112.352096

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Characterization of the PLP-dependent aminotransferase NikK from Streptomyces tendae and its putative role in nikkomycin biosynthesis

Autor: Karl Gruber, Stefanie Nerstheimer, Alexandra Binter, Peter Macheroux, Gustav Oberdorfer, Georg Altenbacher, Sebastian Hofzumahaus

Publikováno v: FEBS Journal. 278:4122-4135

As inhibitors of chitin synthase, nikkomycins have attracted interest as potential antibiotics. The biosynthetic pathway to these peptide nucleosides in Streptomyces tendae is only partially known. In order to elucidate the last step of the biosynthe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::211b19ba5395ed827a5f84ad7bcccd2f
https://doi.org/10.1111/j.1742-4658.2011.08319.x

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A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase

Autor: Karl Lohner, Peter Macheroux, Sigrid Deller, Nicole Staunig, Bruce A. Palfey, Ilian Jelesarov, Karl Gruber, Alexandra Binter

Publikováno v: FEBS Journal. 276:5263-5274

YhdA, a thermostable NADPH:FMN oxidoreductase from Bacillus subtilis, reduces quinones via a ping-pong bi-bi mechanism with a pronounced preference for NADPH. The enzyme occurs as a stable tetramer in solution. The two extended dimer surfaces are pac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b52e2f0f0479ac6282be67d3bbd4ecd9
https://doi.org/10.1111/j.1742-4658.2009.07222.x

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Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations

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)

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

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Collapse of the native structure caused by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase(1.)

Autor: Wolf-Dieter, Lienhart, Venugopal, Gudipati, Michael K, Uhl, Alexandra, Binter, Sergio A, Pulido, Robert, Saf, Klaus, Zangger, Karl, Gruber, Peter, Macheroux

Publikováno v: The FEBS journal

Humanquinone oxidoreductase 1 (NQO1) is essential for the antioxidant defense system, stabilization of tumor suppressors (e.g. p53, p33, and p73), and activation of quinone-based chemotherapeutics. Overexpression of NQO1 in many solid tumors, coupled

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bd7c0bcdc38a91cc8bbeb3ca1752573f
https://pubmed.ncbi.nlm.nih.gov/25143260

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The flavoenzyme azobenzene reductase AzoR from Escherichia coli binds roseoflavin mononucleotide (RoFMN) with high affinity and is less active in its RoFMN form

Autor: Tanja Knaus, Shinobu Nakanishi, Tomoko Mase, Peter Macheroux, Alexandra Binter, Masaru Tanokura, Takuya Miyakawa, Matthias Mack, Tilo Mathes, Simone Langer

Publikováno v: Biochemistry. 52(25)

The Gram-positive bacterium Streptomyces davawensis is the only organism known to produce the antibiotic roseoflavin. Roseoflavin is a structural riboflavin analogue and is converted to the flavin mononucleotide (FMN) analogue roseoflavin mononucleot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::349c608667c5a18e393a9c2fd4f349d2
https://pubmed.ncbi.nlm.nih.gov/23713585

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Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III

Autor: Karl Gruber, Sirano Dhe-Paganon, Alexandra Binter, Roland Viertlmayr, Peter Macheroux, Gustavo Arruda Bezerra, Elena Dobrovetsky, Marija Abramić, Aiping Dong

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 109(17)

Opioid peptides are involved in various essential physiological processes, most notably nociception. Dipeptidyl peptidase III (DPP III) is one of the most important enkephalin-degrading enzymes associated with the mammalian pain modulatory system. He

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c353adeac0d0404f03babd75109225a1
https://pubmed.ncbi.nlm.nih.gov/22493238

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