@article{HansScheerRiedletal.2004, author = {Hans, Stefan and Scheer, Nico and Riedl, Iris and Weiz{\"a}cker, Elisabeth von and Blader, Patrick and Campos-Ortega, Jos{\´e} A.}, title = {her3, a zebrafish member of the hairy-E(spl) family, is repressed by Notch signalling}, series = {Development}, volume = {131}, journal = {Development}, number = {12}, issn = {1477-9129}, doi = {10.1242/dev.01167}, pages = {2957 -- 2969}, year = {2004}, language = {en} } @misc{SiekerTippkoetterMuffleretal.2012, author = {Sieker, T. and Tippk{\"o}tter, Nils and Muffler, K. and Ulber, Roland}, title = {Herstellung von Ethanol, Phenols{\"a}uren, organischen S{\"a}uren und Biogas durch vollst{\"a}ndige Nutzung von Grassilage in einer Bioraffinerie}, series = {Chemie Ingenieur Technik}, volume = {84}, journal = {Chemie Ingenieur Technik}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0009-286X}, doi = {10.1002/cite.201250415}, pages = {1297}, year = {2012}, abstract = {Gr{\"a}ser sind in der Lage, einen großen Teil der f{\"u}r eine biobasierte Wirtschaft ben{\"o}tigten Biomasse zur Verf{\"u}gung zustellen. Um eine ganzj{\"a}hrige Nutzung des Grases zu gew{\"a}hrleisten, muss eine stabile Lagerung des Grases erreicht werden, was z. B. durch Silieren m{\"o}glich ist. Die konservierende Wirkung der Silierung beruht auf der Bildung organischer S{\"a}uren. Um diese zu gewinnen, wird die Silage gepresst, die organischen S{\"a}uren {\"u}ber Fl{\"u}ssig/Fl{\"u}ssig-Extraktion aus dem Presssaft abgetrenntund mittels chromatographischer Methoden weiter aufgereinigt. Im pr{\"a}sentierten Konzept werden die im Presskuchen enthaltenen Lignocellulosen hydrolysiert und die erhaltenen Monosaccharide zu Ethanol fermentiert. Die Phenols{\"a}uren, die in Gr{\"a}sern die Rolle des Lignins {\"u}bernehmen, k{\"o}nnen simultan mit der Hydrolyse der Polysaccharide enzymatisch abgetrennt und als Nebenprodukt gewonnen werden. Die nach der Abtrennung des Ethanols verbleibenden Fermentationsreststoffe werden f{\"u}r die Herstellung von Biogas verwendet.}, language = {de} } @article{KotterHammon1984, author = {Kotter, Michael and Hammon, Ulrich}, title = {Herstellung von Formk{\"o}rpern mit definierter Porenstruktur / Ulrich Hammon ; Michael Kotter}, series = {Chemie - Ingenieur - Technik. 56 (1984), H. 6}, journal = {Chemie - Ingenieur - Technik. 56 (1984), H. 6}, isbn = {0009-286X}, pages = {455 -- 463}, year = {1984}, language = {de} } @inproceedings{SiekerDuwePothetal.2012, author = {Sieker, T. and Duwe, A. and Poth, S. and Tippk{\"o}tter, Nils and Ulber, Roland}, title = {Herstellung von Itacons{\"a}ure aus Buchenholzhydrolysaten}, series = {Kurzfassungsband / GVC-DECHEMA Vortrags- und Diskussionstagung Biopharmazeutische Produktion : 14. - 16. Mai 2012. Konzerthaus Freibung}, booktitle = {Kurzfassungsband / GVC-DECHEMA Vortrags- und Diskussionstagung Biopharmazeutische Produktion : 14. - 16. Mai 2012. Konzerthaus Freibung}, publisher = {DECHEMA}, address = {Frankfurt, M.}, pages = {57}, year = {2012}, language = {de} } @article{Kotter1983, author = {Kotter, Michael}, title = {Herstellung von Tr{\"a}nkkatalysatoren als verfahrenstechnische Aufgabe}, series = {Chemie - Ingenieur - Technik. 55 (1983), H. 3}, journal = {Chemie - Ingenieur - Technik. 55 (1983), H. 3}, isbn = {0009-286X}, pages = {179 -- 185}, year = {1983}, language = {de} } @article{KotterKirchRiekert1984, author = {Kotter, Michael and Kirch, M. and Riekert, L.}, title = {Herstellung von Tr{\"a}nkkatalysatoren mit Nickel als Aktivkomponente auf por{\"o}sen Tr{\"a}gern / R. Kirch ; M. Kotter ; L. Riekert}, series = {Chemiker-Zeitung. 108 (1984), H. 4}, journal = {Chemiker-Zeitung. 108 (1984), H. 4}, isbn = {0009-2894}, pages = {121 -- 129}, year = {1984}, language = {de} } @article{PrielmeierSpeedyLuedemann1987, author = {Prielmeier, Franz and Speedy, R. J. and L{\"u}demann, H.-D.}, title = {High Pressure NMR Self-Diffusion Studies on Supercooled Water}, series = {High Pressure Science and Technology Proceeding XI AIRAPT, Kiew. 1}, journal = {High Pressure Science and Technology Proceeding XI AIRAPT, Kiew. 1}, pages = {75}, year = {1987}, language = {en} } @article{PrielmeierLangRadkowitschetal.1987, author = {Prielmeier, Franz and Lang, E. W. and Radkowitsch, H. and L{\"u}demann, H. D.}, title = {High Pressure NMR Study of the Molecular Dynamics of Liquid fluoroform and deutero-fluoroform / Lang, E. W. ; Prielmeier, F. X. ; Radkowitsch, H. ; L{\"u}demann, H. D.}, series = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10}, journal = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10}, isbn = {0005-9021}, pages = {1025 -- 1033}, year = {1987}, language = {en} } @article{PrielmeierLangRadkowitschetal.1987, author = {Prielmeier, Franz and Lang, E. W. and Radkowitsch, H. and L{\"u}demann, H.-D.}, title = {High Pressure NMR Study of the Molecular Dynamics of Liquid methyl fluoride and deutero-methyl fluoride / Lang, E. W. ; Prielmeier, F. X. ; Radkowitsch, H. ; L{\"u}demann, H. D.}, series = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10}, journal = {Berichte der Bunsen-Gesellschaft f{\"u}r Physikalische Chemie. 91 (1987), H. 10}, isbn = {0005-9021}, pages = {1017 -- 1025}, year = {1987}, language = {en} } @article{HeineHerrmannSelmeretal.2014, author = {Heine, A. and Herrmann, G. and Selmer, Thorsten and Terwesten, F. and Buckel, W. and Reuter, K.}, title = {High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily}, series = {Proteins}, volume = {82}, journal = {Proteins}, number = {9}, publisher = {Wiley-Liss}, address = {New York}, issn = {1097-0134 (E-Journal); 0887-3585 (Print)}, doi = {10.1002/prot.24557}, pages = {2041 -- 2053}, year = {2014}, abstract = {Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 {\AA} as well as in complex with CoA at a resolution of 1.59 {\AA}. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041-2053. © 2014 Wiley Periodicals, Inc.}, language = {en} }