TY - JOUR A1 - Muschallik, Lukas A1 - Molinnus, Denise A1 - Bongaerts, Johannes A1 - Pohl, Martina A1 - Wagner, Torsten A1 - Schöning, Michael Josef A1 - Siegert, Petra A1 - Selmer, Thorsten T1 - (R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme JF - Journal of Biotechnology N2 - The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33–43%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development. Y1 - 2017 U6 - http://dx.doi.org/10.1016/j.jbiotec.2017.07.020 SN - 0168-1656 VL - 258 SP - 41 EP - 50 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Merschenz-Quack, Angelika A1 - Hemmerling, Hans-Jörg A1 - Wunderlich, Hartmut T1 - 1,2-Deoxygenation of vic-Dihydroxyindenoimidazoles: Optimization of a Novel Deoxygenation Reagent. I. / Hemmerling, Hans-Jörg ; Merschenz-Quack, Angelika ; Wunderlich, Hartmut JF - Zeitschrift für Naturforschung B. 59 (2004), H. 10 Y1 - 2004 SN - 0932-0776 SP - 1143 EP - 1152 ER - TY - JOUR A1 - Mang, Thomas A1 - Kricheldorf, Hans R. T1 - 13-C-NMR Sequence Analysis 20. Stereospecificity of the polymerization of D,L-Leu-NCA and D,L-Val-NCA / Kricheldorf, Hans R. ; Mang, Thomas JF - Die makromolekulare Chemie. 182 (1981), H. 11 Y1 - 1981 SN - 1022-1352 SP - 3077 EP - 3098 ER - TY - JOUR A1 - Mang, Thomas A1 - Kricheldorf, Hans R. T1 - 13-C-NMR sequence analysis. 21. Stereoselectivity of oligopeptide syntheses / Kricheldorf, Hans R. ; Mang, Thomas JF - Die makromolekulare Chemie. 183 (1982), H. 9 Y1 - 1982 SN - 1022-1352 SP - 2093 EP - 2111 ER - TY - JOUR A1 - Mang, Thomas A1 - Kricheldorf, Hans R. T1 - 13-C-NMR sequence analysis. 22. Stereoselectivity of the polymerization of D,L-leucine and D,L-valine N-thiocarboxy anhydrides / Kricheldorf, Hans R. ; Mang, Thomas JF - Die makromolekulare Chemie. 183 (1982), H. 9 Y1 - 1982 SN - 1022-1352 SP - 2113 EP - 2129 ER - TY - JOUR A1 - Selmer, Thorsten A1 - Yu, Lihua A1 - Blaser, Martin A1 - Andrei, Paula I. T1 - 4-Hydroxyphenylacetate decarboxylases: properties of a novel subclass of glycyl radical enzyme systems / Yu, L. ; Blaser, M. ; Andrei, PI. ; Pierik, AJ. Selmer, T. JF - Biochemistry. 31 (2006), H. 45 Y1 - 2006 N1 - PMID: 16878993 SP - 9584 EP - 9592 ER - TY - PAT A1 - Banowski, Bernhard A1 - Waldmann-Laue, Marianne A1 - Wadle, Armin A1 - Siegert, Petra A1 - Sättler, Andreas T1 - 5-Lipoxigenase-Inhibitoren in Deodorantien und Antitranspirantien [Offenlegungsschrift] T1 - 5-Lipooxygenase inhibitors in deodorants and antiperspirants [Europäische Patentanmeldung] Y1 - 2004 SP - 1 EP - 12 PB - Deutsches Patent- und Markenamt / Europäisches Patentamt CY - München / Den Hague ER - TY - JOUR A1 - Braband, Henrik A1 - Yegen, Eda A1 - Paulßen, Elisabeth A1 - Abram, Ulrich T1 - [{ReN(PMe2Ph)3}{ReO3N}]2 – Structural Evidence for the Nitridotrioxorhenate(VII) Anion, [ReO3N]2− JF - Zeitschrift für anorganische und allgemeine Chemie : ZAAC = Journal of inorganic and general chemistry Y1 - 2005 U6 - http://dx.doi.org/10.1002/zaac.200500240 SN - 1521-3749 VL - 631 IS - 12 SP - 2408 EP - 2410 ER - TY - JOUR A1 - Biselli, Manfred A1 - Noll, Thomas A1 - Mühlsiepen, Heinz A1 - Engels, Ralf T1 - A cell-culture reactor for the on-line evaluation of radiopharmaceuticals : evaluation of the lumped constant of FDG in human glioma cells / Noll, Thomas ; Mühlensiepen, Heinz ; Engels, Ralf ; Hamacher, Kurt ; Papaspyrou, Manfred ; Langen, Karl-Josef ; Bi JF - Journal of Nuclear Medicine. 41 (2000), H. 3 Y1 - 2000 SN - 0022-3123 SP - 556 EP - 564 ER - TY - JOUR A1 - Scheer, Nico A1 - Wilson, Ian D. T1 - A comparison between genetically humanized and chimeric liver humanized mouse models for studies in drug metabolism and toxicity JF - Drug Discovery Today N2 - Mice that have been genetically humanized for proteins involved in drug metabolism and toxicity and mice engrafted with human hepatocytes are emerging and promising in vivo models for an improved prediction of the pharmacokinetic, drug–drug interaction and safety characteristics of compounds in humans. The specific advantages and disadvantages of these models should be carefully considered when using them for studies in drug discovery and development. Here, an overview on the corresponding genetically humanized and chimeric liver humanized mouse models described to date is provided and illustrated with examples of their utility in drug metabolism and toxicity studies. We compare the strength and weaknesses of the two different approaches, give guidance for the selection of the appropriate model for various applications and discuss future trends and perspectives. Y1 - 2016 U6 - http://dx.doi.org/10.1016/j.drudis.2015.09.002 SN - 1359-6446 VL - 21 IS - 2 SP - 250 EP - 263 PB - Elsevier CY - Amsterdam ER -