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  - 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  - 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  - 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 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  - 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  - 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  -