TY  - RPRT
A1  - Siegert, Petra
A1  - Bongaerts, Johannes
A1  - Wagner, Torsten
A1  - Schöning, Michael Josef
A1  - Selmer, Thorsten
T1  - Abschlussbericht zum Projekt zur Überwachung biotechnologischer Prozesse mittels Diacetyl-/Acetoin-Biosensor und Evaluierung von Acetoin-Reduktasen zur Verwendung in Biotransformationen
Y1  - 2022
N1  - Laufzeit: 01.01.2016 – 31.12.2019 (verlängert bis 31.12.2020)

Förderkennzeichen: 322-8.03.04.02-FH-Struktur 2016/02

Gefördert durch: Ministerium für Innovation, Wissenschaft und Forschung des Landes Nordrhein-Westfalen
CY  - Aachen
ER  - 
TY  - JOUR
A1  - Selmer, Thorsten
A1  - Thamer, Wiebke
A1  - Cirpus, Irina
A1  - Hans, Marcus
T1  - A two [4Fe-4S]-cluster-containing ferredoxin as an alternative electron donor for 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans / Thamer, Wiebke ; Cirpus, Irina ; Hans, Marcus ; Pierik, Antonio, J. ; Selmer, Thorsten ; Bill, Eckhard ;
JF  - Archives of Microbiology. 179 (2003), H. 3
Y1  - 2003
SN  - 1432-072X
SP  - 197
EP  - 204
ER  - 
TY  - JOUR
A1  - Selmer, Thorsten
A1  - Figura, Kurt von
A1  - Schmidt, Bernhard
A1  - Dierks, T.
T1  - A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease / Figura, Kurt von ; Schmidt, Bernhard ; Selmer, Thorsten ; Dierks, Thomas
JF  - Bioessays. 20 (1998), H. 6
Y1  - 1998
SN  - 1521-1878
SP  - 505
EP  - 510
ER  - 
TY  - JOUR
A1  - Selmer, Thorsten
A1  - Schmidt, Bernhard
A1  - Ingendoh, Arnd
A1  - Figura, Kurt von
T1  - A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency / Schmidt, Bernhard ; Selmer, Thorsten ;  Ingendoh, Arnd ;  Figurat, Kurt von
JF  - Cell. 82 (1995), H. 2
Y1  - 1995
SN  - 0092-8674
SP  - 271
EP  - 278
ER  - 
TY  - JOUR
A1  - Schiffels, Johannes
A1  - Selmer, Thorsten
T1  - A flexible toolbox to study protein-assisted metalloenzyme assembly in vitro
JF  - Biotechnology and Bioengineering
Y1  - 2015
U6  - https://doi.org/10.1002/bit.25658
SN  - 1097-0290
VL  - 112
IS  - 11
SP  - 2360
EP  - 2372
PB  - Wiley
CY  - Weinheim
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  - 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  - https://doi.org/10.1016/j.jbiotec.2017.07.020
SN  - 0168-1656
VL  - 258
SP  - 41
EP  - 50
PB  - Elsevier
CY  - Amsterdam
ER  -