@article{SelmerAndrei2001, author = {Selmer, Thorsten and Andrei, Paula I.}, title = {p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol}, series = {European Journal of Biochemistry. 268 (2001), H. 5}, journal = {European Journal of Biochemistry. 268 (2001), H. 5}, isbn = {0014-2956}, pages = {1363 -- 1372}, year = {2001}, language = {en} } @article{SelmerAchebachUnden2005, author = {Selmer, Thorsten and Achebach, Stephanie and Unden, Gottfried}, title = {Properties and significance of apoFNR as a second form of air-inactivated [4Fe-4S]·FNR of Escherichia coli / Achebach, S. ; Selmer, T. ; Unden, G.}, series = {The FEBS Journal. 272 (2005), H. 16}, journal = {The FEBS Journal. 272 (2005), H. 16}, isbn = {1742-464X}, pages = {4260 -- 4269}, year = {2005}, language = {en} } @article{SelmerWillanzheimerHetzel2002, author = {Selmer, Thorsten and Willanzheimer, Angela and Hetzel, Marc}, title = {Propionate CoA-transferase from Clostridium propionicum. Cloning of the gene and identification of glutamate 324 at the active site}, series = {European Journal of Biochemistry. 269 (2002), H. 1}, journal = {European Journal of Biochemistry. 269 (2002), H. 1}, isbn = {0014-2956}, pages = {372 -- 380}, year = {2002}, language = {en} } @article{SelmerScottNaeseretal.2004, author = {Selmer, Thorsten and Scott, Richard and N{\"a}ser, Ulrike and Friedrich, Peter}, title = {Stereochemistry of hydrogen removal from the 'unactivated' C-3 position of 4-hydroxybutyryl-CoA catalysed by 4-hydroxybutyryl-CoA dehydratase / Scott, R. ; N{\"a}ser, U. ; Friedrich, P. ; Selmer, T. ; Buckel, W. ; Golding, BT.}, series = {Chemical Communications : ChemCom (2004)}, journal = {Chemical Communications : ChemCom (2004)}, isbn = {1364-548X}, pages = {1210 -- 1211}, year = {2004}, language = {en} } @article{SelmerDarleyCleggetal.2003, author = {Selmer, Thorsten and Darley, Dan J. and Clegg, William and Harrington, Ross W.}, title = {Stereocontrolled Synthesis of (2R,3S)-2-Methylisocitrate, a Central Intermediate in the Methylcitrate Cycle / Darley, Dan J. ; Selmer, Thorsten ; Clegg, William ; Harrington, Ross W. ; Buckel, Wolfgang ; Golding, Bernardt}, series = {Helvetica chimica acta. 86 (2003), H. 12}, journal = {Helvetica chimica acta. 86 (2003), H. 12}, isbn = {1522-2675}, pages = {3991 -- 3999}, year = {2003}, language = {en} } @article{MartinsBlaserFeliksetal.2011, author = {Martins, Berta M. and Blaser, Martin and Feliks, Mikolaj and Ullmann, Matthias G. and Buckel, Wolfgang and Selmer, Thorsten}, title = {Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme}, series = {Journal of the American Chemical Society}, journal = {Journal of the American Chemical Society}, publisher = {ACS Publications}, address = {Washington, DC}, pages = {1 -- 33}, year = {2011}, language = {en} } @article{SelmerAndreiPieriketal.2004, author = {Selmer, Thorsten and Andrei, Paula I. and Pierik, Antonio J. and Zauner, Stefan}, title = {Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity / Andrei, PI. ; Pierik, AJ. ; Zauner , S. ; Andrei-Selmer, LC. ; Selmer, T.}, series = {European Journal of Biochemistry. 271 (2004), H. 11}, journal = {European Journal of Biochemistry. 271 (2004), H. 11}, isbn = {0014-2956}, pages = {2225 -- 2230}, year = {2004}, language = {en} } @article{SelmerRecksiekDierksetal.1998, author = {Selmer, Thorsten and Recksiek, Michael and Dierks, Thomas and Schmidt, Bernhard}, title = {Sulfatases, Trapping of the Sulfated Enzyme Intermediate by Substituting the Active Site Formylglycine / Recksiek, Michael ; Selmer, Thorsten ; Dierks, Thomas ; Schmidt, Bernhard ; Figura, Kurt von}, series = {Journal of Biological Chemistry. 273 (1998), H. 11}, journal = {Journal of Biological Chemistry. 273 (1998), H. 11}, isbn = {1083-351X}, pages = {6096 -- 6103}, year = {1998}, language = {en} } @article{MuschallikMolinnusJablonskietal.2020, author = {Muschallik, Lukas and Molinnus, Denise and Jablonski, Melanie and Kipp, Carina Ronja and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra}, title = {Synthesis of α-hydroxy ketones and vicinal (R, R)-diols by Bacillus clausii DSM 8716ᵀ butanediol dehydrogenase}, series = {RSC Advances}, volume = {10}, journal = {RSC Advances}, publisher = {Royal Society of Chemistry (RSC)}, address = {Cambridge}, issn = {2046-2069}, doi = {10.1039/D0RA02066D}, pages = {12206 -- 12216}, year = {2020}, abstract = {α-hydroxy ketones (HK) and 1,2-diols are important building blocks for fine chemical synthesis. Here, we describe the R-selective 2,3-butanediol dehydrogenase from B. clausii DSM 8716ᵀ (BcBDH) that belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR) and catalyzes the selective asymmetric reduction of prochiral 1,2-diketones to the corresponding HK and, in some cases, the reduction of the same to the corresponding 1,2-diols. Aliphatic diketones, like 2,3-pentanedione, 2,3-hexanedione, 5-methyl-2,3-hexanedione, 3,4-hexanedione and 2,3-heptanedione are well transformed. In addition, surprisingly alkyl phenyl dicarbonyls, like 2-hydroxy-1-phenylpropan-1-one and phenylglyoxal are accepted, whereas their derivatives with two phenyl groups are not substrates. Supplementation of Mn²⁺ (1 mM) increases BcBDH's activity in biotransformations. Furthermore, the biocatalytic reduction of 5-methyl-2,3-hexanedione to mainly 5-methyl-3-hydroxy-2-hexanone with only small amounts of 5-methyl-2-hydroxy-3-hexanone within an enzyme membrane reactor is demonstrated.}, language = {en} } @article{MuschallikKippReckeretal.2020, author = {Muschallik, Lukas and Kipp, Carina Ronja and Recker, Inga and Bongaerts, Johannes and Pohl, Martina and Gelissen, Melanie and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra}, title = {Synthesis of α-hydroxy ketones and vicinal diols with the Bacillus licheniformis DSM 13T butane-2, 3-diol dehydrogenase}, series = {Journal of Biotechnology}, volume = {202}, journal = {Journal of Biotechnology}, number = {Vol. 324}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {2590-1559}, doi = {10.1016/j.jbiotec.2020.09.016}, pages = {61 -- 70}, year = {2020}, abstract = {The enantioselective synthesis of α-hydroxy ketones and vicinal diols is an intriguing field because of the broad applicability of these molecules. Although, butandiol dehydrogenases are known to play a key role in the production of 2,3-butandiol, their potential as biocatalysts is still not well studied. Here, we investigate the biocatalytic properties of the meso-butanediol dehydrogenase from Bacillus licheniformis DSM 13T (BlBDH). The encoding gene was cloned with an N-terminal StrepII-tag and recombinantly overexpressed in E. coli. BlBDH is highly active towards several non-physiological diketones and α-hydroxyketones with varying aliphatic chain lengths or even containing phenyl moieties. By adjusting the reaction parameters in biotransformations the formation of either the α-hydroxyketone intermediate or the diol can be controlled.}, language = {en} }