Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Alexandra Lerchner"'
Autor:
Rajiv Datar, Carlo Marchetti, Benjamin J Swartzwelter, Charles A. Dinarello, Carl K. Edwards, Uli Binder, Martin Schlapschy, Arne Skerra, Dennis M. de Graaf, Nicholas E. Powers, Alexandra Lerchner
Publikováno v:
J Biol Chem
Journal of Biological Chemistry, 295, 3, pp. 868-882
Journal of Biological Chemistry, 295, 868-882
Journal of Biological Chemistry, 295, 3, pp. 868-882
Journal of Biological Chemistry, 295, 868-882
Interleukin-1 (IL-1) is a key mediator of inflammation and immunity. Naturally-occurring IL-1 receptor antagonist (IL-1Ra) binds and blocks the IL-1 receptor-1 (IL-1R1), preventing signaling. Anakinra, a recombinant form of IL-1Ra, is used to treat a
Publikováno v:
Biotechnology and Applied Biochemistry. 63:616-624
The l-alanine dehydrogenase of Bacillus subtilis (BasAlaDH), which is strictly dependent on NADH as redox cofactor, efficiently catalyzes the reductive amination of pyruvate to l-alanine using ammonia as amino group donor. To enable application of Ba
Publikováno v:
ChemCatChem. 5:3374-3383
A matching dehydrogenase and transaminase pair was engineered with regard to substrate recognition, catalytic activity, and cofactor specificity with the final goal to convert the bicyclic dialcohol isosorbide into a diamine by a multistep biocatalyt
Publikováno v:
Biotechnology and Bioengineering. 110:2803-2814
The NADP+-dependent alcohol dehydrogenase from Ralstonia sp. (RasADH) belongs to the protein superfamily of short-chain dehydrogenases/reductases (SDRs). As an enzyme that accepts different types of substrates—including bulky–bulky as well as sma
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:774-787
Apart from their crucial role in metabolism, pyridoxal 5'-phosphate (PLP)-dependent aminotransferases (ATs) constitute a class of enzymes with increasing application in industrial biotechnology. To provide better insight into the structure-function r
Publikováno v:
Scopus-Elsevier
To facilitate biocatalytic conversion of the biotechnologically accessible dicyclic dialcohol isosorbide into its industrially relevant diamines, we have designed a fusion protein between two homo-oligomeric enzymes: the levodione reductase (LR) from
Publikováno v:
Biotechnology and applied biochemistry. 63(5)
The l-alanine dehydrogenase of Bacillus subtilis (BasAlaDH), which is strictly dependent on NADH as redox cofactor, efficiently catalyzes the reductive amination of pyruvate to l-alanine using ammonia as amino group donor. To enable application of Ba
Autor:
Alexandra Lerchner, Ines Schäffner, Regina Schöps, Renate Ulbrich-Hofmann, Johanna Mansfeld, Helge K. Beer
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1737:94-101
The genes of two phospholipase D (PLD) isoenzymes, PLD1 and PLD2, from poppy seedlings (2829 and 2828 bp) were completely sequenced. The two genes have 96.9% identity in the encoding region and can be assigned to the α-type of plant PLDs. The corres
Publikováno v:
Biotechnology Letters. 27:535-544
Phospholipase D (PLD) from plants or microorganisms is used as biocatalyst in the transformation of phospholipids and phospholipid analogs in both laboratory and industrial scale. In recent years the elucidation of the primary structure of many PLDs
Autor:
Angelika Schierhorn, Renate Ulbrich-Hofmann, Alexandra Lerchner, Hina Younus, Karl-Peter Rücknagel, Regina Schöps, M. Saleemuddin
Publikováno v:
Journal of Protein Chemistry. 22:499-508
A recombinant phospholipase D from white cabbage (PLD2) composed of 812 amino acid residues was studied by site-directed mutagenesis and limited proteolysis to obtain first information on its tertiary structure. Limited proteolysis by thermolysin res