Zobrazeno 1 - 10
of 15
pro vyhledávání: '"E. Bartholomeus Kuettner"'
Autor:
E. Bartholomeus Kuettner, Wieland Kiess, Kerstin Weidle, Anke Tönjes, Norbert Sträter, Michael Stumvoll, Peter Kovacs, Kerstin Krause, Markus Scholz, Yvonne Böttcher, Antje Körner, Dorit Schleinitz, Annette G. Beck-Sickinger, John T. Heiker, Matthias Blüher, Jana Breitfeld
Publikováno v:
Journal of Molecular Medicine. 91:1285-1292
A recent genome-wide association study suggests that genetic variation within the vaspin gene might contribute to the variability in circulating serum visceral adipose tissue-derived serine protease inhibitor (vaspin) concentrations. Here, we analyze
Autor:
Dmitri I. Svergun, Albrecht Otto, Thomas M. Kriegel, Antje Keim, Eva-Christina Müller, Karina Kettner, Daniela Volke, Ralf Hoffmann, Norbert Sträter, David Singer, E. Bartholomeus Kuettner
Publikováno v:
Journal of Biological Chemistry. 285:41019-41033
Crystal structures of the unique hexokinase KlHxk1 of the yeast Kluyveromyces lactis were determined using eight independent crystal forms. In five crystal forms, a symmetrical ring-shaped homodimer was observed, corresponding to the physiological di
Autor:
Antje Keim, Jürgen Kirchberger, Sascha Marek, Norbert Sträter, Marco Kloos, Antje Brüser, E. Bartholomeus Kuettner, Torsten Schöneberg
Publikováno v:
The FASEB Journal. 25:89-98
Eukaryotic ATP-dependent 6-phosphofructokinases (Pfks) differ from their bacterial counterparts in a much more complex structural organization and allosteric regulation. Pichia pastoris Pfk (PpPfk) is, with ∼ 1 MDa, the most complex and probably la
Autor:
Ramona Schmiedel, E. Bartholomeus Kuettner, Norbert Sträter, Thomas Greiner-Stöffele, Antje Keim
Publikováno v:
DNA Repair. 8:219-231
The major AP endonuclease in Escherichia coli Exonuclease III (ExoIII) is frequently used in gene technology due to its strong exonucleolytic activity. A thermostabilized variant of ExoIII or a homologous enzyme from thermophilic organisms could be m
Autor:
Norbert Sträter, Karthik S. Paithankar, Marlis Grunow, Claudia Feller, E. Bartholomeus Kuettner, Antje Keim
Publikováno v:
FEBS Journal. 274:5767-5779
D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida belongs to the family of short-chain dehydrogenases/reductases. We have determined X-ray structures of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida, which was recombinantly ex
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:430-433
Glucose acts as both a carbon source and a hormone-like regulator of gene expression in eukaryotic organisms from yeast to man. Phosphorylation of glucose is executed by hexokinases, which represent a class of multifunctional enzymes that, in additio
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:1290-1293
Temperature-tolerant organisms are an important source to enhance the stability of enzymes used in biotechnological processes. The DNA-cleaving enzyme exonuclease III from Escherichia coli is used in several applications in gene technology. A thermos
Autor:
E. Bartholomeus Kuettner, Thomas M. Kriegel, Ralph Golbik, Hauke Lilie, Albrecht Otto, Karina Kettner, Norbert Sträter
Publikováno v:
Biochemical and biophysical research communications. 435(2)
The bifunctional hexokinase KlHxk1 is a key component of glucose-dependent signal transduction in Kluyveromyces lactis. KlHxk1 is phosphorylated in vivo and undergoes ATP-dependent autophosphorylation-inactivation in vitro. This study identifies seri
Publikováno v:
Journal of molecular biology. 377(2)
Arylmalonate decarboxylase (AMDase) from Bordetella bronchiseptica catalyzes the enantioselective decarboxylation of arylmethylmalonates without the need for an organic cofactor or metal ion. The decarboxylation reaction is of interest for the synthe
Autor:
Karthik S, Paithankar, Claudia, Feller, E Bartholomeus, Kuettner, Antje, Keim, Marlis, Grunow, Norbert, Sträter
Publikováno v:
The FEBS journal. 274(21)
D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida belongs to the family of short-chain dehydrogenases/reductases. We have determined X-ray structures of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida, which was recombinantly ex