Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Bjarne Stoffer"'
Autor:
Jette S. Kastrup, Bjarne Stoffer, Poul Baad Rasmussen, Anja K. Pedersen, Hans Flodgaard, Lars Fogh Iversen, Søren E. Bjørn, Viggo Linde, Ingrid Kjøller Larsen
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 42:442-451
Heparin binding protein (HBP) is an inactive serine protease homologue with important implications in host defense during infections and inflammations. Two mutants of human HBP, [R23S,F25E]HBP and [G175Q]HBP, have been produced to investigate structu
Autor:
Dale R. Cameron, Raymond U. Lemieux, Birte Svensson, Torben P. Frandsen, Monica M. Palcic, Mimi Bach, Bjarne Stoffer, Ulrike Spohr
Publikováno v:
Canadian Journal of Chemistry. 74:319-335
A recently developed technique for the probing of the combining sites of lectins and antibodies, to establish the structure of the epitope that is involved in the binding of an oligosaccharide, is used to study the binding of methyl α-isomaltoside b
Publikováno v:
Biochemistry. 35:8696-8704
Rational protein engineering based on three-dimensional structure, sequence alignment, and previous mutational analysis served to increase thermostability and modulate bond-type specificity in glucoamylase from Aspergillus awamori. The single free cy
Publikováno v:
Biochemistry. 35:15009-15018
Glucoamylase (1,4-alpha-glucan glucohydrolase, EC 3.2.1.3) from Aspergillus, of which the 3D structure is known, releases beta-D-glucose from the non-reducing ends of starch and other related oligo and polysaccharides, cleaving the alpha-1,4-bond pos
Publikováno v:
Biochemistry. 34:10153-10161
We have investigated the binding of mutant forms of glucoamylase from Aspergillus niger to the inhibitors 1-deoxynojirimycin and acarbose. The mutants studied comprise a group of single amino acid replacements in conserved regions near the active sit
Autor:
Torben P. Frandsen, Michael R. Sierks, Jan Lehmbeck, Richard B. Honzatko, Birte Svensson, Bjarne Stoffer, Claude Dupont
Publikováno v:
Biochemistry. 33:13808-13816
Replacement of the catalytic base Glu400 by glutamine in glucoamylase from Aspergillus niger affects both substrates ground-state binding and transition-state stabilization. Compared to those of the wild-type enzyme, Km values for maltose and maltohe
Autor:
David E. Metzler, Alexander E. Aleshin, Birte Svensson, Carol M. Metzler, Trine Christensen, Bjarne Stoffer, Robert D. Scott, Kirill N. Neustroev, Leonid M. Firsov
Publikováno v:
European Journal of Biochemistry. 223:293-302
1H-NMR spectra have been recorded for glucoamylases I and II from Aspergillus awamori var. X100 and from A. niger in the 9-15-ppm region. At least 17 distinct peaks, many of them arising from single protons, are observed. These are designated A-Q, A
Autor:
Torben P. Frandsen, B. Mario Pinto, Bjarne Stoffer, Birte Svensson, Margaret A. Johnson, Karla D. Randell
Publikováno v:
ChemInform. 31
The synthesis of a series of 5-thio- d -glucopyranosylarylamines by reaction of 5-thio- d -glucopyranose pentaacetate with the corresponding arylamine and mercuric chloride catalyst is reported. The products were obtained as anomeric mixtures of the
Publikováno v:
Biochemistry. 39(2)
Transferred nuclear Overhauser effect (trNOE) experiments have been performed to investigate the conformations of the competitive inhibitors, methyl 5'-thio-4-N-alpha-maltoside 3a and methyl 5'-thio-4-S-alpha-maltoside 4 when bound to the catalytic s
Publikováno v:
Technical University of Denmark Orbit
Presteady and steady-state kinetic results on the interactions of a wild-type, and the mutant glucoamylases Trp52-->Phe and Trp317-->Phe, from Aspergillus niger with maltose, maltotriose and maltotetraose have been obtained and analyzed. The results