Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Andrea Tomschy"'
Publikováno v:
Protein Science. 3:411-418
An important question in protein folding is whether compact substructures or domains are autonomous units of folding and assembly. The protomer of the tetrameric D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermoto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6fa6ec25667bc193e6e5a28cc4e2806e
https://doi.org/10.1002/pro.5560030305
https://doi.org/10.1002/pro.5560030305
Publikováno v:
"Protein Engineering, Design and Selection". 7:1471-1478
D-Glyceraldehyde 3-phosphate dehydrogenase from Thermotoga maritima (TmGAPDH) is intrinsically thermostable, exhibiting a thermal transition beyond 105 degrees C. Neither the amino-acid composition nor homology modelling, based on sequence alignment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcfa64137fea097829c5ca6ddaea434b
https://doi.org/10.1093/protein/7.12.1471
https://doi.org/10.1093/protein/7.12.1471
Publikováno v:
European Journal of Biochemistry. 214:43-50
The gene coding for D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima has been cloned and functionally expressed in Escherichia coli. Some 90% of the coding gene was amplified by the polymerase chai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::911c706ff1aae0d7d07785c6c6f37728
https://doi.org/10.1111/j.1432-1033.1993.tb17894.x
https://doi.org/10.1111/j.1432-1033.1993.tb17894.x
Autor:
Alexandra Kronenberger, Kurt Vogel, Martin Lehmann, Dominique Burger, Adolphus P. G. M. van Loon, Luis Pasamontes, Markus Wyss, Roland Brugger, Andrea Tomschy, Dirk Kostrewa, Allan Svendsen, Søren Flensted Lassen
For industrial applications in animal feed, a phytase of interest must be optimally active in the pH range prevalent in the digestive tract. Therefore, the present investigation describes approaches to rationally engineer the pH activity profiles of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44fa5dd249d25efab9beae03dc051c1
https://europepmc.org/articles/PMC123903/
https://europepmc.org/articles/PMC123903/
Autor:
Roland Brugger, Line Schnoebelen, Clemens Broger, Michel Tessier, Adolphus P. G. M. van Loon, Luis Pasamontes, Markus Wyss, Andrea Tomschy
Publikováno v:
Protein science : a publication of the Protein Society. 9(7)
Previously, we determined the DNA and amino acid sequences as well as biochemical and biophysical properties of a series of fungal phytases. The amino acid sequences displayed 49-68% identity between species, and the catalytic properties differed wid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d3a5ee89be6af1da390a9296942e984
https://pubmed.ncbi.nlm.nih.gov/10933495
https://pubmed.ncbi.nlm.nih.gov/10933495
Publikováno v:
Journal of molecular biology. 246(4)
The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophile Thermotoga maritima was determined by Patterson search methods using the known structure of the Bacillus stearothermophilus enzyme. The structure was ref
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d05813a99138448de4ba681ace1a63bc
https://pubmed.ncbi.nlm.nih.gov/7877172
https://pubmed.ncbi.nlm.nih.gov/7877172
Autor:
Andrea Tomschy, Adolphus P. G. M. van Loon, Michel Tessier, Luis Pasamontes, Markus Wyss, Haimin Bürgin, Kurt Vogel, R. Remy, Dirk Kostrewa, Sandra Höfer, Alexandra Kronenberger
Publikováno v:
FEBS Letters. (2-3):169-172
The wild-type phytases from the Aspergillus niger strains NRRL 3135 and T213 display a three-fold difference in specific activity (103 versus 32 U/mg protein), despite only 12 amino acid differences that are distributed all over the sequence of the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::242233cb7551b16da717631c5816f941