Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Hartmut Schurig"'
Publikováno v:
Protein Science. 4:228-236
Enolase (2-phospho-D-glycerate hydrolase; EC 4.2.1.11) from the hyperthermophilic bacterium Thermotoga maritima was purified to homogeneity. The N-terminal 25 amino acids of the enzyme reveal a high degree of similarity to enolases from other sources
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8068c6bff056d24c93bf2f001b36342
https://doi.org/10.1002/pro.5560040209
https://doi.org/10.1002/pro.5560040209
Publikováno v:
Journal of Molecular Biology. 280:525-533
Recombinant phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima (TmPGK) has been expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity applying heat incubation of the crude extract at 80 degree
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::111eef899c3f5ec14b9583279417b204
https://doi.org/10.1006/jmbi.1998.1861
https://doi.org/10.1006/jmbi.1998.1861
Autor:
Uwe Jacob, Günter Auerbach, Robert Huber, Rainer Jaenicke, Mira Grättinger, Hartmut Schurig, Katrin Zaiss
Publikováno v:
Structure. 5(11):1475-1483
Background: Phosphoglycerate kinase (PGK) is essential in most living cells both for ATP generation in the glycolytic pathway of aerobes and for fermentation in anaerobes. In addition, in many plants the enzyme is involved in carbon fixation. Like ot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::857f19ec3c7d9fb9af93c1447b91bc2c
Publikováno v:
Protein & Peptide Letters. 2:281-286
Abstract: The gene encoding 3-phosphoglycerate kinase (PGK) and triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima has been cloned in E.coli. The gene consists of two overlapping open reading frames. In E.coli, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd85ee5a9c93e4f5e9f533e621accfb3
https://doi.org/10.2174/092986650201220524091453
https://doi.org/10.2174/092986650201220524091453
Publikováno v:
The EMBO Journal. 14:442-451
Phosphoglycerate kinase (PGK) from the hyperthermophilic bacterium Thermotoga maritima has been purified to homogeneity. A second larger enzyme with PGK activity and identical N-terminal sequence was also found. Surprisingly, this enzyme displayed tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c91aae614b320d20fbcbc857c335d0c2
https://doi.org/10.1002/j.1460-2075.1995.tb07020.x
https://doi.org/10.1002/j.1460-2075.1995.tb07020.x
Publikováno v:
European Journal of Biochemistry. 216:709-715
The gene for a l(+)-lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima was cloned by complementation of an Escherichia coli pfl. ldh mutant. The gene is part of a 4.5 kb SauIIIA fragment obtained by partial digestion of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf15845a8a1dab475cd1c04c881c56a4
https://doi.org/10.1111/j.1432-1033.1993.tb18190.x
https://doi.org/10.1111/j.1432-1033.1993.tb18190.x
Autor:
Manfred Wuhrer, Stefan Fabry, Hartmut Schurig, Manfred Wozny, Dietmar Reusch, Nicola Beaucamp, Rainer Jaenicke, Doris Wassenberg
Publikováno v:
Biological chemistry. 382(4)
The pgktpi gene locus of Thermotoga maritima encodes both phosphoglycerate kinase (PGK) and a bienzyme complex consisting of a fusion protein of PGK with triosephosphate isomerase (TIM). No separate tpi gene for TIM is present in T. maritima. A frame
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15e9d5aa1543a281b62692a2e072a6b8
https://pubmed.ncbi.nlm.nih.gov/11405233
https://pubmed.ncbi.nlm.nih.gov/11405233
Thermotoga maritima (Tm) expresses a 7 kDa monomeric protein whose 18 N-terminal amino acids show 81% identity to N-terminal sequences of cold shock proteins (Csps) from Bacillus caldolyticus and Bacillus stearothermophilus. There were only trace amo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f00cf564764fc1f139a4dd5fac05695d
https://europepmc.org/articles/PMC2144262/
https://europepmc.org/articles/PMC2144262/
Publikováno v:
Journal of molecular biology. 274(4)
The role of an ionic network of four charged amino acid side-chains in the thermostability of the enzyme D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima (TmGAPDH) has been assessed by site-directed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ede6c8f6c6b8b7502830a069c3986795
https://pubmed.ncbi.nlm.nih.gov/9417944
https://pubmed.ncbi.nlm.nih.gov/9417944
The hyperthermophilic bacterium Thermotoga maritima is capable of gaining metabolic energy utilizing xylan. XynA, one of the corresponding hydrolases required for its degradation, is a 120-kDa endo-1,4-D-xylanase exhibiting high intrinsic stability a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec6eac398f9903e8abf66f6a76746bd9
https://europepmc.org/articles/PMC2143759/
https://europepmc.org/articles/PMC2143759/