Zobrazeno 1 - 10
of 84
pro vyhledávání: '"Peter, Kast"'
Autor:
Helen V. Thorbjørnsrud, Luca Bressan, Tamjidmaa Khatanbaatar, Manuel Carrer, Kathrin Würth-Roderer, Gabriele Cordara, Peter Kast, Michele Cascella, Ute Krengel
Publikováno v:
Biochemistry, 62 (3)
Unlike typical chorismate mutases, the enzyme from Mycobacterium tuberculosis (MtCM) has only low activity on its own. Remarkably, its catalytic efficiency kcat/Km can be boosted more than 100-fold by complex formation with a partner enzyme. Recently
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f865d8c5300632314aee51594b3476e4
Autor:
Christian Stocker, Tamjidmaa Khatanbaatar, Kathrin Würth-Roderer, Gabriele Cordara, Ute Krengel, Peter Kast
Chorismate mutase (CM) and cyclohexadienyl dehydratase (CDT) catalyze two subsequent reactions in the intracellular biosynthesis of phenylalanine. Surprisingly, exported CMs and CDTs exist in bacterial pathogens. Here, we report the discovery of nove
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b482612f2e0397883baae69950bc1dd7
https://doi.org/10.2139/ssrn.4388939
https://doi.org/10.2139/ssrn.4388939
Autor:
Susanne Mailand, Ute Krengel, Peter Kast, Kathrin Würth-Roderer, Helen Vikdal Thorbjørnsrud, Jūrate˙ Fahrig-Kamarauskait≑
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry, 295 (51)
'Journal of Biological Chemistry ', vol: 295, pages: 17514-17534 (2020)
Journal of Biological Chemistry, 295 (51)
'Journal of Biological Chemistry ', vol: 295, pages: 17514-17534 (2020)
Chorismate mutase (CM), an essential enzyme at the branch-point of the shikimate pathway, is required for the biosynthesis of phenylalanine and tyrosine in bacteria, archaea, plants, and fungi. MtCM, the CM from Mycobacterium tuberculosis, has less t
Autor:
Marianne Gamper, Peter Kast
Publikováno v:
BioTechniques, Vol 38, Iss 3, Pp 405-408 (2005)
Reengineering DNA by homologous recombination in Escherichia coli often depends on helper functions provided on a temporarily introduced replicon that is subsequently cured from the cells. The suicide vector pKSS offers a new curing strategy. pKSS sp
Externí odkaz:
https://doaj.org/article/b72af11d3d584863a106c5b2d11d4696
Autor:
Kathrin Roderer, Martin Neuenschwander, Giosiana Codoni, Severin Sasso, Marianne Gamper, Peter Kast
Publikováno v:
PLoS ONE, Vol 9, Iss 12, p e116234 (2014)
The shikimate pathway enzyme chorismate mutase converts chorismate into prephenate, a precursor of Tyr and Phe. The intracellular chorismate mutase (MtCM) of Mycobacterium tuberculosis is poorly active on its own, but becomes >100-fold more efficient
Externí odkaz:
https://doaj.org/article/e9c2f6fb77be47b290ba366282779510
Autor:
Gavin MacBeath, Peter Kast
Publikováno v:
BioTechniques, Vol 24, Iss 5, Pp 789-794 (1998)
pET and similar vectors are widely used for efficient gene expression in Escherichia coli and subsequent protein purification, often by means of a C-terminal histidine (His) tag. We found that the TGA translation termination signal following the His-
Externí odkaz:
https://doaj.org/article/7259b52efd914837a884b27da31d9181
Autor:
Manuel M Müller, Jane R Allison, Narupat Hongdilokkul, Laurent Gaillon, Peter Kast, Wilfred F van Gunsteren, Philippe Marlière, Donald Hilvert
Publikováno v:
PLoS Genetics, Vol 9, Iss 1, p e1003187 (2013)
The contemporary proteinogenic repertoire contains 20 amino acids with diverse functional groups and side chain geometries. Primordial proteins, in contrast, were presumably constructed from a subset of these building blocks. Subsequent expansion of
Externí odkaz:
https://doaj.org/article/0f687fdbf2764a9ca772733f50d682da
Autor:
Peter Kast, Christian Stocker, Matteo Figliuzzi, Rama Ranganathan, Martin Weigt, Pierre Barrat-Charlaix, Michael Socolich, Simona Cocco, William P. Russ, Rémi Monasson, Donald Hilvert
Publikováno v:
Science, 369 (6502)
Science
Science, American Association for the Advancement of Science, 2020, 369 (6502), pp.440-445. ⟨10.1126/science.aba3304⟩
Science
Science, American Association for the Advancement of Science, 2020, 369 (6502), pp.440-445. ⟨10.1126/science.aba3304⟩
The rational design of enzymes is an important goal for both fundamental and practical reasons. Here, we describe a process to learn the constraints for specifying proteins purely from evolutionary sequence data, design and build libraries of synthet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45546e2d6b2865473d78278d7147431e
https://hdl.handle.net/20.500.11850/429569
https://hdl.handle.net/20.500.11850/429569
Autor:
Kathrin Roderer, Peter Kast
Publikováno v:
CHIMIA, Vol 63, Iss 6 (2009)
Directed evolution strategies are being applied ever more frequently to develop novel and improved enzymes for many applications, including those contributing to 'white biotechnology'. In addition to engineering new biocatalysts, evolutionary strateg
Externí odkaz:
https://doaj.org/article/9b02c41b958b48f78406e1a113f37d77
Autor:
Steffi Munack, Jurate Kamarauskaite, Peter Kast, Ute Krengel, Severin Sasso, Kathrin Roderer, Mats Ökvist, André van Eerde
Publikováno v:
J. Mol. Biol.
DAHP synthase and chorismate mutase catalyze key steps in the shikimate biosynthetic pathway en route to aromatic amino acids. In Mycobacterium tuberculosis, chorismate mutase (MtCM; Rv0948c), located at the branch point toward phenylalanine and tyro