Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Catharina Jürgens"'
Publikováno v:
Journal of Molecular Biology. 337:871-879
The (betaalpha)(8)-barrel enzymes N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase (tHisA) and imidazole glycerol phosphate synthase (tHisF) from Thermotoga maritima catalyze two successive reactions in the bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a9365d0c41a5b2724bd932a14e3b2d6
https://doi.org/10.1016/j.jmb.2004.01.062
https://doi.org/10.1016/j.jmb.2004.01.062
Autor:
Olga Mayans, Kasper Kirschner, Matthias Wilmanns, Catharina Jürgens, Halina Szadkowski, Andreas Ivens
Publikováno v:
European Journal of Biochemistry. 269:1145-1153
The aim of this study was to increase the stability of the thermolabile (βα)8-barrel enzyme indoleglycerol phosphate synthase from Escherichia coli by the introduction of disulfide bridges. For the design of such variants, we selected two out of 12
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::498443f2730a4e70b19b93855887ff40
https://doi.org/10.1046/j.1432-1033.2002.02745.x
https://doi.org/10.1046/j.1432-1033.2002.02745.x
Publikováno v:
Current Opinion in Biotechnology. 12:376-381
The (beta alpha)(8)-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (beta alpha)(8)-barrel fold has been used as a model to elucidate the structural basis of protein thermostability and in studies to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3dcf2d5186d1da1c625204ad93251bc
https://doi.org/10.1016/s0958-1669(00)00230-5
https://doi.org/10.1016/s0958-1669(00)00230-5
Autor:
Andreas, Ivens, Olga, Mayans, Halina, Szadkowski, Catharina, Jürgens, Matthias, Wilmanns, Kasper, Kirschner
Publikováno v:
European journal of biochemistry. 269(4)
The aim of this study was to increase the stability of the thermolabile (betaalpha)8-barrel enzyme indoleglycerol phosphate synthase from Escherichia coli by the introduction of disulfide bridges. For the design of such variants, we selected two out
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1467727b4feaf4282db950e868ee7d33
https://pubmed.ncbi.nlm.nih.gov/11856350
https://pubmed.ncbi.nlm.nih.gov/11856350
Autor:
Catharina Jürgens, Reinhard Sterner, Stefan Hettwer, Matthias Wilmanns, D. Wegener, Alexander Strom
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 97(18)
Enzymes participating in different metabolic pathways often have similar catalytic mechanisms and structures, suggesting their evolution from a common ancestral precursor enzyme. We sought to create a precursor-like enzyme for N ′-[(5′-phosphorib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82f48d71492a83c10cd59c288a300bb1
https://pubmed.ncbi.nlm.nih.gov/10944186
https://pubmed.ncbi.nlm.nih.gov/10944186