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of 5
pro vyhledávání: '"Florian Mayerthaler"'
Autor:
Jennifer Rüschenbaum, Wieland Steinchen, Florian Mayerthaler, Anna‐Lena Feldberg, Henning D. Mootz
Publikováno v:
Angewandte Chemie (International ed. in English). 61(48)
Nonribosomal peptide synthetases (NRPSs) employ multiple domains, specifically arranged in modules, for the assembly-line biosynthesis of a plethora of bioactive peptides. It is poorly understood how catalysis is correlated with the domain interplay
Autor:
Wieland Steinchen, Florian Mayerthaler, Xun Sun, Jonas Alfermann, Henning D. Mootz, Haw Yang, Anna Lena Feldberg
Publikováno v:
RSC Chemical Biology
Nonribosomal peptide synthetases (NRPSs) are multifunctional megaenzymes that govern the stepwise biosynthesis of pharmaceutically important peptides. In an ATP-dependent assembly-line mechanism dedicated domains are responsible for each catalytic st
Publikováno v:
ACS Chemical Biology. 14:567-578
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Non-ribosomal peptide synthetases (NRPSs) are large, modular enzymes that produce bioactive peptides of tremendous structural and chemical diversity, due to the incorporation, alongside the canonical 20 amino acids, of non-proteinogenic amino acids,
Autor:
Thomas E. Morrell, Henning D. Mootz, Tamiki Komatsuzaki, Xun Sun, Gerrit Volkmann, Jonas Alfermann, Eva Dehling, Florian Mayerthaler, Haw Yang
Publikováno v:
Nature chemical biology. 13(9)
Nonribosomal peptide synthetases (NRPSs) are multidomain enzyme templates for the synthesis of bioactive peptides. Large-scale conformational changes during peptide assembly are obvious from crystal structures, yet their dynamics and coupling to cata