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  • (-) Eawag Departments = Environmental Microbiology UMIK
  • (-) Publication Year = 2006 - 2018
  • (-) Keywords ≠ bioaugmentation
  • (-) Full Text ≠ Open Access
  • (-) Eawag Authors = Heck, Tobias
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Bacterial β-Aminopeptidases: structural insights and applications for biocatalysis
Heck, T., Geueke, B., & Kohler, H. P. E. (2012). Bacterial β-Aminopeptidases: structural insights and applications for biocatalysis. Chemistry and Biodiversity, 9(11), 2388-2409. https://doi.org/10.1002/cbdv.201200305
Autoproteolytic and catalytic mechanisms for the β-aminopeptidase BapA - a member of the Ntn hydrolase family
Merz, T., Heck, T., Geueke, B., Mittl, P. R. E., Briand, C., Seebach, D., … Grütter, M. G. (2012). Autoproteolytic and catalytic mechanisms for the β-aminopeptidase BapA - a member of the Ntn hydrolase family. Structure, 20(11), 1850-1860. https://doi.org/10.1016/j.str.2012.07.017
Bacterial β-aminopeptidases: function, structure and applications
Heck, T. (2010). Bacterial β-aminopeptidases: function, structure and applications [Doctoral dissertation, ETH Zürich]. https://doi.org/10.3929/ethz-a-006144396
Kinetic analysis of L-carnosine formation by β-aminopeptidases
Heck, T., Makam, V. S., Lutz, J., Blank, L. M., Schmid, A., Seebach, D., … Geueke, B. (2010). Kinetic analysis of L-carnosine formation by β-aminopeptidases. Advanced Synthesis and Catalysis, 352, 407-415. https://doi.org/10.1002/adsc.200900697
β-aminopeptidase-catalyzed biotransformations of β2- dipeptides: kinetic resolution and enzymatic coupling
Heck, T., Reimer, A., Seebach, D., Gardiner, J., Deniau, G., Lukaszuk, A., … Geueke, B. (2010). β-aminopeptidase-catalyzed biotransformations of β2- dipeptides: kinetic resolution and enzymatic coupling. ChemBioChem, 11(8), 1129-1136. https://doi.org/10.1002/cbic.200900757
Kinetic resolution of aliphatic β-amino acid amides by β-aminopeptidases
Heck, T., Seebach, D., Osswald, S., ter Wiel, M. K. J., Kohler, H. P. E., & Geueke, B. (2009). Kinetic resolution of aliphatic β-amino acid amides by β-aminopeptidases. ChemBioChem, 10(9), 1558-1561. https://doi.org/10.1002/cbic.200900184
Enzyme-catalyzed formation of <i>&beta;</i>-peptides: <i>&beta;</i>-peptidyl aminopeptidases BapA and DmpA acting as <i>&beta;</i>-peptide-synthesizing enzymes
Heck, T., Kohler, H. P. E., Limbach, M., Flögel, O., Seebach, D., & Geueke, B. (2007). Enzyme-catalyzed formation of β-peptides: β-peptidyl aminopeptidases BapA and DmpA acting as β-peptide-synthesizing enzymes. Chemistry and Biodiversity, 4(9), 2016-2030. https://doi.org/10.1002/cbdv.200790168
Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β,α-oligopeptides
Geueke, B., Heck, T., Limbach, M., Nesatyy, V., Seebach, D., & Kohler, H. P. E. (2006). Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β,α-oligopeptides. FEBS Journal, 273(23), 5261-5272. https://doi.org/10.1111/j.1742-4658.2006.05519.x
Enzymatic degradation of β- and mixed α,β-oligopeptides
Heck, T., Limbach, M., Geueke, B., Zacharias, M., Gardiner, J., Kohler, H. P. E., & Seebach, D. (2006). Enzymatic degradation of β- and mixed α,β-oligopeptides. Chemistry and Biodiversity, 3(12), 1325-1348. https://doi.org/10.1002/cbdv.200690136