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Crystal structures of BapA complexes with β-öactam-derived inhibitors illustrate substrate specificity and enantioselectivity of β-Aminopeptidases
Heck, T., Merz, T., Reimer, A., Seebach, D., Rentsch, D., Briand, C., … Geueke, B. (2012). Crystal structures of BapA complexes with β-öactam-derived inhibitors illustrate substrate specificity and enantioselectivity of β-Aminopeptidases. ChemBioChem, 13(14), 2137-2145. https://doi.org/10.1002/cbic.201200393
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
Bacterial cell penetration by β<SUP>3</SUP>-oligohomoarginines: indications for passive transfer through the lipid bilayer
Geueke, B., Namoto, K., Agarkova, I., Perriard, J. C., Kohler, H. P. E., & Seebach, D. (2005). Bacterial cell penetration by β3-oligohomoarginines: indications for passive transfer through the lipid bilayer. ChemBioChem, 6(6), 982-985. https://doi.org/10.1002/cbic.200400394
On the biodegradation of <I>β</I>-peptides
Schreiber, J. V., Frackenpohl, J., Moser, F., Fleischmann, T., Kohler, H. P. E., & Seebach, D. (2002). On the biodegradation of β-peptides. ChemBioChem, 3(5), 424-432. https://doi.org/10.1002/1439-7633(20020503)3:5<424::AID-CBIC424>3.0.CO;2-0