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Analytical Biochemistry|May 15, 1997
C-terminal incorporation of fluorogenic and affinity labels using wild-type and mutagenized carboxypeptidase YH R Stennicke, K Olesen, S B Sørensen, et al.Carlsberg Research Communications|January 1, 1988
Carboxypeptidase S-1 from Penicillium janthinellum: enzymatic properties in hydrolysis and aminolysis reactionsK BreddamEuropean Journal of Biochemistry|May 15, 1992
Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenchingK Breddam, M MeldalBiochemistry|October 7, 1997
Substrates with charged P1 residues are efficiently hydrolyzed by serine carboxypeptidases when S3-P1 interactions are facilitatedK Olesen, K BreddamEuropean Journal of Biochemistry|February 15, 1992
Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformisI Svendsen, K BreddamBiochemistry|December 5, 1995
Increase of the P1 Lys/Leu substrate preference of carboxypeptidase Y by rational design based on known primary and tertiary structures of serine carboxypeptidasesK Olesen, K BreddamBiochemistry|September 22, 1992
Interdependency of the binding subsites in subtilisinH Grøn, K BreddamAnalytical Biochemistry|May 15, 1991
Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsinM Meldal, K BreddamProtein Science : a Publication of the Protein Society|May 1, 1994
A conserved glutamic acid bridge in serine carboxypeptidases, belonging to the alpha/beta hydrolase fold, acts as a pH-dependent protein-stabilizing elementU H Mortensen, K BreddamArchives of Biochemistry and Biophysics|August 1, 1993
Application of quantitative structure-activity relationship modeling to the evaluation of the changes in enzymatic activity of carboxypeptidase Y upon chemical modificationsA Kanstrup, K Breddam, O BuchardtPageof 6