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Biochemistry|March 23, 1993
Significance of hydrophobic S4-P4 interactions in subtilisin 309 from Bacillus lentusL M Bech, S B Sørensen, K BreddamEuropean Journal of Biochemistry|November 1, 1992
Mutational replacements in subtilisin 309. Val104 has a modulating effect on the P4 substrate preferenceL M Bech, S B Sørensen, K BreddamBiochemistry|September 7, 1993
Mutational replacements of the amino acid residues forming the hydrophobic S4 binding pocket of subtilisin 309 from Bacillus lentusS B Sørensen, L M Bech, M Meldal, et al.Carlsberg Research Communications|January 1, 1989
Inactivation of carboxypeptidase Y by mutational removal of the putative essential histidyl residueL M Bech, K BreddamCarlsberg Research Communications|January 1, 1988
Chemical modifications of a cysteinyl residue introduced in the binding site of carboxypeptidase Y by site-directed mutagenesisL M Bech, K BreddamProtein Science : a Publication of the Protein Society|October 23, 1997
The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocketS B Sørensen, K BreddamCarlsberg Research Communications|January 1, 1989
Primary structure of carboxypeptidase III from malted barleyS B Sørensen, I Svendsen, K BreddamFEBS Letters|February 3, 1992
Introduction of a free cysteinyl residue at position 68 in the subtilisin Savinase, based on homology with proteinase KL M Bech, S Branner, S Hastrup, et al.FEBS Letters|December 9, 1991
Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acidS B Sørensen, T L Sørensen, K BreddamEuropean Journal of Biochemistry|December 27, 1990
A highly active and oxidation-resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modificationH Grøn, L M Bech, S Branner, et al.Pageof 6