title: Substrate mimetics and freezing strategy: a useful combination that broadens the scope of proteases for synthesis.
abstract: [reaction: see text] We present an irreversible and efficient protease-based method for peptide synthesis which occurs independently of the primary specificity of proteases and also without proteolytic side reactions. The key feature of this approach is the combination of the substrate mimetics strategy with frozen state enzymology. Model reactions catalyzed by several proteases qualify this approach as a powerful concept in the direction of a more universal application of proteases as biocatalysts for peptide ligation.
authors.affiliation: Max-Planck-Society, Research Unit "Enzymology of Protein Folding", Weinbergweg 22, D-06120 Halle/Saale, Germany.
authors.forename: N
authors.initials: N
authors.lastname: Wehofsky
authors.forename: S W
authors.initials: SW
authors.lastname: Kirbach
authors.forename: M
authors.initials: M
authors.lastname: Haensler
authors.forename: J D
authors.initials: JD
authors.lastname: Wissmann
authors.forename: F
authors.initials: F
authors.lastname: Bordusa
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D002918:Chymotrypsin / Q000737:chemistry; D010450:Endopeptidases / Q000737:chemistry*; D005615:Freezing; D010455:Peptides / Q000138:chemical synthesis*; D013696:Temperature; D014357:Trypsin / Q000737:chemistry
chemical_list: D000596:Amino Acids; D010455:Peptides; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin