title: Anhydrosubtilisin-catalyzed peptide synthesis.
abstract: Anhydrosubtilisin was found to be a good catalyst for the peptide synthesis though its hydrolytic activity was fully inhibited. Amino acid (peptide) p-chlorophenyl ester (acyl donor) was coupled with amino acid (peptide) amide in the presence of the modified enzyme. The method did not afford by-products resulting from the hydrolysis of the acyl donor. This is the most advantageous characteristic of the method, since the hydrolysis of the acyl donor is unavoidable for the methods using catalytically active proteases. Anhydrosubtilisin was further shown to be useful for the fragment condensation of peptides.
authors.affiliation: Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Tanizawa
authors.forename: A
authors.initials: A
authors.lastname: Sugimura
authors.forename: Y
authors.initials: Y
authors.lastname: Kanaoka
mesh_terms: D000581:Amidohydrolases; D000595:Amino Acid Sequence; D002384:Catalysis; D004950:Esterases; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D013381:Subtilisins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D004950:Esterases; D013381:Subtilisins; C072607:anhydrosubtilisin; D000581:Amidohydrolases