The specificity of prolyl endopeptidase from Flavobacterium meningoseptum: Mapping the S' subsites by positional scanning via acyl transfer

Article abstract of DOI:10.1016/S0968-0896(98)00145-X

The S₁'-S₃' subsite specificity of prolyl endopeptidase from Flavobacterium meningoseptum was studied by acyl transfer to libraries of amino acid amides and peptides. Whereas the S₁' and S₃' subsites influence the specificity for the amino component by approximately one order of magnitude, the S₂' subsite possesses a markedly higher specificity. Besides the high specificity for hydrophobic residues at P₁'-P₃', proline was efficiently bound by the S₂' and S₃' subsites of the enzyme. In contrast, no binding of P₁' proline-containing peptides was observed. It could be demonstrated that the specificity of the S' subsite is not restricted to l-amino acids. Effective P'-S' interactions were also found for β- and γ-amino acids indicating that the enzyme does not form close contacts to the backbone of P₁' and P₂' amino acid residues. Copyright (C) 1998 Elsevier Science Ltd.