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Specificity of prolyl endopeptidase
Author(s) -
Nomura Kohji
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81118-8
Subject(s) - chemistry , enzyme kinetics , stereochemistry , proline , prolyl endopeptidase , endopeptidase , pyrrolidine , residue (chemistry) , substrate (aquarium) , enzyme , active site , biochemistry , amino acid , biology , ecology
A series of tetrapeptides, Cbz(Bz)‐Gly‐X‐Leu‐Gly, were synthesized and the kinetic parameters, k cat and, determined for their hydrolyses by prolyl endopeptidase from Flavobacterium . The peptides with X = N ‐Me‐Ala, Sar and Ala as well as the standard substrate (X = Pro) were found to be good substrates, while those with X = α‐aminobutyryl, Hyp, Ser and Gly were poor substrates, and those with X = pipecolyl, α‐aminoisobutyryl, N ‐Me‐Val, N ‐Me‐Leu, Hyp(O‐Bzl) and Ser(O‐Bzl) were not cleaved at all. These results suggest that the specificity‐determining site or Sl subsite of the enzyme is designed to fit exactly the proline residue of the substrate with allowance for the residues carrying substituents at the N and/or C α which must not exceed the size of the pyrrolidine ring of proline.