Specificity of prolyl endopeptidase

FEBS Letters

Nomura, Kohji¹ 

[1] Department of Biochemistry, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakaecho, Itabashiku, Tokyo-173, Japan

关键词: Prolyl endopeptidase;    Primary specificity;    Synthetic substrate;    Hyp;    hydroxyproline;    Sar;    sarcosyi or N-Me-Gly;    Abu;    α-aminobutyryl;    Aib;    α-aminoisobutyryl;    Pip;    pipecolyl;    Cbz;    N-α-benzyloxycarbonyl;    Bz;    N-α-benzoyl;    Bzl;    benzyl;    MCA;    4-methylcoumaryl-7-amide;    Suc;    succinyl;   

DOI  :  10.1016/0014-5793(86)81118-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown