A novel peptidyl‐prolyl cisltrans isomerase from Escherichia coli

FEBS Letters

Mann, Karlheinz²  Schierhorn, Angelika³  Rahfeld, Jens-U.¹  Fischer, Gunter¹ 

[1] Max-Planck-Gesellschaft, Arbeitsgruppe “Enzymologie der Peptidbindung”, Weinbergweg 16a, D-06120 Halle/Saale, Germany;Max-Planck-Institut für Biochemie, Am Klopferspitz, D-82152 Martinsried, Germany;Martin-Luther-Universität Halle-Wittenberg, Lehrstuhl für Molekulare Biochemie, Weinbergweg 16a, D-06120 Halle/Saale, Germany

关键词: Escherichia coli: Peptidyl-prolyl cis/trans isomerase;    FK506;    Cyclosporin A;    Proline;   

DOI  :  10.1016/0014-5793(94)80608-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel peptidyl-prolyl cis/trans isomerase was isolated from Escherichia coli cell extract and characterized partially. Determination of the molecular mass by electrospray mass spectrometry indicated a protein of 10102 ± 2 Da, smaller than cyclophilins or FK506 binding proteins currently known. The specificity constant k _cat/K _m determined with Succinyl-Ala-Xaa-Pro-Phe-4-nitroanilide (Xaa = Leu) had a value comparable to those from cyclophilins from the same organism. However, the pattern of subsite specificity (Xaa = Gly, Ala, Val, Ile, Leu, Phe, Trp, His, Lys and Glu) was reminiscent of FK506 binding peptidyl-prolyl cis/trans isomerases. The enzyme activity was not inhibited by cyclosporin A or FK506 at inhibitor concentrations of < 5 μM, concentrations that affect most bacterial peptidyl-prolyl cis/trans isomerases. Computer-assisted analysis of 21 amino acid residues of the N-terminus determined by Edman degradation revealed no homology to known peptidyl-prolyl cis/trans isomerases.

【 授权许可】

Unknown