A NOVEL PEPTIDYL-PROLYL CIS/TRANS ISOMERASE FROM ESCHERICHIA-COLI

被引：144

作者：

RAHFELD, JU

SCHIERHORN, A

MANN, K

FISCHER, G

机构：

[1] MAX PLANCK GESELL,ARBEITSGRP ENZYMOL PEPTIDBINDUNG,D-06120 HALLE,GERMANY

[2] UNIV HALLE WITTENBERG,LEHRSTUHL MOLEK BIOCHEM,D-06120 HALLE,GERMANY

[3] MAX PLANCK INST BIOCHEM,D-82152 MARTINSRIED,GERMANY

来源：

FEBS LETTERS | 1994年 / 343卷 / 01期

关键词：

ESCHERICHIA COLI; PEPTIDYL-PROLYL CIS-TRANS-ISOMERASE; FK506; CYCLOSPORINE A; PROLINE;

D O I：

10.1016/0014-5793(94)80608-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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, ne, 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 mu M, 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.

引用

页码：65 / 69

页数：5

共 29 条

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