FEBS Letters | |
A novel peptidyl‐prolyl cisltrans isomerase from Escherichia coli | |
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
【 预 览 】
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