A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli.

Abstract:

: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 FK 506 binding proteins currently known. The specificity constant kcat/Km 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 microM, 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Rahfeld JU,Schierhorn A,Mann K,Fischer G

doi

10.1016/0014-5793(94)80608-x

subject

Has Abstract

pub_date

1994-04-18 00:00:00

pages

65-9

issue

1

eissn

0014-5793

issn

1873-3468

journal_volume

343

pub_type

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