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A novel peptidyl‐prolyl cisltrans isomerase from Escherichia coli
Author(s) -
Rahfeld Jens-U.,
Schierhorn Angelika,
Mann Karlheinz,
Fischer Gunter
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80608-x
Subject(s) - isomerase , edman degradation , fkbp , escherichia coli , chemistry , cis trans isomerases , peptidylprolyl isomerase , biochemistry , prolyl isomerase , enzyme , stereochemistry , peptide sequence , pin1 , gene
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.