Peptidyl-prolyl cis-trans isomerase activity as studied by dynamic proton NMR spectroscopy.
Recently the identity of the peptidyl-prolyl cis-trans isomerase (PPIase), which accelerates the cis/trans isomerization of prolyl peptide bonds and cyclophilin, the binding protein for the immunosuppressive drug Cyclosporin A (CsA), was discovered. The PPIase catalysis toward the substrate Suc-Ala-Phe-Pro-Phe-pNA has been studied by 1H NMR spectroscopy. Using the bandshape analysis technique the rate of interconversion between the cis and trans isomers of the substrate could be measured in the presence of PPIase and under equilibrium conditions. The acceleration is inhibited by equimolar amounts of CsA. The results provide evidence that the PPIase catalysis is more complex than a simple exchange between two states.
Hübner
D
D
Department of Biochemistry, Martin-Luther-University, Halle, Germany.
Drakenberg
T
T
Forsén
S
S
Fischer
G
G
D000591:Amino Acid Isomerases / Q000378:metabolism*; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D019696:Peptidylprolyl Isomerase; D013379:Substrate Specificity
D002352:Carrier Proteins; D009842:Oligopeptides; C069564:succinimidyl-alanyl-phenylalanyl-prolyl-phenylalanine 4-nitroanilide; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase