The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin

Dorothee Kern; Torbjörn Drakenberg; Mats Wikström; Sture Forsén; Holger Bang; Gunter Fischer

doi:10.1016/0014-5793(93)81338-Z

The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin

Dorothee Kern
, Torbjörn Drakenberg
, Mats Wikström
, Sture Forsén
, Holger Bang
, Gunter Fischer

VTT Technical Research Centre of Finland

Research output: Contribution to journal › Article › Scientific › peer-review

42 Citations (Scopus)

Abstract

The cytosolic peptidyl‐prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One‐ and two‐dimensional ¹H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide.

Original language	English
Pages (from-to)	198-203
Journal	FEBS Letters
Volume	323
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(93)81338-Z
Publication status	Published - 1993
MoE publication type	A1 Journal article-refereed

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title = "The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin",

abstract = "The cytosolic peptidyl‐prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One‐ and two‐dimensional 1H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide. ",

author = "Dorothee Kern and Torbj{\"o}rn Drakenberg and Mats Wikstr{\"o}m and Sture Fors{\'e}n and Holger Bang and Gunter Fischer",

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T1 - The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin

AU - Kern, Dorothee

AU - Drakenberg, Torbjörn

AU - Wikström, Mats

AU - Forsén, Sture

AU - Bang, Holger

AU - Fischer, Gunter

PY - 1993

Y1 - 1993

N2 - The cytosolic peptidyl‐prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One‐ and two‐dimensional 1H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide.

AB - The cytosolic peptidyl‐prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One‐ and two‐dimensional 1H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide.

U2 - 10.1016/0014-5793(93)81338-Z

DO - 10.1016/0014-5793(93)81338-Z

M3 - Article

SN - 0014-5793

VL - 323

SP - 198

EP - 203

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin

Abstract

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