Activity, tissue distribution and site‐directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1

FEBS Letters

Jung, Stephan¹  Hoshi, Toshinori²  Hansel, Alfred¹  Heinemann, Stefan H.¹  Kasperczyk, Hubert¹ 

[1] Molecular and Cellular Biophysics, Medical Faculty of the Friedrich Schiller University Jena, Drackendorfer St. 1, D-07747 Jena, Germany;Department of Physiology, University of Pennsylvania, Richards D100, 3700 Hamilton Walk, Philadelphia, PA 19104, USA

关键词: Methionine sulfoxide;    Reactive oxygen species;    Oxidative stress;    Posttranslational modification;    Potassium channel;    MetO;    M(O);    methionine sulfoxide;    MSR;    methionine sulfoxide reductase;    DTT;    dithiothreitol;    TRX;    thioredoxin;   

DOI  :  10.1016/S0014-5793(02)03171-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human CBS1 is a methionine sulfoxide reductase of type B (MSRB) as it specifically reduced Met-R-SO in peptides with dithiothreitol or the thioredoxin system as reductants. Mutation C169S in the active site completely abolished enzymatic activity, while mutation W110A only reduced activity and C105S had no effect. Like human MSRA, hCBS1 showed in vivo reducing activity coexpressed with the Drosophila ShC/B potassium channel in oocytes, by accelerating the overall inactivation time course. hCBS1-encoding mRNA is most abundant in muscle tissues, especially in the heart and thereby shows an expression pattern different to the human MSRA.

【 授权许可】

Unknown