Diastereoselective reduction of protein‐bound methionine sulfoxide by methionine sulfoxide reductase

FEBS Letters

Schöneich, Christian²  Squier, Thomas C.¹  Sharov, Victor S.²  Ferrington, Deborah A.¹ 

[1] Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA;Department of Pharmaceutical Chemistry, University of Kansas, 2095 Constant Avenue, Lawrence, KS 66047, USA

关键词: Calmodulin;    Oxidative stress;    Hydrogen peroxide;    Methionine sulfoxide;    Peptide methionine sulfoxide reductase;    Diastereoselectivity;   

DOI  :  10.1016/S0014-5793(99)00888-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D-sulfoxide diastereomer of CaM-bound L-MetSO (L-Met-D-SO). After exhaustive reduction by pMSR, the ratio of L-Met-D-SO to L-Met-L-SO decreased to about 1:25 for hydrogen peroxide-oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR.

【 授权许可】

Unknown