Effect of divalent cations on the ATPase activity of Escherichia coli SecA

FEBS Letters

Kim, Hyoungman¹  Ahn, Taeho¹  Kim, Joon-Sik¹  Ko, Junsang¹  Park, Chankyu¹ 

[1]Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Kusong-Dong, Yusong-Gu, Taejon 305-701, South Korea

关键词: SecA;    Intrinsic ATPase activity;    Calcium ion;    Magnesium ion;    8-Anilino-1-naphthalene-sulfonic acid binding;    NBS;    nucleotide binding site;    pRBP;    precursor form of ribose binding protein;    IMV;    inverted membrane vesicle;    Pi;    inorganic phosphate;    ANS;    8-anilino-1-naphthalene-sulfonic acid;    T m;    the midpoint temperature of the thermal denaturation curve;   

DOI  :  10.1016/S0014-5793(01)02265-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It was found that Ca²⁺ stimulates the intrinsic SecA ATPase activity in the absence as well as in the presence of liposome. On the other hand, Mg²⁺, the general cofactor for ATPase, did not affect the intrinsic SecA ATPase but reduced the portion of ATPase activity enhanced by Ca²⁺. The enhancement of SecA ATPase activity correlated well with the increase in 8-anilino-1-naphthalene-sulfonic acid binding of SecA, suggesting that increased exposure of hydrophobic residues stimulates the enzyme activity.

【 授权许可】

Unknown