Calcium ion binding by thermitase

FEBS Letters

Frömmel, Cornelius¹  Briedigkeit, Lutz¹ 

[1] Research Department, Bereich Medizin der Humboldt-Universität zu Berlin, Schumannstr. 20/21, GDR-1040 Berlin, GDR

关键词: Bacterial protease;    Thermitase;    Subtilisin;    Ca2+ binding;    Stability;    pNPA;    p-nitrophenyl acetate;    SCB;    subtilisin Carlsberg;    TRM;    thermitase;   

DOI  :  10.1016/0014-5793(89)80935-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Thermitase is a thermostable member of the subtilisin protease family. It was found that this enzyme binds very strongly one calcium ion. This metal ion cannot be removed without denaturation by any known method. A second binding site for calcium ions can be depleted partially by gel filtration, similar to the strong binding site of subtilisin Carlsberg. In both enzymes the calcium ion bound to this site can be removed completely using Ca²⁺ chelating reagent. In thermitase and subtilisin Carlsberg, depleting calcium ions from any binding site results in a significant decrease of stability against autolysis.

【 授权许可】

Unknown