Influence of Subunit Interface Mutations on Kinetic and Dynamic Properties of Alkaline Phosphatase from E. coli

Croatica Chemica Acta

Pavela-Vrančić, Maja¹  Soldo, Barbara¹  Bučević-Popović, Viljemka¹  Orhanović, Stjepan¹  Šprung, Matilda¹ 

[1] Department of Chemistry, Faculty of Science, University of Split, N. Tesle 12, HR-21000 Split, Croatia

关键词: room temperature phosphorescence;    acrylamide quenching;    kinetic properties;    protein dynamics;    subunit interface;   

DOI  :  

学科分类：化学（综合）

来源: Croatica Chemica Acta

【 摘 要 】

Mutations, replacing amino acids involved in the formation of hydrogen bonds between subunits of dimeric alkaline phosphatase, have been introduced. Influence of mutations on kinetic properties and structural stability of mutant enzymes...

【 授权许可】

Unknown