Energy transduction at the catalytic site of enzymes: Hydrolysis of phosphoester bonds and synthesis of pyrophosphate by alkaline phosphatase

FEBS Letters

Nayudu, Ramachandra V.¹  de Meis, Leopoldo¹ 

[1] Instituto de Ciencias Biomedicas, Departamento de Bioquimica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21910, Brazil

关键词: Energy transduction;    Catalytic site;    Alkaline phosphatase;    Mops;    4-morpholinepropanesulfonic acid;    Mes;    2-(N-morpholino)ethanesulfonic acid;   

DOI  :  10.1016/0014-5793(89)81082-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Alkaline phosphatase from mouse intestinal epithelial cells catalyzes the synthesis of pyrophosphate from P_i during hydrolysis of either glucose 6-phosphate, ATP, ADP, inorganic pyrophosphate or p-nitrophenylphosphate. The rate of pyrophosphate synthesis is increased by MgCl₂ and by decreasing the pH of the medium from 8.5 to 6.0. The data presented indicate that at the catalytic site of alkaline phosphatase the energies of hydrolysis of the phosphoserine residue and of pyrophosphate are different from those measured in aqueous solutions.

【 授权许可】

Unknown