Tightly bound pyrophosphate in Escherichia coli inorganic pyrophosphatase

FEBS Letters

Shestakov, Alexander A.¹  Avaeva, Svetlana M.¹  Baykov, Alexander A.¹ 

[1] A.N.Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, and Department of Chemistry, Moscow State University, Moscow 119899, USSR

关键词: Inorganic pyrophosphatase;    Pyrophosphate synthesis;    Active site;    Enzyme-substrate interaction;    (Escherichia coli);   

DOI  :  10.1016/0014-5793(90)80187-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hexameric inorganic pyrophosphatase of Escherichia coli contains about 1 of ‘structural’ pyrophosphate, which survives gel nitration and prolonged incubation with Mg²⁺, does not exchange with medium phosphate and pyrophosphate but is removed with 0.8 M perchloric acid. The site of pyrophosphate binding seems to be another than the active site. An additional 0.9 mol of enzyme-bound pyrophosphate is formed in the presence of phosphate and Mg²⁺ but this pyrophosphate is in fast equilibrium with medium phosphate and appears to be bound to the active site.

【 授权许可】

Unknown