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嗜热细菌PS3的F1 - ATP酶在50%二甲基亚砜中合成与酶结合的ATP 。

The synthesis of enzyme-bound ATP by the F1-ATPase from the thermophilic bacterium PS3 in 50% dimethylsulfoxide.

作者信息

Yoshida M

出版信息

Biochem Biophys Res Commun. 1983 Aug 12;114(3):907-12. doi: 10.1016/0006-291x(83)90646-0.

DOI:10.1016/0006-291x(83)90646-0
PMID:6225432
Abstract

Purified TF1 (F1-ATPase from a thermophilic bacterium PS3) synthesizes enzyme-bound ATP from medium Pi and enzyme-bound ADP in the presence of 50% dimethylsulfoxide (DMSO). Once ATP was formed on the enzyme, it was not released even after removal of DMSO and Pi from the solution. The half maximal concentration of medium Pi for ATP synthesis was 1mM. The pH optimum for enzyme-bound ATP formation was about 6.5. Under the optimum conditions, a yield of up to 0.8 mol of ATP/mol of TF1 was obtained.

摘要

纯化的TF1（来自嗜热细菌PS3的F1 - ATP合酶）在50%二甲基亚砜（DMSO）存在的情况下，能利用培养基中的无机磷酸（Pi）和酶结合的二磷酸腺苷（ADP）合成酶结合的ATP。一旦在酶上形成ATP，即使从溶液中去除DMSO和Pi后，它也不会释放。ATP合成的培养基Pi半最大浓度为1毫摩尔。酶结合的ATP形成的最适pH约为6.5。在最佳条件下，每摩尔TF1可获得高达0.8摩尔ATP的产量。

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