Differential effect of phosphatidylethanolamine molecular species on glycerophosphate acyltransferase activity of Escherichia coli.
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The effect of phosphatidylethanolamine (PE) molecular species on the reconstitution of partially purified glycerophosphate acyltransferase of Escherichia coli was investigated. The acyltransferase activity was abolished by 1, 2-di-unsaturated (U-U) PE, but not by 1-saturated-2-unsaturated (S-U) PE or 1-saturated-2-cyclopropanoyl PE. Since both the U-U and S-U PE used in the present work are in a fluid state at temperatures above about 30°C, the differential effect cannot be accounted for in terms of the membrane fluidity. Therefore, the inactivation of the reconstituted enzyme was attributed to the large amount of the 1, 2-di-cis-vaccenoyl species of PE.
- 社団法人 日本生化学会の論文
社団法人 日本生化学会 | 論文
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