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J. Biochem, 1982, Vol. 91, No. 4 1093-1101
© 1982 Japanese Biochemical Society

research-article

Transacylation between Diacylphospholipids and 2-Acyl Lysophospholipids Catalyzed by Escherichia coli Extract1

Hiroshi HOMMA and Shoshichi NOJIMA

Department of Health Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113

When 2-acyl lysophosphatidylethanolamine, 2-acyl lysophosphatidyiglycerol, and 2-acyl lysophosphatidyicholine were incubated with the envelope fraction of Escherichia coil in the presence of Mg2+ ion, they were acylated to the corresponding diacylphospholipids. The inner and outer membrane fractions both had acylation activity. 2-Acyl lysophosphatidylethanolamine was shown to be acylated at the 1-position by an endogenous acyl donor present in the envelope fraction. Under the conditions used, acylation was specific for 2-acyl lysophosphatidylethanolamine, and the 1-acyl isomer was not appreciably acylated.

The acylation was resistant to N-ethylmaleimide and p-chloromercuribenzoate, but was inhibited by Cu2+ and Hg2+ ions. Ca2+ and Mg2+ ions stimulated the activity about 1.5-fold, but EDTA was not inhibitory. The activity had a broad pH optimum between 6 and 8. On boiling the envelope fraction, about 55% of the activity was lost rapidly, while the remainder was lost gradually.

The endogenous acyl donor present in the envelope fraction was shown to be membrane phospholipids. The acylation was not observed with free fatty acids prepared by alkaline hydrolysis of the phospholipids. Studies with purified phospholipids showed that the major phospholipids of E. coil (phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin) and phosphatidic acid acted as acyl donors. Thus, transacylation between diacylphospholipids and 2-acyl lysophospholipids catalyzed by E. coil envelopes was demonstrated.

1This work was supported in part by Grant-in-Aid (Nos. 56118006 and 56370034) for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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