Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by HOMMA, H.
Right arrow Articles by NOJIMA, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by HOMMA, H.
Right arrow Articles by NOJIMA, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1987, Vol. 101, No. 4 1033-1039
© 1987 Japanese Biochemical Society

other

Characteristics of Phospholipid Transacylase of Escherichia coli1

Hiroshi HOMMA2, Ichiro KUDO, Keizo INOUE and Shoshichi NOJIMA3

Faculty of Pharmaceutical Sciences, The University of Tokyo Bunkyo-ku, Tokyo 113

2Present address: Kyoritsu College of Pharmacy, Minato-ku, Tokyo 105.

3 Present address:Faculty of Pharmaceutical sciences, Teikyo University, sagamiko, Kanagawa 199–01

We have previously demonstrated the activity(ies) of phospholipid transacylase in Escherichia coli extract (Homma & Nojima (1982) J. Biochem. 91, 1093–1101), which catalyzed a new type of reaction of acyl transfer from diacylphospholipids to lysophospholipids. In this communication we report the specificities and characteristics of this enzyme activity. The activity catalyzed a reversible transfer of an acyl group between diacylphospholipids and lysophospholipids. The acyl group in the 1-position of the glycerol backbone was selectively transferred, and palmitic acid was the only fatty acid species transferred. Presumably, neutral lipids do not serve as substrates. The transacylase was firmly associated with the envelope fraction of E. coli. Neither potassium chloride nor urea was effective in solubilization of the activity and only about half of the activity was solubilized with Triton X-100. This observation was consistent with the equal distribution of the activity between the outer membrane and the inner membrane of E. coli. Functional aspects of this phospholipid transacylase are also discussed.

1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.