Reverse reaction of lysophosphatidylinositol acyltransferase. Functional reconstitution of coenzyme A-dependent transacylation system

The Journal of Biological Chemistry
Atsushi YamashitaKeizo Waku

Abstract

CoA-dependent transacylation activity in microsomes catalyzes the transfer of fatty acid between phospholipids and lysophospholipids in the presence of CoA without the generation of free fatty acid. We examined the mechanism of the transacylation system using partially purified acyl-CoA:lysophosphatidylinositol (LPI) acyltransferase (LPIAT) from rat liver microsomes to test our hypothesis that both the reverse and forward reactions of acyl-CoA:lysophospholipid acyltransferases are involved in the CoA-dependent transacylation process. The purified LPIAT fraction exhibited ATP-independent acyl-CoA synthetic activity and CoA-dependent LPI generation from PI, suggesting that LPIAT could operate in reverse to form acyl-CoA and LPI. CoA-dependent acylation of LPI by the purified LPIAT fraction required PI as the acyl donor. In addition, the combination of purified LPIAT and recombinant lysophosphatidic acid acyltransferase could reconstitute CoA-dependent transacylation between PI and phosphatidic acid. These results suggest that the CoA-dependent transacylation system consists of the following: 1) acyl-CoA synthesis from phospholipid through the reverse action of acyl-CoA:lysophospholipid acyltransferases; and 2) transfer of fatty a...Continue Reading

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Citations

Oct 11, 2008·Journal of Biochemistry·Saori OkaTakayuki Sugiura
May 30, 2013·Prostaglandins & Other Lipid Mediators·Atsushi YamashitaTakayuki Sugiura
Oct 23, 2016·Journal of Hepatology·Felix StickelMarsha Y Morgan
Oct 20, 2018·International Journal of Obesity : Journal of the International Association for the Study of Obesity·Giuseppina R UmanoSonia Caprio
Feb 8, 2020·Journal of Lipid Research·Sookyoung Jeon, Rotonya Carr

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