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Coenzyme-A-Independent Transacylation System; Possible Involvement of Phospholipase A2 in Transacylation
Atsushi Yamashita1, Yasuhiro Hayashi2, Naoki Matsumoto3
1Faculty of Pharma-Sciences, Teikyo University, 2-11-1 Kaga, Itabashi-Ku, Tokyo 173-8605, Japan. ayamashi@pharm.teikyo-u.ac.jp.
Biology
|March 31, 2017
Summary
The CoA-independent transacylation system transfers fatty acids, especially arachidonic acid, without coenzyme A (CoA). This membrane-bound system is crucial for lipid metabolism but its enzymes remain unidentified.
Area of Science:
- Biochemistry
- Lipid Metabolism
Background:
- The coenzyme A (CoA)-independent transacylation system facilitates fatty acid transfer between phospholipids and lysophospholipids.
- This system preferentially utilizes C20 and C22 polyunsaturated fatty acids, such as arachidonic acid, esterified at the *sn*-2 position of glycerophospholipids.
Purpose of the Study:
- To review the characteristics of the calcium-independent, membrane-bound CoA-independent transacylation system.
- To highlight its selectivity for arachidonic acid and discuss its physiological significance.
- To explore potential enzymatic mechanisms, including the role of phospholipase A2.
Main Methods:
- Literature review of CoA-independent transacylation.
- Analysis of substrate specificity and reaction conditions.
- Speculative discussion on enzyme identification.
Main Results:
- The CoA-independent transacylation system operates without cofactors like CoA.
- It shows a strong preference for arachidonic acid and other long-chain polyunsaturated fatty acids.
- The system is involved in acylating alkyl ether-linked lysophospholipids and enriching arachidonic acid in these lipids.
Conclusions:
- The CoA-independent transacylation system plays a vital role in the metabolism of eicosanoids and platelet-activating factor.
- The specific enzymes catalyzing these reactions are yet to be identified.
- Phospholipase A2 is a potential candidate enzyme involved in this transacylation process.