Coenzyme-A-Independent Transacylation System; Possible Involvement of Phospholipase A2 in Transacylation

The coenzyme A (CoA)-independent transacylation system catalyzes fatty acid transfer from phospholipids to lysophospholipids in the absence of cofactors such as CoA. It prefers to use C20 and C22 polyunsaturated fatty acids such as arachidonic acid, which are esterified in the glycerophospholipid at...

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Bibliographic Details
Published in:Biology (Basel, Switzerland) Switzerland), 2017-03, Vol.6 (2), p.23
Main Authors: Yamashita, Atsushi, Hayashi, Yasuhiro, Matsumoto, Naoki, Nemoto-Sasaki, Yoko, Koizumi, Takanori, Inagaki, Yusuke, Oka, Saori, Tanikawa, Takashi, Sugiura, Takayuki
Format: Article
Language:English
Subjects:
Arachidonic acid
Calcium
catalytic activity
Coenzyme A
Cofactors
Eicosanoids
Enzymes
esterification
lipid metabolism
Phospholipase A2
Phospholipids
Platelet-activating factor
Polyunsaturated fatty acids
Review
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Summary:The coenzyme A (CoA)-independent transacylation system catalyzes fatty acid transfer from phospholipids to lysophospholipids in the absence of cofactors such as CoA. It prefers to use C20 and C22 polyunsaturated fatty acids such as arachidonic acid, which are esterified in the glycerophospholipid at the -2 position. This system can also acylate alkyl ether-linked lysophospholipids, is involved in the enrichment of arachidonic acid in alkyl ether-linked glycerophospholipids, and is critical for the metabolism of eicosanoids and platelet-activating factor. Despite their importance, the enzymes responsible for these reactions have yet to be identified. In this review, we describe the features of the Ca -independent, membrane-bound CoA-independent transacylation system and its selectivity for arachidonic acid. We also speculate on the involvement of phospholipase A2 in the CoA-independent transacylation reaction.
ISSN:2079-7737
2079-7737
DOI:10.3390/biology6020023