The Enzymatic Function of Tafazzin

Tafazzin is a putative enzyme that is involved in cardiolipin metabolism, it may carry mutations responsible for Barth syndrome. To identify the biochemical reaction catalyzed by tafazzin, we expressed the full-length isoform of Drosophila melanogaster tafazzin in a baculovirus-Sf9 insect cell syste...

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Bibliographic Details
Published in:The Journal of biological chemistry 2006-12, Vol.281 (51), p.39217-39224
Main Authors: Xu, Yang, Malhotra, Ashim, Ren, Mindong, Schlame, Michael
Format: Article
Language:English
Subjects:
1-Acylglycerophosphocholine O-Acyltransferase - chemistry
1-Acylglycerophosphocholine O-Acyltransferase - physiology
Acylation
Animals
Baculoviridae - metabolism
Cardiolipins - metabolism
Cell Line
Drosophila Proteins - chemistry
Drosophila Proteins - physiology
Gene Expression Regulation, Enzymologic
Insecta
Mitochondria - metabolism
Models, Chemical
Phosphatidylcholines - chemistry
Phospholipids - chemistry
Protein Binding
Substrate Specificity
Time Factors
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Summary:Tafazzin is a putative enzyme that is involved in cardiolipin metabolism, it may carry mutations responsible for Barth syndrome. To identify the biochemical reaction catalyzed by tafazzin, we expressed the full-length isoform of Drosophila melanogaster tafazzin in a baculovirus-Sf9 insect cell system. Tafazzin expression induced a new enzymatic function in Sf9 cell mitochondria, namely 1-palmitoyl-2-[14C]linoleoyl-phosphatidylcholine:monolysocardiolipin linoleoyltransferase. We also found evidence for the reverse reaction, because tafazzin expression caused transfer of acyl groups from phospholipids to 1-[14C]palmitoyl-2-lyso-phosphatidylcholine. An affinity-purified tafazzin construct, tagged with the maltose-binding protein, catalyzed both forward and reverse transacylations between cardiolipin and phosphatidylcholine, but was unable to utilize CoA or acyl-CoA as substrates. Whereas tafazzin supported transacylations between various phospholipid-lysophospholipid pairs, it showed the highest rate for the phosphatidylcholine-cardiolipin transacylation. Transacylation activities were about 10-fold higher for linoleoyl groups than for oleoyl groups, and they were negligible for arachidonoyl groups. The data show that Drosophila tafazzin is a CoA-independent, acyl-specific phospholipid transacylase with substrate preference for cardiolipin and phosphatidylcholine.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M606100200