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Related Experiment Videos

The enzymatic function of tafazzin.

Yang Xu1, Ashim Malhotra, Mindong Ren

  • 1Departments of Anesthesiology and Cell Biology, New York University School of Medicine, New York, New York 10016, USA.

The Journal of Biological Chemistry
|November 4, 2006
PubMed
Summary

Tafazzin, an enzyme linked to Barth syndrome, acts as a CoA-independent phospholipid transacylase. It specifically transfers acyl groups between cardiolipin and phosphatidylcholine, crucial for cardiolipin metabolism.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Tafazzin is a protein implicated in cardiolipin metabolism and Barth syndrome.
  • Its precise biochemical function remained uncharacterized.

Purpose of the Study:

  • To elucidate the enzymatic activity of tafazzin.
  • To identify the specific biochemical reaction catalyzed by tafazzin.

Main Methods:

  • Expressed full-length Drosophila melanogaster tafazzin in a baculovirus-Sf9 insect cell system.
  • Utilized an affinity-purified, maltose-binding protein-tagged tafazzin construct.
  • Assayed transacylation activity between various phospholipids and lysophospholipids.

Main Results:

  • Tafazzin expression induced 1-palmitoyl-2-[14C]linoleoyl-phosphatidylcholine:monolysocardiolipin linoleoyltransferase activity.

Related Experiment Videos

  • Demonstrated CoA-independent, acyl-specific transacylation between cardiolipin and phosphatidylcholine.
  • Observed highest activity for linoleoyl group transfer, with preference for cardiolipin and phosphatidylcholine.

    • Conclusions:

    • Drosophila tafazzin functions as a CoA-independent acyl-specific phospholipid transacylase.
    • The enzyme preferentially catalyzes transacylations involving cardiolipin and phosphatidylcholine.
    • This activity is crucial for understanding cardiolipin metabolism and Barth syndrome pathogenesis.