Reference: Stoops JK and Wakil SJ (1978) The isolation of the two subunits of yeast fatty acid synthetase. Biochem Biophys Res Commun 84(1):225-31

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Abstract


The two subunits that comprise the yeast fatty acid synthetase (designated alpha and beta) have been isolated. The separation was performed using DEAE Biogel A chromatography after first treating yeast fatty acid synthetase with 3,4,5,6 tetrahydrophthalic anhydride. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the fractions eluted from the ion exchange column indicated that the separation of the subunits was essentially complete. It was possible to remove the 3,4,5,6 tetrahydrophthalate derivative from the subunits and regenerate certain of the partial activities. The alpha subunit was found to have the beta-keto reductase activity as well as the acyl carrier protein component associated with it. The beta subunit had the acetyl and malonyl transacylases and the palmitoyl transferase activity associated with it. The different extent to which the malonyl and acetyl transacylase activities were regained indicated that these two catalytic sites have separate domains in the beta subunit.

Reference Type
Journal Article | Research Support, U.S. Gov't, Non-P.H.S. | Research Support, U.S. Gov't, P.H.S.
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Stoops JK, Wakil SJ
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