Abstract
In recent years, the molecular organization of the plant fatty acid synthetases has been examined in extracts from various plant tissues, and in all cases was found to be nonassociated and similar to the prokaryotic type of E. coli (1, 2, 3). Many of the individual component enzymes have been partially purified including malonyl-CoAracyl carrier protein (ACP) transacylase (4), β-ketoacyl-ACP reductase (5, 6), (β-hydroxylacyl-ACP dehydrase (6), enoyl ACP reductase (5, 6) and acetyl-CoA: ACP transacylase (ATA) (1). ATA has the lowest specific activity in comparison with the other enzymes in the system and has been reported as catalyzing the rate-limiting step in the plant fatty acid synthetase (FAS) system: the thioester transfer reaction between acetyl-CoA and acyl carrier protein to form acetyl-ACP.
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