Stereospecificity of hydrogen transfer by pyridine nucleotide-dependent enoyl reductases in fatty acid synthesis: Studies with enzymes obtained from developing castor bean seeds and Chlorella vulgaris

1978 ◽  
Vol 62 (2) ◽  
pp. 173-178 ◽  
Author(s):  
Brady Vick ◽  
Harry Beevers

1993 ◽  
Vol 48 (7-8) ◽  
pp. 616-622 ◽  
Author(s):  
Jochen Fuhrmann ◽  
Klaus-Peter Heise

Abstract The colorless embryos of Cuphea wrightii A. Gray accumulate capric (about 30%) and lauric acid (about 50%) in their storage lipids. Fractionation studies show that the capacities for the synthesis of these medium-chain fatty acids (MCFA) from [1-14C]acetate were strictly bound to intact plastids. These, in turn, obligately required the addition of ATP. ATP could partially be substituted by ADP. Reduction of the pyridine nucleotide pool, required for opti­mum MCFA formation within the plastids, was driven by glucose 6-phosphate. Under these conditions the plastids were capable of synthesizing MCFA like the intact tissue. The presence of CoA in the incubation medium induced acyl-CoA formation. The observed accumulation of unesterified capric and lauric acid in the absence of CoA suggests that acyl-ACP thioesterase activity is involved in the chain termination. Treatment with cerulenin led to an unexpectedly small reduction of total fatty acid synthesis while the chain elongation of capric acid was clearly inhibited. A similar accumulation of capric acid at the expense of longer chain fatty acids has been observed after replacing ATP by ADP. These findings implicate that even the condensing enzymes are involved in the control of chain ter­mination.


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