scholarly journals Inhibition of plant fatty acid synthesis by nitroimidazoles

1981 ◽  
Vol 198 (1) ◽  
pp. 193-198 ◽  
Author(s):  
A V Jones ◽  
J L Harwood ◽  
M R Stratford ◽  
P K Stumpf
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Soluble Fraction ◽  
Acid Synthesis ◽  
Long Chain Fatty Acids ◽  
Reduction Potentials ◽  
Marked Inhibition ◽  
Mechanism Of Inhibition ◽  
Pea Seeds ◽  
Electron Reduction

1. The effect of the addition of a number of nitroimidazoles was tested on fatty acid synthesis by germinating pea seeds, isolated lettuce chloroplasts and a soluble fraction from pea seeds. 2. All the compounds tested had a marked inhibition on stearate desaturation by lettuce chloroplasts and on the synthesis of very-long-chain fatty acids by pea seeds. 3. In contrast, the effect of the drugs on total fatty acid synthesis from [14C]acetate in chloroplasts was related to the compound's electron reduction potentials. 4. Of the compounds used, only metronidazole had a marked inhibition on palmitate elongation in the systems tested. 5. The mechanism of inhibition of plant fatty acid synthesis by nitroimidazoles is discussed and the possible relevance of these findings to their neurotoxicity is suggested.

Discussion: Cellular location of fat synthesizing enzymes

1958 ◽  
Vol 149 (936) ◽  
pp. 420-420 ◽  
Keyword(s):  
Fatty Acid ◽  
Recent Work ◽  
Fatty Acid Synthesis ◽  
Phosphate Buffer ◽  
Soluble Fraction ◽  
Acid Synthesis ◽  
Intracellular Distribution ◽  
Mitochondrial Enzymes ◽  
Cellular Location

Dr P. McLean asked what were my ideas on the possible intracellular distribution of the two fatty-acid synthesizing systems that I had postulated and also what I thought of the recent work from Gurin’s laboratory, showing the solubilization of certain mitochondrial enzymes (concerned in fatty-acid synthesis) which occurs in the presence, but not in the absence, of phosphate buffer. In reply, I would say that my immediate and superficial impression is that the DPNH -utilizing system is located in the soluble fraction of the cell (obtained by centrifugation at 100000 x g for 1 h), whilst the TPNH -utilizing system is located in the microsomes. There appears to be no TPNH -utilizing system located in the soluble fraction.

scholarly journals Lipase-induced alterations of fatty acid synthesis by subcellular fractions from germinating pea (Pisum sativum L.)

1982 ◽  
Vol 204 (2) ◽  
pp. 463-470 ◽  
Author(s):  
J Sanchez ◽  
B R Jordan ◽  
J Kay ◽  
J L Harwood
Keyword(s):  
Fatty Acid ◽  
Total Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Microsomal Fraction ◽  
Soluble Fraction ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Phospholipase Activity ◽  
Pisum Sativum L ◽  
Malonyl Coa

1. The effect of exogenous lipases on fatty acid synthesis from [14C]malonyl-CoA by the microsomal and soluble fractions from germinating peas was studied. 2. Addition of phospholipase A2 or the lipase from Rhizopus arrhizus had no effect on total fatty acid synthesis by the soluble fraction but caused severe inhibition of that by the microsomal fraction. 3. The addition of enzymes with phospholipase activity particularly inhibited the microsomal stearate elongase. 4. Control studies indicated that the phospholipase-induced inhibition of fatty acid synthesis was due to the location of fatty acid synthetase, palmitate elongase and stearate elongase on the outside of the microsomal vesicles. 5. Experiments with a trypsin-like proteinase showed that approximately half the microsomal fatty acid synthesis was resistant to proteolysis. 6. Although addition of exogenous phospholipases had no effect on total fatty acid synthesis by the soluble fraction, it did increase alpha-hydroxylation of newly-formed palmitate and stearate. 7. The results provide further evidence for differences between the soluble and particulate fatty acid synthetase and palmitate elongase activities of germinating pea.

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