scholarly journals Fluazifop, a grass-selective herbicide which inhibits acetyl-CoA carboxylase in sensitive plant species

1988 ◽  
Vol 254 (1) ◽  
pp. 307-310 ◽  
Author(s):  
K A Walker ◽  
S M Ridley ◽  
T Lewis ◽  
J L Harwood
Keyword(s):  
Fatty Acid ◽  
Hordeum Vulgare ◽  
De Novo ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Acetyl Coa Carboxylase ◽  
Sensitive Species ◽  
Acetyl Coa ◽  
Different Types ◽  
Selective Herbicide

Fluazifop is a grass-selective herbicide that appears to act by inhibiting fatty acid synthesis de novo in sensitive species. Results from four different types of experiment show that this inhibition is due to an action of fluazifop on acetyl-CoA carboxylase and not on fatty acid synthetase. The acetyl-CoA carboxylase from sensitive barley (Hordeum vulgare), but not from resistant pea (Pisum sativum), is inhibited by the R stereoisomer, a finding that agrees with the herbicidal specificity of fluazifop.

scholarly journals Chronic ethanol administration depresses fatty acid synthesis in rat adipose tissue

1988 ◽  
Vol 251 (2) ◽  
pp. 547-551 ◽  
Author(s):  
J S Wilson ◽  
M A Korsten ◽  
L P Donnelly ◽  
P W Colley ◽  
J B Somer ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Chronic Ethanol ◽  
Ethanol Administration ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Chronic Ethanol Administration

Administration of ethanol as part of a nutritionally adequate liquid diet to female Wistar rats was found to depress markedly incorporation of labelled glucose into adipose-tissue acylglycerol fatty acids. Similar results with labelled pyruvate and acetate suggested inhibition of the fatty-acid-synthesis pathway at, or distal to, the acetyl-CoA carboxylase step. Activities of acetyl-CoA carboxylase and fatty acid synthetase were markedly lower in ethanol-fed animals. The activity of another lipogenic enzyme, phosphatidate phosphohydrolase, was not affected by chronic ethanol feeding. These findings suggest that chronic ethanol administration has marked effects on adipose-tissue lipogenesis.

scholarly journals Differential effects of 2-oxo acids on pyruvate utilization and fatty acid synthesis in rat brain

1974 ◽  
Vol 140 (1) ◽  
pp. 25-29 ◽  
Author(s):  
John B. Clark ◽  
John M. Land
Keyword(s):  
Fatty Acid ◽  
Pyruvate Dehydrogenase ◽  
Citrate Synthase ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Synthetase Activity ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Carboxylase Activity ◽  
Old Rats

1. The effects of 2-oxo-4-methylpentanoate, 2-oxo-3-methylbutanoate and 2-oxo-3-methylpentanoate on the activity of pyruvate dehydrogenase (EC 1.2.4.1), citrate synthase (EC 4.1.3.7), acetyl-CoA carboxylase, (EC 6.4.1.2) and fatty acid synthetase derived from the brains of 14-day-old rats were investigated. 2. The pyruvate dehydrogenase enzyme activity was competitively inhibited by 2-oxo-3-methylbutanoate with respect to pyruvate with a Ki of 2.04mm but was unaffected by 2-oxo-4-methylpentanoate or 2-oxo-3-methylpentanoate. 3. The citrate synthase activity was inhibited competitively (with respect to acetyl-CoA) by 2-oxo-4-methylpentanoate (Ki~7.2mm) and 2-oxo-3-methylbutanoate (Ki~14.9mm) but not by 2-oxo-3-methylpentanoate. 4. The acetyl-CoA carboxylase activity was not inhibited significantly by any of the 2-oxo acids investigated. 5. The fatty acid synthetase activity was competitively inhibited (with respect to acetyl-CoA) by 2-oxo-4-methylpentanoate (Ki~930μm) and 2-oxo-3-methylpentanoate (Ki~3.45mm) but not by 2-oxo-3-methylbutanoate. 6. Preliminary experiments indicate that 2-oxo-4-methylpentanoate and 2-oxo-3-phenylpropionate (phenylpyruvate) significantly inhibit the ability of intact brain mitochondria from 14-day-old rats to oxidize pyruvate. 7. The results are discussed with reference to phenylketonuria and maple-syrup-urine disease. A biochemical mechanism is proposed to explain the characteristics of these diseases.

scholarly journals The effect of progesterone on prolactin stimulation of fatty acid synthesis, glycerolipid synthesis and lipogenic-enzyme activities in mammary glands of pseudopregnant rabbits, after explant culture or intraductal injection

1985 ◽  
Vol 231 (2) ◽  
pp. 321-328 ◽  
Author(s):  
P Martyn ◽  
I R Falconer
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Mammary Glands ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Physiological Concentration ◽  
Intraductal Injection ◽  
Glycerolipid Synthesis

The activities of lipogenic enzymes, such as acetyl-CoA carboxylase, fatty acid synthetase and glucose-6-phosphate dehydrogenase, and glycerolipid synthesis increased significantly in mammary explants of 11-day-pseudopregnant rabbits in response to prolactin, in the presence of near-physiological concentrations of insulin and corticosterone in culture. Increasing the concentration of progesterone in culture resulted in suppression of glycerolipid synthesis and activities of acetyl-CoA carboxylase and fatty acid synthetase, but not the pentose phosphate dehydrogenases. However, at near-physiological concentration of progesterone, only acetyl-CoA carboxylase activity was decreased. Injection of prolactin intraductally into 11-day-pseudopregnant rabbits stimulated glycerolipid synthesis, fatty acid synthesis and enzymes involved in fatty acid synthesis, after 3 days. Intraductal injection of progesterone separately or together with prolactin had no significant effect on basal or stimulated lipogenesis in mammary glands. Intramuscular injection of progesterone at 10 mg/day did not suppress fatty acid synthesis stimulated when prolactin was injected intraductally, but a significant inhibition was observed at a higher dose (80 mg/day).

scholarly journals Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase.

1996 ◽  
Vol 134 (4) ◽  
pp. 949-961 ◽  
Author(s):  
S Saitoh ◽  
K Takahashi ◽  
K Nabeshima ◽  
Y Yamashita ◽  
Y Nakaseko ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fission Yeast ◽  
Fatty Acid Synthesis ◽  
Fatty Acid Synthetase ◽  
Acid Synthesis ◽  
Temperature Sensitive ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Nuclear Structures ◽  
Yeast Mutants

Two fission yeast temperature-sensitive mutants, cut6 and lsd1, show a defect in nuclear division. The daughter nuclei differ dramatically in size (the phenotype designated lsd, large and small daughter). Fluorescence in situ hybridization (FISH) revealed that sister chromatids were separated in the lsd cells, but appeared highly compact in one of the two daughter nuclei. EM showed asymmetric nuclear elongation followed by unequal separation of nonchromosomal nuclear structures in these mutant nuclei. The small nuclei lacked electron-dense nuclear materials and contained highly compacted chromatin. The cut6+ and lsd1+ genes are essential for viability and encode, respectively, acetyl CoA carboxylase and fatty acid synthetase, the key enzymes for fatty acid synthesis. Gene disruption of lsd1+ led to the lsd phenotype. Palmitate in medium fully suppressed the phenotypes of lsd1. Cerulenin, an inhibitor for fatty acid synthesis, produced the lsd phenotype in wild type. The drug caused cell inviability during mitosis but not during the G2-arrest induced by the cdc25 mutation. A reduced level of fatty acid thus led to impaired separation of non-chromosomal nuclear components. We propose that fatty acid is directly or indirectly required for separating the mother nucleus into two equal daughters.

A novel acetyl-CoA carboxylase inhibitor reduces de novo fatty acid synthesis in HepG2 cells and rat primary hepatocytes

2007 ◽  
Vol 468 (1) ◽  
pp. 44-48 ◽  
Author(s):  
Yoshinori Sugimoto ◽  
Yoshimitsu Naniwa ◽  
Takayuki Nakamura ◽  
Hirotsugu Kato ◽  
Masanori Yamamoto ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Hepg2 Cells ◽  
De Novo ◽  
Acid Synthesis ◽  
Acetyl Coa Carboxylase ◽  
Primary Hepatocytes ◽  
Acetyl Coa ◽  
Rat Primary Hepatocytes

scholarly journals Docking of acetyl-CoA carboxylase to the plastid envelope membrane attenuates fatty acid production in plants

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Yajin Ye ◽  
Krisztina Nikovics ◽  
Alexandra To ◽  
Loïc Lepiniec ◽  
Eric T. Fedosejevs ◽  
...  
Keyword(s):  
Fatty Acid ◽  
De Novo ◽  
Acid Synthesis ◽  
Fine Tuning ◽  
Envelope Membrane ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Fatty Acid Production ◽  
Control Light ◽  
Plant Life Cycle

AbstractIn plants, light-dependent activation of de novo fatty acid synthesis (FAS) is partially mediated by acetyl-CoA carboxylase (ACCase), the first committed step for this pathway. However, it is not fully understood how plants control light-dependent FAS regulation to meet the cellular demand for acyl chains. We report here the identification of a gene family encoding for three small plastidial proteins of the envelope membrane that interact with the α-carboxyltransferase (α-CT) subunit of ACCase and participate in an original mechanism restraining FAS in the light. Light enhances the interaction between carboxyltransferase interactors (CTIs) and α-CT, which in turn attenuates carbon flux into FAS. Knockouts for CTI exhibit higher rates of FAS and marked increase in absolute triacylglycerol levels in leaves, more than 4-fold higher than in wild-type plants. Furthermore, WRINKLED1, a master transcriptional regulator of FAS, positively regulates CTI1 expression by direct binding to its promoter. This study reveals that in addition to light-dependent activation, “envelope docking” of ACCase permits fine-tuning of fatty acid supply during the plant life cycle.

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