[46] Interconversion of apo- and holofatty acid synthetases of rat and pigeon liver

Burton, David N.; Sobhy, C.M.; Jenik, Robert A.; Porter, John W.

doi:10.1016/0076-6879(79)62226-7

Cited by 5 publications

(2 citation statements)

References 19 publications

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“…Next, the 5'-AMP moiety of ATP is added to form dephospho-CoA, which is subsequently phosphorylated on the 3'-hydroxyl to form CoA. CoA serves as the 4'-phosphopantetheine donor in the biogenesis of ACP (7,13,23). E. coli, in contrast to mammals, is capable of synthesizing pantothenate (6) via the condensation of pantoic acid and /1-alanine (18).…”

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confidence: 99%

Regulation of coenzyme A biosynthesis

Jackowski¹,

Rock²

1981

J Bacteriol

233

149

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Coenzyme A (CoA) and acyl carrier protein are two cofactors in fatty acid metabolism, and both possess a 4'-phosphopantetheine moiety that is metabolically derived from the vitamin pantothenate. We studied the regulation of the metabolic pathway that gives rise to these two cofactors in an Escherichia coli ,B-alanine auxotroph, strain SJ16. Identification and quantitation of the intracellular and extracellular f.-alanine-derived metabolites from cells grown on increasing 8l-alanine concentrations were performed. The intracellular content of acyl carrier protein was relatively insensitive to ,B-alanine input, whereas the CoA content increased as a function of external ,B-alanine concentration, reaching a maximum at 8 ,M ,B-alanine. Further increase in the fl-alanine concentration led

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confidence: 99%

Regulation of coenzyme A biosynthesis

Jackowski¹,

Rock²

1981

J Bacteriol

233

149

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“…This finding was demonstrated experimentally by the studies of Yu and Burton (84). Then, two 4'-phosphopantetheine prosthetic groups are covalently bound to the enzyme (85). It appears from the work of Lornitzo and Porter*** that this occurs by separate processes, and that two separate enzymes may be required for this process.…”

Section: Fatty Acid Synthetasementioning

confidence: 99%

Induction of fatty acid synthetase and acetyl-CoA carboxylase by isolated rat liver cells

Porter¹,

Swenson²

1983

Enzyme Induction and Modulation

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SummaryCurrent studies on the synthesis of long-chain fatty acids by isolated rat liver cells are largely concerned with the regulation of the activity of previously existing acetyl-CoA carboxylase and fatty acid synthetase, and with the regulation of the quantity of these enzymes. These studies have required the development of methods for obtaining high yields of viable hepatocytes that respond to hormonal treatment. Such methods have been developed over the past 10-15 years through the efforts of several laboratories. These studies ha ve also required the development of a method to determine whether a change in the activity of an enzyme is due to a modification of preexisting enzyme or to a change in quantity of that enzyme. The most satisfactory method to use for such studies is immunotitration of enzyme activity.In recent years studies on the regulation of acetyl-CoA carboxylase have largely centered upon the effect of phosphorylation-dephosphorylation on the activity of this enzyme and whether glucagon inhibits the activity of this enzyme through this process. Much data from a number oflaboratories have suggested that glucagon regulates the activity ofthis enzyme through phosphorylation-dephosphorylation. However, several ofthese studies involved the use of crude systems in which competing enzymes and substrates that can significantly interfere with acetyl-CoA carboxylase activity measurements were still present. Hence, a confirmation of these studies needs to be carried out under conditions in which the effects of competing enzymes and substrates are eliminated.Studies on changes in quantity of acetyl-CoA carboxylase and ratty acid synthetase have shown that these enzymes are induced by the fasting and refeeding of animals. They have also shown that insulin stimulates (10-to 3D-fold) the induction ofthese enzymes. This induction appears to be due to a change in the quantity of translatable mRNA which may, in turn, be due to a change in the rate of transcription of the genes coding for these enzymes.

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Induction of fatty acid synthetase and acetyl-CoA carboxylase by isolated rat liver cells

Porter

Swenson

1983

Mol Cell Biochem

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Current studies on the synthesis of long-chain fatty acids by isolated rat liver cells are largely concerned with the regulation of the activity of previously existing acetyl-CoA carboxylase and fatty acid synthetase, and with the regulation of the quantity of these enzymes. These studies have required the development of methods for obtaining high yields of viable hepatocytes that respond to hormonal treatment. Such methods have been developed over the past 10-15 years through the efforts of several laboratories. These studies have also required the development of a method to determine whether a change in the activity of an enzyme is due to a modification of preexisting enzyme or to a change in quantity of that enzyme. The most satisfactory method to use for such studies is immunotitration of enzyme activity. In recent years studies on the regulation of acetyl-CoA carboxylase have largely centered upon the effect of phosphorylation-dephosphorylation on the activity of this enzyme and whether glucagon inhibits the activity of this enzyme through this process. Much data from a number of laboratories have suggested that glucagon regulates the activity of this enzyme through phosphorylation-dephosphorylation. However, several of these studies involved the use of crude systems in which competing enzymes and substrates that can significantly interfere with acetyl-CoA carboxylase activity measurements were still present. Hence, a confirmation of these studies needs to be carried out under conditions in which the effects of competing enzymes and substrates are eliminated. Studies on changes in quantity of acetyl-CoA carboxylase and fatty acid synthetase have shown that these enzymes are induced by the fasting and refeeding of animals. They have also shown that insulin stimulates (10- to 30-fold) the induction of these enzymes. This induction appears to be due to a change in the quantity of translatable mRNA which may, in turn, be due to a change in the rate of transcription of the genes coding for these enzymes.

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[46] Interconversion of apo- and holofatty acid synthetases of rat and pigeon liver

Cited by 5 publications

References 19 publications

Regulation of coenzyme A biosynthesis

Regulation of coenzyme A biosynthesis

Induction of fatty acid synthetase and acetyl-CoA carboxylase by isolated rat liver cells

Induction of fatty acid synthetase and acetyl-CoA carboxylase by isolated rat liver cells

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