Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.4.1.2 (acetyl-CoA carboxylase)
 2,876 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two cAMP-independent acetyl-CoA carboxylase (ACC) protein kinases have been partially purified from rat liver cytosol and microsomal extracts. The first kinase, present in greatest activity in microsomal extracts, appears to be identical to casein kinase I by characteristic molecular size on gel filtration (Mr 40,000) and sodium dodecyl sulfate-gel electrophoresis (Mr 34,000), autophosphorylation of this single subunit, inability to efficiently utilize GTP, and resistance to inhibition by heparin and 2,3-diphosphoglycerate. The second kinase, predominant in cytosol, appears to be identical to casein kinase II by characteristic molecular size on gel filtration (Mr 150,000), an autophosphorylated subunit of Mr 25,000, a Km for GTP nearly equal to that of ATP, inhibition by heparin and 2,3 DPG, and relative substrate specificity. Despite the incorporation of up to 2 mol 32P/mol carboxylase subunit (kinase I) and 0.6 mol/subunit (kinase II), phosphorylation by either kinase causes no change in carboxylase activity. The site(s) phosphorylated by each kinase and by the cAMP-dependent protein kinase on carboxylase appear to be clustered on a Mr 16,000 cyanogen bromide peptide that is readily released on incubation with trypsin. The potential roles of these kinases in the regulation of ACC remain to be clarified.
Arch Biochem Biophys 1983 Dec
PMID:Phosphorylation of acetyl-coenzyme A carboxylase by casein kinase I and casein kinase II. 614 63

The development of the lipogenic capacity in brown adipose tissue was studied in suckling lean (Fa/fa) and obese (fa/fa) Zucker pups aged from 7 to 22 days. In both lean and obese pups, activities of the two key lipogenic enzymes, fatty acid synthetase and acetyl-CoA carboxylase, and of citrate cleavage enzyme rose from the early to the late suckling period. Compared with lean pups, 7-day-old fa/fa pups showed a 35% increase in fat accumulation in interscapular brown adipose tissue and a 25% increase in fatty acid synthetase activity. By 10 days of age, fat deposition, lipogenesis in vivo (assessed by the incorporation of 3H from 3H2O into fatty acids) and fatty acid synthetase activity were 1.5-2-fold higher in pre-obese than in lean pups. Compared with lean pups, the increased lipogenesis in vivo observed in brown adipose tissue of 10-day-old pre-obese pups could not entirely account for the difference in fat deposition observed in this tissue, suggesting that additional mechanisms are at play to explain the increased fat content of this tissue.
Biochem J 1983 Dec 15
PMID:Development of fatty acid-synthetic capacity in interscapular brown adipose tissue during suckling in genetically obese Zucker rats. 614 88

When rats adapted to a stock diet were fed on various high-carbohydrate diets, the hepatic activities of glucose-6-phosphate dehydrogenase, malic enzyme and acetyl-CoA carboxylase were more greatly increased by fructose than by any other carbohydrate. Even in the diabetic state, the enzyme activities were somewhat increased by fructose feeding. After feeding on the diets for 9 days, the hepatic concentrations of intermediates of carbohydrate metabolism were generally lower in the diabetics than in the normals. Moreover, in both the normal and diabetic rats, the concentrations of fructose-1-phosphate, acetyl-CoA, citrate and malate were increased by fructose as were the enzyme activities. These results suggest that the metabolic pathway of fructose is predominant with respect to that of glucose and consequently lipogenesis may be able to be increased in the fructose-fed rats.
J Nutr Sci Vitaminol (Tokyo) 1983 Dec
PMID:Effects of high-fructose diet on lipogenic enzymes and their substrate and effector levels in diabetic rats. 614 42

The subcellular distribution of acetyl-CoA carboxylase [acetyl-CoA-carbon dioxide ligase (ADP-forming), EC 6.4.1.2] was determined in mesophyll protoplasts isolation from barley, a C3 plant, and sorghum, a C4 plant. In both species, all of the mesophyll acetyl-CoA carboxylase was demonstrated to be chloroplastic. In barley leaves and mesophyll protoplasts, a single biotinyl protein of 60,000 Da was identified by a modified Western-blotting procedure. The subcellular distribution of this biotinyl protein was identical to that found for acetyl-CoA carboxylase. These results are discussed in relation to the compartmentation of reactions requiring malonyl-CoA as a substrate.
Arch Biochem Biophys 1984 Dec
PMID:Subcellular distribution of acetyl-coenzyme A carboxylase in mesophyll cells of barley and sorghum leaves. 615 78

Octanoate and N6,O2'-dibutyryl adenosine 3',5'-monophosphate (dibutyryl cyclic AMP) cause a marked inhibition of net glucose utilization and lactate and pyruvate accumulation by hepatocytes isolated from meal-fed rats. Acetate is much less effective as an inhibitor of glycolysis. Fatty acid synthesis, as measured by tritiated water incorporation, is inhibited by dibutyryl cyclic AMP, whereas it is stimulated by 10 mM acetate and 1 mM octanoate. Stimulation of fatty acid synthesis by 1 mM octanoate, however, is lost paradoxically at higher concentrations of octanoate. Rates of fatty acid synthesis estimated by [1-14C]octanoate incorporation were consistently higher than rates calculated on the basis of tritiated water incorporation, raising the question as to which is the better index of the rate of de novo fatty acid synthesis. The effects of octanoate were studied because it was reasoned that this fatty acid should not inhibit acetyl-CoA carboxylase but should inhibit glycolysis and supply acetyl-CoA for lipogenesis. This was found to be the case, proving that glycolytic activity is not necessary for rapid rates of de novo fatty acid synthesis by liver.
Biochim Biophys Acta 1983 Dec 20
PMID:Effects of octanoate and acetate upon hepatic glycolysis and lipogenesis. 631 44

Swine were fed corn- or barley-based diets with, or without, culture filtrate (CF) of Trichoderma viride for 21 days. Weight gains were nonsignificantly but slightly increased by CF. The activities of beta-hydroxy-beta-methylglutaryl coenzyme A (HMG-CoA) reductase, cholesterol 7 alpha-hydroxylase, acetyl-CoA carboxylase (ACX), fatty acid synthetase (FAS) and other lipogenic enzymes in several tissues were determined. Significant decreases in the activities of HMG-CoA reductase and cholesterol 7 alpha-hydroxylase in all tissues of swine fed the CF-diets were observed. The major site for the regulation of cholesterol biosynthesis was adipose tissue followed by the intestine, liver, lung and muscle in order of activity. The concentrations of cholesterol in serum and muscle were decreased 27% and 23%, respectively, by CF. ACX and FAS activities increased ca. 2-fold when CF was fed with either of the cereal-based diets. The major sites for fatty acid synthesis was the adipose tissue and, to a lesser extent, the liver. Very low rates of synthesis were detected in intestine, lung and muscle. Similar distributions of activities were found for related lipogenic enzymes.
Lipids 1982 Dec
PMID:Effects of cereals and culture filtrate of Trichoderma viride on lipid metabolism of swine. 689 42

Various physical fractions of the barley kernel were fed to one-day-old female and male chickens to determine their effect on hepatic beta-hydroxy-beta-methylglutaryl coenzyme A (HMG-CoA) reductase, cholesterol 7 alpha-hydroxylase and the lipogenic enzymes, acetyl-CoA carboxylase (ACX), malic enzyme (ME), citrate-cleavage enzyme (CCE) and fatty acid synthetase (FAS) at the subcellular level. Significant inhibition (p less than 0.01) of cholesterol biosynthesis accompanied by significant decreases in plasma cholesterol concentrations and induction of fatty acid synthesis were found in diets based on pearled barley, barley pearlings and a high-protein barley flour (HPBF: aleurone and subaleurone layers of barley endosperm) separated from the pearlings when compared to corn. Lower weight gains in 1- to 4-week-old birds fed the high-protein barley flour were found to be the result of lower feed consumption; pair feeding of 12-week-old birds with diets based on corn and high-protein barley flour produced equal weight gains in both treatments and significant reductions in hepatic HMG-CoA reductase, plasma cholesterol and induction in several lipogenic enzymes in birds fed the high-protein barley flour. Substitutions of 5-20% high-protein barley flour for corn in a corn-based diet produced significant weight gains (p less than 0.01) of 10 to 20% in 2-week-old chickens, inhibited cholesterol biosynthesis by 45-65% and produced a 3-fold increase in a fatty acid synthetase. The results indicate that HPBF contains an inhibitor(s) of cholesterol biosynthesis and a growth factor(s) when compared to a corn-based diet.
Lipids 1982 Dec
PMID:Effects of different fractions of the barley kernel on the hepatic lipid metabolism of chickens. 716 70

We previously isolated a mutant of Escherichia coli that is preferentially affected in the synthesis of rRNA and has a mutation in the gene (accD) encoding a subunit of acetyl-CoA carboxylase. Using this mutant and other mutants of the pathway for fatty acid and phospholipid biosynthesis as well as cerulenin, a specific inhibitor of fatty acid synthesis, we show that (i) inhibition of fatty acid synthesis in the presence of both a carbon source and all 20 amino acids stimulates the accumulation of guanosine tetraphosphate (ppGpp) and leads to preferential inhibition of rRNA synthesis, (ii) this ppGpp accumulation is spoT dependent, and (iii) the generation of the metabolic signal that stimulates this spoT-mediated response probably does not depend on either phospholipid starvation or a significant reduction in the level of ATP.
Proc Natl Acad Sci U S A 1993 Dec 01
PMID:spoT-dependent accumulation of guanosine tetraphosphate in response to fatty acid starvation in Escherichia coli. 750 90

The genes encoding two subunits of acetyl coenzyme A carboxylase, biotin carboxyl carrier protein, and biotin carboxylase have been cloned from Bacillus subtilis. DNA sequencing and RNA blot hybridization studies indicated that the B. subtilis accB homolog which encodes biotin carboxyl carrier protein, is part of an operon that includes accC, the gene encoding the biotin carboxylase subunit of acetyl coenzyme A carboxylase.
J Bacteriol 1995 Dec
PMID:The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis. 759 99

1. The activity of the lipogenic enzyme, acetyl-CoA carboxylase, was investigated in four insect species; Bombyx mori (Lepidoptera), Tenebrio molitor (Coleoptera), Glossina morsitans and Sarcophaga nodosa (Diptera). 2. Acetyl-CoA carboxylase activity in larval, pupal and adult forms was compared with the saponifiable lipid mass at each stage of the life-cycle, and found to follow similar patterns except for Tenebrio molitor. 3. The results are examined in relation to known metabolic requirements for each insect.
Comp Biochem Physiol B 1993 Dec
PMID:Insect acetyl-CoA carboxylase: activity during the larval, pupal and adult stages of insect development. 790 74


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