A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.
A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.
An enzyme that, in the presence of ATP and COENZYME A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and ORTHOPHOSPHATE. This reaction represents an important step in fatty acid biosynthesis. This enzyme was formerly listed as EC 4.1.3.8.
A carboxy-lyase that catalyzes the decarboxylation of (S)-2-Methyl-3-oxopropanoyl-CoA to propanoyl-CoA. In microorganisms the reaction can be coupled to the vectorial transport of SODIUM ions across the cytoplasmic membrane.
Intracellular signaling protein kinases that play a signaling role in the regulation of cellular energy metabolism. Their activity largely depends upon the concentration of cellular AMP which is increased under conditions of low energy or metabolic stress. AMP-activated protein kinases modify enzymes involved in LIPID METABOLISM, which in turn provide substrates needed to convert AMP into ATP.
Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.
Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.
A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.
A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration.
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
An enzyme with high affinity for carbon dioxide. It catalyzes irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose. EC 4.1.1.31.
Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.
Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
An acetic acid ester of CARNITINE that facilitates movement of ACETYL COA into the matrices of mammalian MITOCHONDRIA during the oxidation of FATTY ACIDS.
A species of gram-negative bacteria and nitrogen innoculant of PHASEOLUS VULGARIS.
Inorganic compounds that contain magnesium as an integral part of the molecule.
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.
The rate dynamics in chemical or physical systems.
An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
An autosomal recessive metabolic disorder caused by absent or decreased PYRUVATE CARBOXYLASE activity, the enzyme that regulates gluconeogenesis, lipogenesis, and neurotransmitter synthesis. Clinical manifestations include lactic acidosis, seizures, respiratory distress, marked psychomotor delay, periodic HYPOGLYCEMIA, and hypotonia. The clinical course may be similar to LEIGH DISEASE. (From Am J Hum Genet 1998 Jun;62(6):1312-9)
S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
Ribulose substituted by one or more phosphoric acid moieties.
A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.
Derivatives of caprylic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated eight carbon aliphatic structure.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
Formation of an acetyl derivative. (Stedman, 25th ed)
An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.
A lipid cofactor that is required for normal blood clotting. Several forms of vitamin K have been identified: VITAMIN K 1 (phytomenadione) derived from plants, VITAMIN K 2 (menaquinone) from bacteria, and synthetic naphthoquinone provitamins, VITAMIN K 3 (menadione). Vitamin K 3 provitamins, after being alkylated in vivo, exhibit the antifibrinolytic activity of vitamin K. Green leafy vegetables, liver, cheese, butter, and egg yolk are good sources of vitamin K.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.
A deficiency in the activities of biotin-dependent enzymes (propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, and PYRUVATE CARBOXYLASE) due to one of two defects in BIOTIN metabolism. The neonatal form is due to HOLOCARBOXYLASE SYNTHETASE DEFICIENCY. The late-onset form is due to BIOTINIDASE DEFICIENCY.
Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.
Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A specific protein in egg albumin that interacts with BIOTIN to render it unavailable to mammals, thereby producing biotin deficiency.
Carbohydrates present in food comprising digestible sugars and starches and indigestible cellulose and other dietary fibers. The former are the major source of energy. The sugars are in beet and cane sugar, fruits, honey, sweet corn, corn syrup, milk and milk products, etc.; the starches are in cereal grains, legumes (FABACEAE), tubers, etc. (From Claudio & Lagua, Nutrition and Diet Therapy Dictionary, 3d ed, p32, p277)
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.

Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. (1/960)

The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-dependent enzyme that catalyzes the first committed step of fatty acid biosynthesis. In its functional cycle, this protein engages in heterologous protein-protein interactions with three distinct partners, depending on its state of post-translational modification. Apo-BCCP interacts specifically with the biotin holoenzyme synthetase, BirA, which results in the post-translational attachment of biotin to a single lysine residue on BCCP. Holo-BCCP then interacts with the biotin carboxylase subunit of acetyl-CoA carboxylase, which leads to the addition of the carboxylate group of bicarbonate to biotin. Finally, the carboxy-biotinylated form of BCCP interacts with transcarboxylase in the transfer of the carboxylate to acetyl-CoA to form malonyl-CoA. The determinants of protein-protein interaction specificity in this system are unknown. The NMR solution structure of the unbiotinylated form of an 87 residue C-terminal domain fragment (residue 70-156) of BCCP (holoBCCP87) and the crystal structure of the biotinylated form of a C-terminal fragment (residue 77-156) of BCCP from Escherichia coli acetyl-CoA carboxylase have previously been determined. Comparative analysis of these structures provided evidence for small, localized conformational changes in the biotin-binding region upon biotinylation of the protein. These structural changes may be important for regulating specific protein-protein interactions. Since the dynamic properties of proteins are correlated with local structural environments, we have determined the relaxation parameters of the backbone 15N nuclear spins of holoBCCP87, and compared these with the data obtained for the apo protein. The results indicate that upon biotinylation, the inherent mobility of the biotin-binding region and the protruding thumb, with which the biotin group interacts in the holo protein, are significantly reduced.  (+info)

A multisubunit acetyl coenzyme A carboxylase from soybean. (2/960)

A multisubunit form of acetyl coenzyme A (CoA) carboxylase (ACCase) from soybean (Glycine max) was characterized. The enzyme catalyzes the formation of malonyl CoA from acetyl CoA, a rate-limiting step in fatty acid biosynthesis. The four known components that constitute plastid ACCase are biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and the alpha- and beta-subunits of carboxyltransferase (alpha- and beta-CT). At least three different cDNAs were isolated from germinating soybean seeds that encode BC, two that encode BCCP, and four that encode alpha-CT. Whereas BC, BCCP, and alpha-CT are products of nuclear genes, the DNA that encodes soybean beta-CT is located in chloroplasts. Translation products from cDNAs for BC, BCCP, and alpha-CT were imported into isolated pea (Pisum sativum) chloroplasts and became integrated into ACCase. Edman microsequence analysis of the subunits after import permitted the identification of the amino-terminal sequence of the mature protein after removal of the transit sequences. Antibodies specific for each of the chloroplast ACCase subunits were generated against products from the cDNAs expressed in bacteria. The antibodies permitted components of ACCase to be followed during fractionation of the chloroplast stroma. Even in the presence of 0.5 M KCl, a complex that contained BC plus BCCP emerged from Sephacryl 400 with an apparent molecular mass greater than about 800 kD. A second complex, which contained alpha- and beta-CT, was also recovered from the column, and it had an apparent molecular mass of greater than about 600 kD. By mixing the two complexes together at appropriate ratios, ACCase enzymatic activity was restored. Even higher ACCase activities were recovered by mixing complexes from pea and soybean. The results demonstrate that the active form of ACCase can be reassembled and that it could form a high-molecular-mass complex.  (+info)

The Saccharomyces cerevisiae hyperrecombination mutant hpr1Delta is synthetically lethal with two conditional alleles of the acetyl coenzyme A carboxylase gene and causes a defect in nuclear export of polyadenylated RNA. (3/960)

In a screen for mutants that display synthetic lethal interaction with hpr1Delta, a hyperrecombination mutant of Saccharomyces cerevisiae, we have isolated a novel cold-sensitive allele of the acetyl coenzyme A (CoA) carboxylase gene, acc1(cs), encoding the rate-limiting enzyme of fatty acid synthesis. The synthetic lethal phenotype of the acc1(cs) hpr1Delta double mutant was only partially complemented by exogenous fatty acids. hpr1Delta was also synthetically lethal with a previously isolated, temperature-sensitive allele of ACC1, mtr7 (mRNA transport), indicating that the lethality of the acc1(cs) hpr1Delta double mutant was not allele specific. The basis for the interaction between conditional acc1 alleles and hpr1Delta was investigated in more detail. In the hpr1Delta mutant background, acetyl-CoA carboxylase enzyme activity was reduced about 15-fold and steady-state levels of biotinylated Acc1p and ACC1 mRNA were reduced 2-fold. The reduced Acc1p activity in hpr1Delta cells, however, did not result in an altered lipid or fatty acid composition of the mutant membranes but rendered cells hypersensitive to soraphen A, an inhibitor of Acc1p. Similar to mtr7, hpr1Delta and acc1(cs) mutant cells displayed a defect in nuclear export of polyadenylated RNA. Oversized transcripts were detected in hpr1Delta, and rRNA processing was disturbed, but pre-mRNA splicing appeared wild type. Surprisingly, the transport defect of hpr1Delta and acc1(cs) mutant cells was accompanied by an altered ring-shaped structure of the nucleolus. These observations suggest that the basis for the synthetic lethal interaction between hpr1Delta and acc1 may lie in a functional overlap of the two mutations in nuclear poly(A)+ RNA production and export that results in an altered structure of the nucleolus.  (+info)

Light-dependent changes in redox status of the plastidic acetyl-CoA carboxylase and its regulatory component. (4/960)

Plastidic acetyl-CoA carboxylase (ACCase; EC 6.4.1.2), which catalyses the synthesis of malonyl-CoA and is the regulatory enzyme of fatty acid synthesis, is activated by light, presumably under redox regulation. To obtain evidence of redox regulation in vivo, the activity of ACCase was examined in pea chloroplasts isolated from plants kept in darkness (dark-ACCase) or after exposure to light for 1 h (light-ACCase) in the presence or absence of a thiol-reducing agent, dithiothreitol (DTT). The protein level was similar for light-ACCase and dark-ACCase, but the activity of light-ACCase in the absence of DTT was approx. 3-fold that of dark-ACCase. The light-ACCase and dark-ACCase were activated approx. 2-fold and 6-fold by DTT respectively, indicating that light-ACCase was in a much more reduced, active form than the dark-ACCase. This is the first demonstration of the light-dependent reduction of ACCase in vivo. Measurement of the activities of ACCase, carboxyltransferase and biotin carboxylase in the presence and absence of DTT, and the thiol-oxidizing agent, 5, 5'-dithiobis-(2-nitrobenzoic) acid, revealed that the carboxyltransferase reaction, but not the biotin carboxylase reaction, was redox-regulated. The cysteine residue(s) responsible for redox regulation probably reside on the carboxyltransferase component. Measurement of the pH dependence of biotin carboxylase and carboxyltransferase activities in the ACCase suggested that both components affect the activity of ACCase in vivo at a physiological pH range. These results suggest that the activation of ACCase by light is caused partly by the pH-dependent activation of two components and by the reductive activation of carboxyltransferase.  (+info)

Phosphorylation control of cardiac acetyl-CoA carboxylase by cAMP-dependent protein kinase and 5'-AMP activated protein kinase. (5/960)

Acetyl-CoA carboxylase (ACC) is regarded in liver and adipose tissue to be the rate-limiting enzyme for fatty acid biosynthesis; however, in heart tissue it functions as a regulator of fatty acid oxidation. Because the control of fatty acid oxidation is important to the functioning myocardium, the regulation of ACC is a key issue. Two cardiac isoforms of ACC exist, with molecular masses of 265 kDa and 280 kDa (ACC265 and ACC280). In this study, these proteins were purified from rat heart and used in subsequent phosphorylation and immunoprecipitation experiments. Our results demonstrate that 5' AMP-activated protein kinase (AMPK) is able to phosphorylate both ACC265 and ACC280, resulting in an almost complete loss of ACC activity. Although cAMP-dependent protein kinase phosphorylated only ACC280, a dramatic loss of ACC activity was still observed, suggesting that ACC280 contributes most, if not all, of the total heart ACC activity. ACC280 and ACC265 copurified under all experimental conditions, and purification of heart ACC also resulted in the specific copurification of the alpha2 isoform of the catalytic subunit of AMPK. Although both catalytic subunits of AMPK were expressed in crude heart homogenates, our results suggest that alpha2, and not alpha1, is the dominant isoform of AMPK catalytic subunit regulating ACC in the heart. Immunoprecipitation studies demonstrated that specific antibodies for both ACC265 and ACC280 were able to coimmunoprecipitate the alternate isoform along with the alpha2 isoform of AMPK. Taken together, the immunoprecipitation and the purification studies suggest that the two isoforms of ACC in the heart exist in a heterodimeric structure, and that this structure is tightly associated with the alpha2 subunit of AMPK.  (+info)

Induction of lipogenesis during differentiation in a "preadipocyte" cell line. (6/960)

3T3-L1 fibroblasts differentiate in culture into cells having adipocyte character. This transition is accompanied by a 40- to 50-fold rise in the incorporation of [14C]acetate into triglyceride. The increase in lipogenic rate is exactly parallel to a coordinate rise in the activities of the key enzymes of the fatty acid biosynthetic pathway (ATP-citrate lyase, acetyl-CoA carboxylase, and fatty acid synthetase). Immunological studies indicate that the elevated acetyl-CoA carboxylase activity is the product of an increased cellular enzyme level.  (+info)

Structure and selectivity in post-translational modification: attaching the biotinyl-lysine and lipoyl-lysine swinging arms in multifunctional enzymes. (7/960)

The post-translational attachment of biotin and lipoic acid to specific lysine residues displayed in protruding beta-turns in homologous biotinyl and lipoyl domains of their parent enzymes is catalysed by two different ligases. We have expressed in Escherichia coli a sub-gene encoding the biotinyl domain of E.coli acetyl-CoA carboxylase, and by a series of mutations converted the protein from the target for biotinylation to one for lipoylation, in vivo and in vitro. The biotinylating enzyme, biotinyl protein ligase (BPL), and the lipoylating enzyme, LplA, exhibited major differences in the recognition process. LplA accepted the highly conserved MKM motif that houses the target lysine residue in the biotinyl domain beta-turn, but was responsive to structural cues in the flanking beta-strands. BPL was much less sensitive to changes in these beta-strands, but could not biotinylate a lysine residue placed in the DKA motif characteristic of the lipoyl domain beta-turn. The presence of a further protruding thumb between the beta2 and beta3 strands in the wild-type biotinyl domain, which has no counterpart in the lipoyl domain, is sufficient to prevent aberrant lipoylation in E.coli. The structural basis of this discrimination contrasts with other forms of post-translational modification, where the sequence motif surrounding the target residue can be the principal determinant.  (+info)

Volume overload hypertrophy of the newborn heart slows the maturation of enzymes involved in the regulation of fatty acid metabolism. (8/960)

OBJECTIVES: The purpose of this study was to determine the effect of volume overload hypertrophy in the newborn heart on the cardiac enzymes controlling fatty acid metabolism. BACKGROUND: Shortly after birth, a rise in 5'-adenosine monophosphate-activated protein kinase (AMPK) activity results in the phosphorylation and inhibition of acetyl coenzyme A (CoA) carboxylase (ACC), and a decline in myocardial malonyl CoA levels with increased fatty acid oxidation rates. Whether the early onset of hypertrophy in the newborn heart alters this maturational increase in fatty acid oxidation is unknown. METHODS: Newborn piglets underwent endovascular stenting of the ductus arteriosus on day 1 of life with a 4.5-mm diameter stent, resulting in a left to right shunt, and left ventricular (LV) volume loading. Left ventricular and right ventricular samples from fetal, newborn, three-week control and three-week stented animals were compared. RESULTS: Stenting resulted in echocardiographic evidence of volume overload and myocardial hypertrophy. In control animals, left ventricular ACC activity declined from 274 +/- 30 pmol/mg/min on day 1 to 115 +/- 12 after three weeks (p < 0.05), but did not display this maturation drop in hypertrophied hearts, remaining elevated (270 +/- 50 pmol/mg/min, p < 0.05). At three weeks, malonyl CoA levels remained 2.8-fold higher in hypertrophied hearts than in control hearts. In control hearts, LV AMPK activity increased 178% between day 1 and three weeks, whereas in hypertrophied hearts AMPK activity at three weeks was only 71% of control values, due to a significant decrease in expression of the catalytic subunit of AMPK. CONCLUSIONS: Early onset LV volume overload with hypertrophy results in a delay in the normal maturation of fatty acid oxidation in the newborn heart.  (+info)

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The activities of two lipogenic enzymes, acetyl-CoA carboxylase and fatty acid synthase, were determined in two transplantable mammary adenocarcinomas (13762 and R3230AC) carried by non-pregnant, pregnant and lactating rats, and in mammary tissue of control animals (non-tumour-carrying) of comparable physiological states. During mammary-gland differentiation of control or tumour-carrying animals, the activities of acetyl-CoA carboxylase and fatty acid synthase in the lactating gland increased by about 40-50-fold over the values found in non-pregnant animals. On the other hand, in tumours carried by lactating dams there were only modest increases (1.5-2-fold) in acetyl-CoA carboxylase and fatty acid synthase compared with the neoplasms carried by non-pregnant animals. On the basis of the Km values for different substrates and immunodiffusion and immunotitration data, the fatty acid synthase of neoplastic tissues appeared to be indistinguishable from the control mammary-gland enzyme. However, a ...
Acetyl-coenzyme A carboxylase α (ACC-alpha) is considered as the key regulatory enzyme in fatty acid biosynthesis. ACC-alpha gene is located on Caprine chromosome 11 and is polymorphic in many goat breeds. In the current study, we aimed to find possible single nucleotide polymorphisms (SNPs) in the exon 1 region of the ACC-alpha gene in Iranian Mahabadi goat breed. Genomic DNA was extracted from blood samples of 150 Mahabadi does. The exon 1 region of the ACC-alpha gene was amplified to produce a 390 bp fragment. The PCR products were analyzed by both polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) and polymerase chain reaction-single strand conformation polymorphism (PCR-SSCP) techniques. RFLP was performed utilizing HinfI endonuclease enzyme. No polymorphism was observed after digestion of the PCR products using HinfI. However, SSCP of the PCR products revealed two conformation patterns at the exon 1 region of goat ACC-alpha gene with frequencies of 86% and 14%,
Acetyl-CoA carboxylase (ACC) is a biotin carboxylase that catalyzes the ATP-dependent condensation of acetyl-CoA and carbonate to form malonyl-CoA. The malonyl-CoA produced by ACC serves two major physiologic functions. It is an essential and rate-limiting substrate for de novo lipogenesis (DNL), and it acts as an allosteric inhibitor of the enzyme carnitine-palmitoyl transferase I (CPT-1). Acetyl-CoA carboxylase (ACC) inhibitors offer significant potential for the treatment of type 2 diabetes mellitus (T2DM), hepatic steatosis, and cancer. Acetyl-CoA carboxylase (ACC) in mammals is encoded by two related enzymes ACC1 and ACC2, which catalyze the ATP dependent carboxylation of acetyl-CoA to form malonyl-CoA. ACC1 encodes a cytoplasmic isoform that is thought to be the predominant isoform controlling FASyn, whereas ACC2 is tethered to the mitochondrial outer membrane, where localized malonyl-CoA production blocks CPT-1 function to prevent fatty acids from entering the mitochondria to undergo ...
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Acetyl-CoA carboxylase is a biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis. The Escherichia coli enzyme is composed of a homodimeric biotin carboxylase, biotinylated biotin carboxyl carrier protein (BCCP), and an α2β2 heterotetrameric carboxyltransferase. Catalysis by acetyl-CoA carboxylase proceeds via two half-reactions. In the first half-reaction, biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to BCCP, to form carboxybiotin. In the second half-reaction, carboxyltransferase transfers the carboxyl group from carboxybiotin to acetyl-CoA to form malonyl-CoA. All biotin-dependent carboxylases are proposed to have a two-site ping-pong mechanism where the carboxylase and transferase activities are separate and do not interact. This posits two hypotheses: either biotin carboxylase and BCCP undergo the first half-reaction, BCCP dissociates, and then BCCP interacts with carboxyltransferase to
As the spread of antibiotic resistant bacteria steadily increases, there is an urgent need for new antibacterial agents. Because fatty acid synthesis is only used for membrane biogenesis in bacteria, the enzymes in this pathway are attractive targets for antibacterial agent development. Acetyl-CoA carboxylase catalyzes the committed and regulated step in fatty acid synthesis. In bacteria, the enzyme is composed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. Fragment-based screening revealed that amino-oxazole inhibits biotin carboxylase activity and also exhibits antibacterial activity against Gram-negative organisms. In this report, we redesigned previously identified lead inhibitors to expand the spectrum of bacteria sensitive to the amino-oxazole derivatives by including Gram-positive species. Using 9,411 small organic building blocks, we constructed a diverse combinatorial library of 1.2 × 108 amino-oxazole derivatives. A subset
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The process leading to the rise of acetyl-CoA carboxylase activity in rat mammary tissue after the onset of lactation was investigated. The kinetics of change in enzyme activity and enzyme immunotitratable with antibody against avian liver acetyl-CoA carboxylase were determined during the course of lactogenic differentiation. The antibody inactivates and specifically precipitates acetyl-CoA carboxylase from rat mammary tissue as well as that from chicken liver cytosol. Characterization of the immunoprecipitate of the mammary tissue carboxylase by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis reveals a single biotin-containing polypeptide of about 230000mol.wt. This molecular weight is approximately twice that reported for the avian liver enzyme. However, chicken liver cytosol prepared in the presence of trypsin inhibitor and subjected to immunoprecipitation gives rise to a biotin-containing subunit of 230000mol.wt. as determined by sodium dodecyl sulphate/polyacrylamide-gel ...
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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.
References for Abcams Recombinant Human Acetyl Coenzyme A carboxylase alpha protein (ab79625). Please let us know if you have used this product in your…
TY - JOUR. T1 - Resveratrol downregulates acetyl-CoA carboxylase α and fatty acid synthase by AMPK-mediated downregulation of mTOR in breast cancer cells. AU - Sahng, Wook Park. AU - Yoon, Sarah. AU - Moon, Jong Seok. AU - Park, Byeong Woo. AU - Kim, Kyung Sup. PY - 2008/11/21. Y1 - 2008/11/21. N2 - Overexpression of HER2 in breast cancer cells is considered to induce the expression of acetyl-CoA carboxylase α (ACACA) and fatty acid synthase (FASN) through activation of mammalian target of rapamycin (mTOR) signaling pathway. Resveratrol, a red wine polyphenol, has been shown to induce apoptosis in several cancers by interfering in several signaling pathways. Present study elucidated the mechanism by which resveratrol downregulates ACACA and FASN in breast cancer cells. Resveratrol activated AMP-activated protein kinase (AMPK) and downregulated mTOR in BT-474 cells. These effects of resveratrol were mimicked by AICAR, an AMPK activator, and exogenously expressed constitutively active AMPK, ...
Acetyl-CoA Carboxylase 1 antibody (acetyl-CoA carboxylase alpha) for ICC/IF, IHC-P, WB. Anti-Acetyl-CoA Carboxylase 1 pAb (GTX132081) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
ID ACACB_HUMAN Reviewed; 2458 AA. AC O00763; A6NK36; Q16852; Q1HEC1; Q6KE87; Q6KE89; Q6TY48; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 22-NOV-2017, entry version 179. DE RecName: Full=Acetyl-CoA carboxylase 2; DE EC=6.4.1.2 {ECO:0000269,PubMed:16854592, ECO:0000269,PubMed:20952656}; DE AltName: Full=ACC-beta; DE Includes: DE RecName: Full=Biotin carboxylase; DE EC=6.3.4.14; DE Flags: Precursor; GN Name=ACACB; Synonyms=ACC2, ACCB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=9099716; DOI=10.1074/jbc.272.16.10669; RA Abu-Elheiga L., Almarza-Ortega D.B., Baldini A., Wakil S.J.; RT Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, RT chromosomal mapping, and ...
Breast tumor recurrence and metastasis represent the main causes of cancer-related death in women, and treatments are still lacking. Here, we define the lipogenic enzyme acetyl-CoA carboxylase (ACC) 1 as a key player in breast cancer metastasis. ACC1 phosphorylation was increased in invading cells both in murine and human breast cancer, serving as a point of convergence for leptin and transforming growth factor (TGF) β signaling. ACC1 phosphorylation was mediated by TGFβ-activated kinase (TAK) 1, and ACC1 inhibition was indispensable for the elevation of cellular acetyl-CoA, the subsequent increase in Smad2 transcription factor acetylation and activation, and ultimately epithelial-mesenchymal transition and metastasis induction. ACC1 deficiency worsened tumor recurrence upon primary tumor resection in mice, and ACC1 phosphorylation levels correlated with metastatic potential in breast and lung cancer patients. Given the demonstrated effectiveness of anti-leptin receptor antibody treatment in ...
Acetyl-CoA carboxylase (ACC) regulates synthesis and oxidation of fatty acids, and mice lacking the ACC2 isoform are leaner than wild-type animals. Choi et al. further characterized whole-body energy metabolism and insulin sensitivity of Acc2-/- mice and obtained results supporting the possibility of ACC2 inhibitors as agents to treat obesity and type 2 diabetes. By monitoring activity of the animals, food consumption, and energy expenditure, the authors showed that Acc2-/- animals ate more food than did wild-type animals but were still leaner than the control animals. The Acc2-/- animals were also resistant to obesity brought on by eating a diet high in fats. These effects could be explained by the increase in energy expenditure that was observed in the knockout animals. Although oxidation of fats and of carbohydrates have been thought to be mutually exclusive (thus providing an explanation for insulin resistance observed in animals with excess fatty acids), Choi et al. found that oxidation of ...
Acetyl-CoA Carboxylase (ACC) regulates the metabolism of fatty acids. This enzyme catalzes the formation of Malonyl CoA through the irreversible carboxylation of acetyl C
M.R. Munday; Regulation of mammalian acetyl-CoA carboxylase. Biochem Soc Trans 1 October 2002; 30 (5): A101. doi: https://doi.org/10.1042/bst030a101c. Download citation file:. ...
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Complete information for ACACB gene (Protein Coding), Acetyl-CoA Carboxylase Beta, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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The effects of two preparations of highly purified human GH (hGH) on lipid metabolism were studied in the GH-deficient little mouse (50-60 days old). Marked decreases in incorporation of [14C]glucose into fatty acid and in the activity of acetyl-CoA carboxylase in the epididymal fat pads were observed after i.p. injection of hGH at a dose of 1·0μg/g body weight or after continuous infusion of hGH by osmotic minipump. The rate of glucose incorporation into fatty acid decreased from 107·0 ± 27·6 (s.e.m.) to 38·1 ± 19·6 μmol/g tissue per h after a single injection of hGH and from 174·1±28·5 to 56·3±20·3 μmol/g tissue per h after continuous infusion of hGH for 2 days. Activity of the lipogenic enzyme acetyl-CoA carboxylase was also reduced by more than 50% in the epididymal fat pad from hGH-treated mice in comparison with the corresponding control animals. Incubation of isolated fat pads with hGH (0·1 μg/ml) revealed similar inhibitory effects of the hormone on fatty acid synthesis ...
Polyclonal Antibody for studying acetyl-CoA carboxylase 1 (Ser80) phosphate/acetyl-CoA carboxylase 2 (Ser222) phosphate in the Metabolism research area.
putative acetyl-CoA carboxylase biotin carboxylase subunit [PokAC2] GTGTTCCGCACCGTCCTCGTCGCCAACCGGGGCGAGATCGCCCTGCGTGTCGCGCGCGCC TGCCGTGAACTGGGGATCAGGGTCGCCGTCGTGTACTCCACCGAGGACACCGACAGCGAG GTCGTGCGGTACGCCGACGAGGCGGTCCGCATCGGCCCGGGGTCGGCGCAGGCGAGCTAC CTCAGCATCCCCGCCGTCATCGAGGCCGCCCGGCGCGTCGGCGCGGACGCGATCCACCCC GGGTACGGATTCCTCTCCGAGAACGCCGACTTCGCCGAGGTGTGCGCGGCCGAGGGCATC ACCTTCATCGGCCCGCCCCCGGAGGTGATGGAGGCGCTGGGCGACAAGTCCACCTGCCGC GGCCTCATGGCCGACGCGGGGCTGCCCCTGCTGCCCGGCACGCTGGACCCCGTGTCGTCG CCGCGCGAGGCCGAGGCGTTCGCCGCCGAGATCGGCTACCCGGTGGTGGTGAAGGCGGTG GCCGGGGGCGGCGGCCGCGGGATCGGAGTGGCGCACTCGGCCGACGAGTTCCCCGCCGTC TACCGGGAGACGCGACGCCACGCCGCCGCCGTGTTCGGGGACGGCAGGGTCTATCTGGAG CGCTATCTGCAGTCCGCACGGCACGTGGAGATCCAGATACTCGCCGACCGCTTCGGCAAT GTGATCCATCTCGGCGAGCGCGACTGCTCGGTGCAGCGCCGCCATCAGAAGCTCATCGAG GAGACCCCGGCTCCCGGGCTGGACCGCGATGTGCTCGCCGCGATGGCGGAACACGCCGTG CAGGGAGCCAAGGCCGCCGGATACGTCGGCGCGGGGACCTTCGAGTTCCTGTACGACGAC AGCGGACGCTTCTACTTCATGGAGGTCAACTGCCGTATCCAGGTCGAGCATCCGGTCACA ...
TY - JOUR. T1 - The Solubility of Carbon-Dioxide in Mixtures of Water and Ethanol. AU - CARGILL, R W AU - MacPhee, Donald E. PY - 1981. Y1 - 1981. M3 - Article. SP - 232. JO - Journal of Chemical Research. JF - Journal of Chemical Research. SN - 0308-2342. IS - 8. ER - ...
TY - JOUR. T1 - CARBON-DIOXIDE FIXATION AND CONIDIATION IN FUSARIUM-CULMORUM GROWN IN CONTINUOUS CULTURE. AU - Larmour, R. AU - Marchant, R. PY - 1977. Y1 - 1977. M3 - Article. VL - 99. SP - 59. EP - 68. JO - Journal of General Microbiology. JF - Journal of General Microbiology. SN - 0022-1287. IS - MAR. ER - ...
The Nature Index tracks the affiliations of high-quality scientific articles. Updated monthly, the Nature Index presents research outputs by institution and country. Use the Nature Index to interrogate publication patterns and to benchmark research performance.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQRNGEGHTLPKT 1 - 70 PSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGTQGLEATDTNGLSSSARPQ 71 - 140 GQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAGSSRESTRKGSRASLGALSLEAYLTTGEA 141 - 210 ETRVPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIR 211 - 280 RWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAG 281 - 350 WGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK 351 - 420 RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIF 421 - 490 LMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGY 491 - 560 VSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGV 561 - 630 TPISFETPSNPPLARGHVIAARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQF 631 - 700 GHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPD 701 - 770 IMLGVVCGALNVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM 771 - 840 ...
The main function of Acetyl-CoA is to carry acyl groups or thioesters. It is the precursor to HMG CoA, an important part of cholesterol and ketone synthesis. It can also be found as a vital reagent in the synthesis of fatty acids and sterols, as well as the oxidation of fatty acids as well as the breaking down of many amino acids. [2] Acetyl-CoA is well known as the junction between Glycolysis and the Citric Acid Cycle as well as an essential component in balancing between carbohydrate and fat metabolism. Acetyl-CoA has also been a central metabolite that is involved in many metabolic transformations within the cell. The acetyl group of the acetyl-CoA is used to oxidize via the TCA cycle to reduce NAD+ and FAD to NADH and FADH2, respectively. These products are then used to fuel ATP production through the electron transport train. In May 2011, Ling Cai et al. found that Acetyl-Coa functioned as a carbon-source rheostat that signals the initiation of the cellular growth program by promoting the ...
PROJECT DESCRIPTION: Our gene of interest is accC gene from E. coli 0157:H7 accC gene is the biotin subunit of ACC enzyme which catalyze the biosynthesis of Malonyl CoA. Malonyl CoA controls the rate of fatty acid (Triacylglycerol) biosynthesis. TAG is the fatty acid i.e. used for the biofuel production.In this experiment we will identify if the overexpression of accC gene in E.coli might enhance the production of TAG. For this process we will clone our gene of interest in to plasmid pSB1A3 and transform it in host E. coli. We will do thin layer chromatography for the quantification of fatty acids. Source: Biology department of University of Northern Iowa� Media: Luria Broth� Gene: Acetyl CoA carboxylase biotin carboxylase (accC)� Accession #: NC_011353.1 Region: 4242644..4243993 total base pair- 1350� Introns: None because Bacteria does not have any introns. Bio-brick Compatibility: Compatible Plasmid used: Vector Plasmid pSB1A3 Promoter used:Part: BBa_J23100 ...
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The U.K. power sector could face as much as $2.3 billion a year in extra costs if the government continues to reduce the amount of carbon dioxide that businesses are allowed to emit, analysts said.
UCL Discovery is UCLs open access repository, showcasing and providing access to UCL research outputs from all UCL disciplines.
The World Wild Fund (WWF) last month issued organizations vision for 2050, drafted by 100 scientists and meteorologists in Geneva, Switzerland.
volume\ The CO{}2 concentration in the digestion rebwp8:Sludge digestion (anaerobic) gas is a measure of the stability of the digestion rebwp8:Sludge digestion (anaerobic) . It can be determined with a CO{}2 analyser, with a certain volume of digestion rebwp8:Sludge digestion (anaerobic) gas ...
March was the first month in modern records that levels of the heat-trapping gas exceeded 400 parts per million at sites across the entire globe.
FOSTER CITY, Calif.-(BUSINESS WIRE)-Gilead Sciences, Inc. (Nasdaq:GILD) today announced results from an open-label, proof-of-concept study evaluating GS-0976, an investigational inhibitor of Acetyl-CoA carboxylase (ACC), in patients with nonalcoholic steatohepatitis (NASH). The data, from ten patients treated with GS-0976 20 mg taken orally once daily for 12 weeks, indicated that treatment …. ...
Acetyl-CoA is a molecule that is broken down and used by the body for energy production. If the body has too much acetyl-CoA, it...
Respiration in plants refers to the cellular mechanism that involves complete combustion of glucose and oxygen into by-products like water, carbon-dioxide and physical enegy.
Free Essay: ENTERPRENEUR Financial Accounting - ACC 557 ENTERPRENEUR Describe the type of business you have created including: a. The product or service, and...
A pair of human lungs have around 600 million balloon-like structures called alveoli. These exchange the carbon-dioxide waste in your blood for oxygen!
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We studied the regulation of brain acetyl CoA carboxylase (ACC) activity during food deprivation and under the influence of hormones of glucose homeostasis: glucagon and insulin. Mice were deprived of food and water for time periods of 1, 3, 6, 9, 12 and 24 hours and were then allowed to re-feed for 5, 30 and 60 minutes. Mice that were deprived for up to 6 h, and then re-fed for 60 min, consumed the same amount of food compared to the ad libitum (control) animals. However, after 9 h of deprivation, mice consumed only 50% of food present even after 1 h of re-feeding, compared to the controls. The ACC activity was measured in the whole mouse brain of controls and after 1, 3, 6, 9, 12, and 24 h of food deprivation. Brain extracts assayed from control mice expressed an ACC activity of 0.988 ± 0.158 fmol/min/mg tissue without citrate and 0.941 ± 0.175 fmol/min/mg tissue with citrate. After 1 h of food deprivation, the total ACC activity without citrate decreased to 0.575 ± 0.087 fmol/min/mg and in the
Acetyl-CoA carboxylase is an essential enzyme, as it catalyzes the first committed and regulated step in fatty-acid biosynthesis in all organisms excepting few Archaea and Eubacteria. Acetyl-CoA carboxylase from gram-negative and gram-positive bacteria is a multifunctional enzyme composed of three separate proteins. The carboxyltransferase subunit catalyzes the transfer of a carboxyl group from carboxybiotin to acetyl-CoA, forming malonyl-CoA. The crystal structure of the Escherichia coli (E. coli) carboxyltransferase component of acetyl-CoA carboxylase revealed a unique Zn-domain, presumed to mediate nucleic acid binding, that is absent in the eukaryotic enzyme. Notably, the Zn-domain, adjacent to the active site of carboxyltransferase, makes for a unique target in the development of novel antibiotics capable of highly specific binding. Utilizing an Electrophoretic Mobility Shift Assay as part of this study, we investigated the nonspecific nucleic-acid binding and substrate (malonyl-CoA and biocytin)
Haystead TA, Campbell DG and Hardie DG. Biochemistry Department, Dundee University, Scotland.. We have examined the sites phosphorylated on acetyl-CoA carboxylase in response to insulin in isolated adipocytes. Two tryptic peptides derived from the enzyme become more radioactive after treatment of 32P-labelled cells with insulin. One of these (T4a) accounts for a large part of the total increase in phosphate observed after insulin treatment, and comigrates with the peptide containing the sites phosphorylated in vitro by casein kinase-2. The other may correspond to the I site peptide originally described by Brownsey and Denton in 1982: labelling of this peptide is stimulated at least threefold by insulin treatment, but it is a minor phosphopeptide and, even after insulin treatment, accounts for only about 2.5% of the enzyme-bound phosphate (equivalent to less than 0.1 mol phosphate/mol 240-kDa subunit). Two other major tryptic phosphopeptides (T1 and T4b) labelled in adipocytes do not change ...
1A6X: Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase.
Acacb - Acacb (Myc-DDK-tagged) - Mouse acetyl-Coenzyme A carboxylase beta (Acacb) available for purchase from OriGene - Your Gene Company.
Depletion of mtDNA in myocytes causes insulin resistance and alters nuclear gene expression that may be involved in rescuing processes against cellular stress. Here we show that the expression of C1q tumor necrosis factor a-related protein isoform 5 (C1QTNF5) is drastically increased following depletion of mtDNA in myocytes. C1QTNF5 is homologous to adiponectin in respect to domain structure, and its expression and secretion from myocytes correlated negatively with the cellular mtDNA content. Similar to adiponectin, C1QTNF5 induced the phosphorylation of AMP-activated protein kinase (AMPK), leading to increased cell surface recruitment of GLUT4 and increased glucose uptake. Treatment of cells with purified recombinant C1QTNF5 increased the phosphorylation of acetyl-CoA carboxylase and stimulated fatty acid oxidation. C1QTNF5-mediated phosphorylation of AMPK or acetyl-CoA carboxylase was unaffected by depletion of adiponectin receptors such as AdipoR1 or AdipoR2, which indicated that adiponectin ...
Insulin prevents fat-burning in part by locking fat in adipose tissue and in part by shutting down transport of fatty acids into the mitochondrion inside cells. By downregulating lipoprotein lipase (LPL) at heart and skeletal muscle and upregulating it at adipose tissue, insulin shifts dietary fat away from heart and muscle and toward adipose tissue. By downregulating hormone-sensitive lipase in adipose tissue, it prevents the release of free fatty acids from adipose tissue into the blood. At the cellular level, insulin leads to the phosphorylation and deactivation of AMPK. Since AMPK inhibits acetyl CoA carboxylase, insulin-mediated deactivation of AMPK leads to activation of acetyl CoA carboxylase and the conversion of acetyl CoA to malonyl CoA. Malonyl CoA inhibits carnitine palmitoyl transferase-1 (CPT-1) and thus blocks the transport of fatty acids into the mitochondrion. Nevertheless, all of these steps are also regulated at the most fundamental level by energy status, as covered in lesson 22.
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putative acyl-CoA carboxylase alpha subunit [putative Acyl-CoA carboxylase] ATGAGCGCCGCCCTCCTAGGCCTCCGTCAGGCCCGCATACGCAAGGTGTTGATCGCCAAC CGTGGCGAAATCGCTGTTCGTGTCGCCCGGGCGTGCCGAGACGCCGGTATCGCGAGCGTG GCGGTGTACGCCGAGCCGGACCGGGACGCACTGCATGTGCGGGCCGCGGACGAGGCGTTC GCGCTGGGCGGTGACACCCCCGCGACCAGCTACCTCGACATGGCCAAGGTGCTGCAGGCC GCCAAGGACTCCGGCGCGGACGCCATCCACCCCGGTTACGGCTTCCTTTCCGAGAACGCC GACTTCGCCCAGGCCGTCCTGGACGCCCAGCTGATCTGGATCGGCCCGCCGCCGCAGGCG ATTCGCGACCTGGGTGACAAGGCCCATATCGCCCAGCGCGCCGGCGCCCCGCTGGTCGCC GGCACCCCCGACCCGGTCTCGGGCTCGGACGAGGTCGTCGCCTTCGCGGAGGAGCACGGG CTGCCGATCGCCATCAAGGCCGCCTTCGGTGGCGGTGGCCGCGGTCTGAAGGTCGCCCGC ACCCTGGAAGAAGTCCCCGAGCTGTACGACTCGGCCGTCCGCGAGGCGGTGGCCGCCTTC GGCCGCGGTGAGTGCTTCGTCGAGCGCTACCTCGACAAGCCCCGGCACGTGGAGACCCAG TGCCTGGCCGACTCCCACGGCAACGTGGTCGTCGTCTCCACCCGCGACTGCTCACTGCAG CGCCGCCACCAGAAGCTGGTCGAGGAGGCGCCCGCGCCGTTCCTCTCCGACGAGCAGGTC GCCGAGCTGTACTCCTCTTCGAAGGCCATCCTCAAGGAGGCCGGCTATGTCGGCGCCGGG ACCGTGGAGTTCCTGGTCGGCACGGACGGCACGATCTCCTTCCTGGAGGTCAACACCCGC ...
MetabolismFatty acid and phospholipid metabolismBiosynthesisacetyl-CoA carboxylase, biotin carboxylase subunit (TIGR00514; EC 6.3.4.14; HMM-score: 11.1) ...
Chapter 16 (Part 3). Fatty acid Synthesis. ACP vs. Coenzyme A. Citrate Lyase. Citrate synthase. Malate dehydrogenase. Pyruvate carboxylase. Malate Enzyme. Fatty Acid Synthesis Occurs in the Cytosol. Acetyl-CoA Carboxylase. Acetyl-CoA + HCO 3 - + ATP  malonyl-CoA + ADP. Slideshow...
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_1647 (SAUSA300_RS08990); symbol: accD; product: acetyl-CoA carboxylase subunit beta
The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia. [provided by RefSeq, Jul 2008 ...
Insulin resistance (IR) is a common pathophysiological feature of Type 2 diabetes. Although the mechanisms leading to IR are still elusive, evidence has shown that aerobic exercise can reverse this process. To investigate the effects of aerobic exercise on IR, the authors created an IR animal model by feeding C57BL/6 mice a high-fat diet for 8 wk. They then compared the effect of 6 wk of treadmill training (60 min/d) at 75% VO2max on mice in normal-diet (NE) and high-fat-diet (HE) groups with their sedentary control groups. Levels of skeletal-muscle AMPKα (AMP-activated protein kinase α), ACC (acetyl-CoA carboxylases), and CPT1 (carnitine palmitoyltransferase 1) mRNA and AMPKα, pAMPK-Thr172, ACC, pACC-Ser79, and CPT1 protein expressions were analyzed. In addition, fasting serum levels of insulin, triglyceride, and cholesterol were measured. The results demonstrate that 6 wk of exercise increased AMPKα mRNA expression by 11% and 25 % (p , .01) in the NE and HE groups, respectively, and AMPKα ...
AMP-activated protein kinase (AMPK) is a key energy-sensitive enzyme that controls numerous metabolic and cellular processes. Mammalian target of rapamycin (mTOR) is another energy/nutrientsensitive kinase that controls protein synthesis and cell growth. In this study we determined whether older versus younger men have alterations in the AMPK and mTOR pathways in skeletal muscle, and examined the effect of a long term resistance type exercise training program on these signaling intermediaries. Older men had decreased AMPKa2 activity and lower phosphorylation of AMPK and its downstream signaling substrate acetyl-CoA carboxylase (ACC). mTOR phosphylation also was reduced in muscle from older men. Exercise training increased AMPKa1 activity in older men, however, AMPKa2 activity, and the phosphorylation of AMPK, ACC and mTOR, were not affected. In conclusion, older men have alterations in the AMPK-ACC and mTOR pathways in muscle. In addition, prolonged resistance type exercise training induces an isoform
Acetogenesis the carbonic acids are converted to acetate, H{}2 and CO{}2. Just these substances can be changed directly into methane by methanogenic bacteria. This process is also called anaerobic oxidation, because electrons in the form of H{}2 are released. The releasing of butyric ...
Air-conditioning equipment installed as recently as 10 years ago is an energy-guzzling monster compared with the latest equipment, and Mitsubishi Electric...
Watch this brief, video picture of practice that captures everyday classroom life and provides real-life examples of how students learn and think about climate change topics.
FOSTER CITY, Calif.-(BUSINESS WIRE)-Gilead Sciences, Inc. (Nasdaq:GILD) today announced results from an open-label, proof-of-concept study evaluating GS-0976, an investigational inhibitor of Acetyl-CoA carboxylase (ACC), in patients with nonalcoholic steatohepatitis (NASH). The data, from ten patients treated with GS-0976 20 mg taken orally once daily for 12 weeks, indicated that treatment …. ...
Knockout Tested Rabbit recombinant monoclonal Acetyl Coenzyme A Carboxylase (phospho S79) antibody [EP1885Y] - BSA and Azide free. Validated in WB, Dot and tested in Mouse, Rat, Human.
Lung cancers is certainly the most regular form of cancers. causing from SCD blockade had been completely reversed by either oleic (18:1n-9), palmitoleic acidity (16:1n-7) or cis-vaccenic acidity (18:1n-7) showing that cis-MUFA are essential elements for cancers cell growth. Additionally, co-treatment of cells with CVT-11127 and CP-640186, a particular acetylCoA carboxylase (ACC) inhibitor, do not really potentiate the development inhibitory impact of these substances, recommending that inhibition of SCD1 or ACC impacts a equivalent focus on important for cell growth, most likely MUFA, the common fatty acidity item in the path. This speculation was additional strengthened by the remark that exogenous oleic acidity reverses the anti-growth impact of SCD and ACC inhibitors. Cediranib Finally, exogenous oleic acidity refurbished the internationally reduced amounts of cell fats in cells going through a blockade of SCD activity, suggesting that energetic lipid activity is definitely needed for the ...
Antibodies for proteins involved in acetyl-CoA metabolic process pathways, according to their Panther/Gene Ontology Classification
A new study by paleoecologist Margaret Fraiser at the University of Wisconsin, Milwaukee, offers an interesting new theory behind the cause of the Earths largest extinction: copious carbon-dioxide
A new study by paleoecologist Margaret Fraiser at the University of Wisconsin, Milwaukee, offers an interesting new theory behind the cause of the Earths largest extinction: copious carbon-dioxide
Continuous monitoring for carbon-monoxide in the assembly calibration, cold header, and screw machine departments of an automotive company using a portable detector shows the highest concentration to be 30 ppm in the assembly department, and the average concentration of 15 ppm in all four departments. No measurable concentrations of carbon-dioxide (124389), nitrogen- dioxide (10102440), or sulfur-
The ACC gene encodes a truncated copy of the tomato 1-amino-cyclopropane-1-carboxylic acid (ACC) synthase encoding gene in order to suppress expression of the endogenous unmodified gene (which is required for normal ethylene biosynthesis) through gene silencing ...
The present invention provides compounds of formula I: ##STR00001## along with methods of use of these compounds as pharmaceuticals, particularly in the treatment of obesity, metabolic syndrome, athe
project24,Project 24: Over expression of Acetyl- CoA carboxylase (ACC) sub-unit accC in E.coli to enhance fatty acid accumulation for Bio-fuel production.Fuel-it-up (Sanju Timilsina and Parul Sirohi ...
Western blotting results of adipogenesis-specific markers.Representative image of 3 repeats and quantification of (A) PPARγ, (B) C/EBPα, and (C) Acetyl CoA ca
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Boone, A.N.; Brownsey, R.W.; Elliott, J.E.; Kulpa, J.E.; Lee, W.M. (2006). "Regulation of acetyl-CoA carboxylase". Biochemical ... "A Mechanism for the Potent Inhibition of Eukaryotic Acetyl-Coenzyme a Carboxylase by Soraphen A, a Macrocyclic Polyketide ... 2000). "Pig Heart CoA Transferase Exists as Two Oligomeric Forms Separated by a Large Kinetic Barrier". Biochemistry. 39 (37): ... Wohl, RC; Markus, G (1972). "Phosphoenolpyruvate carboxylase of Escherichia coli. Purification and some properties". The ...
Acetyl-CoA carboxylase 2 also known as ACC-beta or ACC2 is an enzyme that in humans is encoded by the ACACB gene. Acetyl-CoA ... Human acetyl-CoA carboxylase has recently become a target in the design of new anti-obesity drugs. However, when the gene for ... Kreuz S, Schoelch C, Thomas L, Rist W, Rippmann JF, Neubauer H (September 2009). "Acetyl-CoA carboxylases 1 and 2 show distinct ... Corbett JW, Harwood JH (November 2007). "Inhibitors of mammalian acetyl-CoA carboxylase". Recent Patents on Cardiovascular Drug ...
This group of herbicides acts by inhibiting plant acetyl-CoA carboxylase (ACCase), a completely different mechanism of action ... Lichtenthaler, Hartmut K. (1990). "Mode of Action of Herbicides Affecting Acetyl-CoA Carboxylase and Fatty Acid Biosynthesis". ... Whittingham, William G. (2016). "Herbicidal Aryloxyphenoxypropionate Inhibitors of Acetyl-CoA Carboxylase". Bioactive ... a grass-selective herbicide which inhibits acetyl-CoA carboxylase in sensitive plant species". Biochemical Journal. 254 (1): ...
... and other similar herbicides act by inhibiting plant acetyl-CoA carboxylase (ACCase). Their selectivity for grasses ... Lichtenthaler, Hartmut K. (1990). "Mode of Action of Herbicides Affecting Acetyl-CoA Carboxylase and Fatty Acid Biosynthesis". ... Kaundun, Shiv S (2014-05-06). "Resistance to acetyl-CoA carboxylase-inhibiting herbicides". Pest Management Science. 70 (9): ... domain of Acetyl-CoA carboxylase of Phalaris minor". Network Modeling Analysis in Health Informatics and Bioinformatics. 8. doi ...
Acetyl-CoA carboxylase 1 also known as ACC-alpha or ACCa is an enzyme that in humans is encoded by the ACACA gene. Acetyl-CoA ... Yoon S, Lee MY, Park SW, Moon JS, Koh YK, Ahn YH, Park BW, Kim KS (September 2007). "Up-regulation of acetyl-CoA carboxylase ... Ray H, Suau F, Vincent A, Dalla Venezia N (January 2009). "Cell cycle regulation of the BRCA1/acetyl-CoA-carboxylase complex". ... March 2007). "Haplotype-based analysis of common variation in the acetyl-coA carboxylase alpha gene and breast cancer risk: a ...
"Leptin activates hypothalamic acetyl-CoA carboxylase to inhibit food intake". Proceedings of the National Academy of Sciences. ...
Current research in the Liang Tong's lab focuses on enzymes involved in fatty acid metabolism, including Acetyl-CoA carboxylase ... Wei, J.; Tong, L. (2015). "Crystal structure of the 500-kDayeast acetyl-CoA carboxylase holoenzyme dimer". Nature. 526: 723-727 ... and the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer using X-ray crystallography. In addition to structural studies, ... "Crystal structure of the a6b6 holoenzyme of propionyl-coenzyme A carboxylase". Nature. 466: 1001-1005. Xiang, K.; Nagaike, T.; ...
For example, protein kinase A phosphorylates acetyl-CoA carboxylase and pyruvate dehydrogenase. Such covalent modification has ...
Acetyl-CoA carboxylase (ACC) converts acetyl-CoA to malonyl-CoA, an inhibitor of carnitine palmitoyltransferase 1 (CPT-1). CPT- ... MCD is an antagonist to ACC, decarboxylating malonyl-CoA to acetyl-CoA, resulting in decreased malonyl-CoA and increased CPT-1 ... When AMPK phosphorylates acetyl-CoA carboxylase 1 (ACC1) or sterol regulatory element-binding protein 1c (SREBP1c), it inhibits ... Hutber CA, Hardie DG, Winder WW (February 1997). "Electrical stimulation inactivates muscle acetyl-CoA carboxylase and ...
Acetyl-CoA carboxylase: an important regulator of fatty acid oxidation in the heart". Canadian Journal of Physiology and ... ALCAR in the cytosol can also form a pool of acetyl-groups for CoA, should the cell need it. Excess acetyl-CoA causes more ... acetyl-CoA + carnitine ⇌ CoA + acetylcarnitine where the acetyl group displaces the hydrogen atom in the central hydroxyl group ... acetyl-CoA is the primary substrate for the Krebs cycle, once it is de-acetylated, it must be re-charged with an acetyl-group ...
McCarty MF (2001). "Inhibition of acetyl-CoA carboxylase by cystamine may mediate the hypotriglyceridemic activity of ... In the first, pantethine serves as the precursor for synthesis of coenzyme A. CoA is involved in the transfer of acetyl groups ...
... particularly in biotin-dependent enzymes such as propionyl-CoA carboxylase and acetyl-CoA carboxylase, which he studied in and ... Kresge, Nicole; Simoni, Robert D.; Hill, Robert L. (8 December 2006). "Acetyl-CoA Carboxylase and Other Biotin-dependent ...
2000). "AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation". Am. J. ... "Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase". Eur. J ...
... and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR ... "Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle". J. Biol. Chem. 272 (20 ...
... and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR ... 2003). "Effects of thyroid state on AMP-activated protein kinase and acetyl-CoA carboxylase expression in muscle". J. Appl. ...
The enzyme acetyl CoA carboxylase is responsible for introducing a carboxyl group to acetyl CoA, rendering malonyl-CoA. Then, ... De novo fatty-acid synthesis is regulated by two important enzymes, namely acetyl-CoA carboxylase and fatty acid synthase. ... so cancer cells contain many enzymes for de novo cholesterol synthesis from acetyl-CoA. De novo lipogenesis (DNL) is the ... the enzyme fatty-acid synthase is responsible for turning malonlyl-CoA into fatty-acid chain. De novo fatty-acid synthesis is ...
In the case of E. coli Acetyl-CoA carboxylase, the BCCP is a separate protein known as accB (P0ABD8). On the other hand, in ... Haloferax mediterranei Propionyl-CoA carboxylase, the BCCP pccA (I3R7G3) is fused with biotin carboxylase. v t e v t e ... domain that carry biotin and carboxybiotin throughout the ATP-dependent carboxylation by biotin-dependent carboxylases. ...
Acetyl-CoA carboxylase (ACCase) is an enzyme which catalyzes a key metabolic step in the synthesis of oils in algae. The ...
By controlling the activity of the pyruvate dehydrogenase and the acetyl-CoA carboxylase enzymes, insulin promotes unsaturated ...
Many carboxylases, including Acetyl-CoA carboxylase, Methylcrotonyl-CoA carboxylase, Propionyl-CoA carboxylase, and Pyruvate ... OMIM - gamma-glutamyl carboxylase, contributed by McKusick VA, last updated October 2004 [1] Morris DP, Stevens RD, Wright DJ, ... Carboxylation occurs in the liver and is performed by γ-glutamyl carboxylase (GGCX). GGCX requires vitamin K as a cofactor and ... In the EC scheme, such carboxylases are classed under EC 6.3.4, "Other Carbon-Nitrogen Ligases". Another example is the ...
May 2008). "Chronic Suppression of Acetyl-CoA Carboxylase 1 in β-Cells Impairs Insulin Secretion via Inhibition of Glucose ... Fransson U, Rosengren AH, Schuit FC, Renström E, Mulder H (July 2006). "Anaplerosis via pyruvate carboxylase is required for ... August 2006). "Compensatory responses to pyruvate carboxylase suppression in islet beta-cells. Preservation of glucose- ...
Other predicted interacting proteins are acetyl-CoA carboxylases A and B, glycine dehydrogenase, 3-oxoacid CoA transferase 2. ... C2orf81 protein is predicted to interact highly with enoyl-CoA hydratase and hydroxyacyl-CoA dehydrogenase, based on textmining ...
... acid synthesis is an anabolic process that starts from the conversion of acetyl-CoA to malonyl-CoA by acetyl-CoA carboxylase. ... Malonyl CoA leads to fatty acid synthesis (FAS) and is involved in the elongation of fatty acids through Fatty acid synthase ( ...
... acetyl-CoA carboxylase and propionyl-CoA carboxylase. These enzymes generate malonyl-CoA and (S)-methylmalonyl-CoA, ... Malonyl-CoA, in a series of reactions is further split into acetyl-CoA and glyoxylate. Glyoxylate is incorporated into beta- ... methylmalyl-coA which is then split, again through a series of reactions to release pyruvate as well as acetate, which is used ...
Glucose oxidation produces citrate which can be converted to malonyl-CoA by acetyl-CoA carboxylase. Malonyl-CoA inhibits the ... The concentration of malonyl-CoA depends on the balance between acetyl-CoA carboxylase (ACC) and malonyl-CoA decarboxylase (MCD ... "Characterization of 5'AMP-activated protein kinase activity in the heart and its role in inhibiting acetyl-CoA carboxylase ... acetyl-CoA]/[CoA] and [NADH]/[NAD+]. These both serve to inhibit pyruvate dehydrogenase activity. It has been proposed that ...
ACCase Inhibitors kill grasses and inhibit the first step in lipid synthesis, acetyl-CoA carboxylase, thus affecting cell ... and synthesized from acetyl-CoA or basic intermediates of glycolysis They often end in -ol (menthol) and comprise the majority ...
Long term fatty acid synthesis regulation is dependent on the rate of acetyl-CoA carboxylase (ACC) synthesis, the rate-limiting ... Numa S, Ringelmann E, Lynen F (December 1965). "[On inhibition of acetyl-CoA-carboxylase by fatty acid-coenzyme A compounds]". ... Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC (March 2003). "The 1.75 A crystal structure of acetyl-CoA ... Fatty acyl CoA synthetase catalyzes the activation of a long fatty acid chain to a fatty acyl CoA, requiring the energy of 1 ...
In 2016, Nimbus Therapeutics sold an Acetyl-CoA carboxylase (ACC) inhibitor designed by Schrödinger to Gilead in a deal worth ... Acetyl-CoA Carboxlyase (ACC) Program for NASH and Other Liver Diseases". www.businesswire.com (Press release). Retrieved 2019- ...
... acetyl-CoA carboxylase, PPARα, and acyl-CoA oxidase. Changes in expression were reportedly due to epigenetic regulation of ...
Acetyl-CoA carboxylase catalyzes the production of malonyl-CoA from acetyl-CoA. Malonyl-CoA reduces the activity of carnitine ... Fatty acids are enzymatically broken down in β-oxidation to form acetyl-CoA. Under normal conditions, acetyl-CoA is further ... switches off acetyl-CoA carboxylase, turns on malonyl-CoA decarboxylase, and consequently induces ketogenesis. Ethanol is a ... acetyl-CoA is then used instead in biosynthesis of ketone bodies via acetoacetyl-CoA and β-hydroxy-β-methylglutaryl-CoA (HMG- ...
acetyl-CoA carboxylase. rubisco. tRNAs. tRNA. photosystem II. tRNAs. tRNAs. photosystem II ...
Malonyl-CoA synthesis. *ATP citrate lyase. *Acetyl-CoA carboxylase. Fatty acid synthesis/. Fatty acid synthase. *Beta-ketoacyl- ... 3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA ... Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, ... The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons ...
acetyl-CoA carboxylase) kinase (EC 2.7.11.27). *-. Tropomyosin kinase (EC 2.7.11.28). *- ... 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4). *BCKDK ...
3-hydroxy-3-methylglutaryl-CoA lyase deficiency. *3-Methylcrotonyl-CoA carboxylase deficiency ... K→acetyl-CoA. Lysine/straight chain. *Glutaric acidemia type 1. *type 2 ...
Pyruvate carboxylase. *Acetyl-CoA carboxylase. *Propionyl-CoA carboxylase. *Methylcrotonyl-CoA carboxylase. Other. *Polyketide ...
to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... to succinyl-CoA. *Methylmalonyl-CoA mutase. to oxaloacetate. *Pyruvate carboxylase. *Aspartate transaminase ...
Xerophytes, such as cacti and most succulents, also use PEP carboxylase to capture carbon dioxide in a process called ... Acetyl. -CoA Polyketides Terpenoid. backbones Terpenoids. & carotenoids (vitamin A) Cholesterol Bile acids ... Plants that do not use PEP-carboxylase in carbon fixation are called C3 plants because the primary carboxylation reaction, ... 5-bisphosphate carboxylase/oxygenase and decrease in carbon fixation. Some plants have evolved mechanisms to increase the CO. 2 ...
... acetyl CoA carboxylase, which is involved in the synthesis of fatty acids from acetate; pyruvate CoA carboxylase, involved in ... β-methylcrotonyl CoA carboxylase, involved in the metabolism of leucine; and propionyl CoA carboxylase, which is involved in ... Multiple carboxylase deficiency, an inborn error of metabolism, can lead to biotin deficiency even when dietary biotin intake ... Its active form is a coenzyme called thiamine pyrophosphate (TPP), which takes part in the conversion of pyruvate to acetyl ...
to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... to succinyl-CoA. *Methylmalonyl-CoA mutase. to oxaloacetate. *Pyruvate carboxylase. *Aspartate transaminase ... An important enzyme in this pathway is HMG-CoA reductase, usually a target for intervention in cardiovascular complications. ... The "statin" family of cholesterol-reducing medications inhibits HMG-CoA reductase. One possible side effect of statins is ...
... can be carboxylated in the cytosol by acetyl-CoA carboxylase, giving rise to malonyl-CoA, a substrate required for ... Increased concentration of acetyl-CoA activates PDK.[19]. *Acetyl-CoA is also an allosteric activator of pyruvate carboxylase.[ ... The cytosolic acetyl-CoA can also condense with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) which is the ... acetyl-CoA can then be used to synthesize fatty acids through carboxylation by acetyl-CoA carboxylase into malonyl CoA, the ...
By controlling the activity of the pyruvate dehydrogenase and the acetyl-CoA carboxylase enzymes, insulin promotes unsaturated ...
... is converted into acetyl-CoA and thereby contributes to the synthesis of ketones, steroids, fatty acids, and other compounds. ... MC-CoA. carboxylase. MG-CoA. hydratase. HMG-CoA. reductase. HMG-CoA synthase ... Following this pathway, HMB in the cytosol is first converted to cytosolic β-hydroxy-β-methylglutaryl-CoA (HMG-CoA), which can ... Human metabolic pathway for HMB and isovaleryl-CoA relative to L-leucine.[1][2][3] Of the two major pathways, L-leucine is ...
The enzyme is inhibited by high ratios of ATP:ADP, acetyl-CoA:CoA, and NADH:NAD, as high concentrations of ATP, acetyl-CoA, and ... This induces the enzyme to change its conformation, and creates a binding site for the acetyl-CoA. Only when this citroyl-CoA ... It is also inhibited by succinyl-CoA, which resembles Acetyl-coA and acts as a uncompetitive inhibitor. Citrate inhibits the ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ...
... (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to ... Malonyl-CoA decarboxylase. References[edit]. *^ a b c Tong L (August 2005). "Acetyl-coenzyme A carboxylase: crucial metabolic ... In Escherichia coli, accA encodes the alpha subunit of the acetyl-CoA carboxylase,[6] and accD encodes its beta subunit.[7] ... "accA, acetyl-CoA carboxylase alpha subunit (Escherichia coli str. K-12 substr. MG1655)". NCBI gene. National Center for ...
Malonyl-CoA synthesis. *ATP citrate lyase. *Acetyl-CoA carboxylase. Fatty acid synthesis/. Fatty acid synthase. *Beta-ketoacyl- ...
For example, protein kinase A phosphorylates acetyl-CoA carboxylase and pyruvate dehydrogenase. Such covalent modification has ...
Methylcrotonyl-CoA carboxylase. *Methylglutaconyl-CoA hydratase. (See Template:Leucine metabolism in humans - this diagram does ... K→acetyl-CoA. LYSINE→. *Saccharopine dehydrogenase. *Glutaryl-CoA dehydrogenase. LEUCINE→. *3-Hydroxybutyryl-CoA dehydrogenase ...
... is formed from propionyl-CoA by propionyl-CoA carboxylase by help of biotin (vitamin B7). It is converted ... Propionyl CoA → Methylmalonyl CoA → Succinyl CoA. See also[edit]. *Methylmalonyl CoA epimerase ... Methylmalonyl-CoA is the thioester consisting of coenzyme A linked to methylmalonic acid. It is an important intermediate in ... into succinyl-CoA by methylmalonyl-CoA mutase, in a reaction that requires vitamin B12 as a cofactor. In this way, it enters ...
SCoAacetyl-CoA + NADH + CO2. The product of this reaction, acetyl-CoA, is the starting point for the citric acid cycle. Acetyl- ... However, it is also possible for pyruvate to be carboxylated by pyruvate carboxylase to form oxaloacetate. This latter reaction ... The carbons lost as CO2 originate from what was oxaloacetate, not directly from acetyl-CoA. The carbons donated by acetyl-CoA ... Acetyl-CoA cannot be transported out of the mitochondrion. To obtain cytosolic acetyl-CoA, citrate is removed from the citric ...
... in the large subunit of CPSase is also present as a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase (ACC), ... propionyl-CoA carboxylase (PCCase), pyruvate carboxylase (PC) and urea carboxylase. The large subunit in bacterial CPSase has ...
... carboxylase. References[edit]. *^ a b c Wilson JM, Fitschen PJ, Campbell B, Wilson GJ, Zanchi N, Taylor L, ... is converted into acetyl-CoA and thereby contributes to the synthesis of ketones, steroids, fatty acids, and other compounds. ... 3-Methylcrotonyl-CoA or β-Methylcrotonyl-CoA is an intermediate in the metabolism of leucine.[1][2][3] ... Following this pathway, HMB in the cytosol is first converted to cytosolic β-hydroxy-β-methylglutaryl-CoA (HMG-CoA), which can ...
Cyclohexanedione targets the Acetyl-CoA carboxylase which is involved in the first step of fat synthesis: ATP-dependent ... carboxylation of acetyl-CoA to malonyl-CoA. Lipids are important in making up the cell membrane. ...
The cytosolic acetyl-CoA is carboxylated by acetyl CoA carboxylase into malonyl-CoA, the first committed step in the synthesis ... To obtain cytosolic acetyl-CoA, citrate (produced by the condensation of acetyl-CoA with oxaloacetate) is removed from the ... Pyruvate is then decarboxylated to form acetyl-CoA in the mitochondrion. However, this acetyl CoA needs to be transported into ... There it is cleaved by ATP citrate lyase into acetyl-CoA and oxaloacetate. The oxaloacetate is returned to the mitochondrion as ...
tryptophan catabolic process to acetyl-CoA. • L-kynurenine catabolic process. • tryptophan catabolic process. • tryptophan ... Methylcrotonyl-CoA carboxylase. *Methylglutaconyl-CoA hydratase. (See Template:Leucine metabolism in humans - this diagram does ...
Palmitate negatively feeds back on acetyl-CoA carboxylase (ACC), which is responsible for converting acetyl-CoA to malonyl-CoA ...
Acetyl-CoA is formed into malonyl-CoA by acetyl-CoA carboxylase, at which point malonyl-CoA is destined to feed into the fatty ... The cytosolic acetyl-CoA is carboxylated by acetyl CoA carboxylase into malonyl CoA, the first committed step in the synthesis ... cause the dephosphorylation of acetyl-CoA carboxylase, thus promoting the formation of malonyl-CoA from acetyl-CoA, and ... Citrate acts to activate acetyl-CoA carboxylase under high levels, because high levels indicate that there is enough acetyl-CoA ...
The Escherichia coli galactitol operon protein, gatY, and N-acetyl galactosamine operon protein, agaY, which are tagatose- ... Phosphoenolpyruvate carboxylase. *Phosphoribosylaminoimidazole carboxylase. *Pyrophosphomevalonate decarboxylase. *Pyruvate ... Malonyl-CoA decarboxylase. *Ornithine decarboxylase. *Oxaloacetate decarboxylase. *Phosphoenolpyruvate carboxykinase. * ...
Malonyl-CoA synthesis. *ATP citrate lyase. *Acetyl-CoA carboxylase. Fatty acid synthesis/. Fatty acid synthase. *Beta-ketoacyl- ... acyl-CoA dehydrogenase activity. • identical protein binding. • oxidoreductase activity. • medium-chain-acyl-CoA dehydrogenase ... ACADM, acyl-CoA dehydrogenase, C-4 to C-12 straight chain, ACAD1, MCAD, MCADH, acyl-CoA dehydrogenase medium chain. ... carnitine metabolic process, CoA-linked. • fatty acid beta-oxidation. • regulation of lipid metabolic process. ...
... converted into acetyl CoA, which is then converted into malonyl CoA by acetyl CoA carboxylase, which is allosterically ... and allosterically regulates the enzyme acetyl-CoA carboxylase, which is the regulating enzyme in the conversion of acetyl-CoA ... Citrate can be transported out of the mitochondria and into the cytoplasm, then broken down into acetyl-CoA for fatty acid ... Citrate synthase catalyzes the condensation of oxaloacetate with acetyl CoA to form citrate. Citrate then acts as the substrate ...
3-hydroxy-3-methylglutaryl-CoA lyase deficiency. *3-Methylcrotonyl-CoA carboxylase deficiency ... K→acetyl-CoA. Lysine/straight chain. *Glutaric acidemia type 1. *type 2 ...
Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to ... Malonyl-CoA decarboxylase. References[edit]. *^ a b c Tong L (August 2005). "Acetyl-coenzyme A carboxylase: crucial metabolic ... In Escherichia coli, accA encodes the alpha subunit of the acetyl-CoA carboxylase,[6] and accD encodes its beta subunit.[7] ... "accA, acetyl-CoA carboxylase alpha subunit (Escherichia coli str. K-12 substr. MG1655)". NCBI gene. National Center for ...
... acetyl-CoA carboxylase kinase (cAMP-independent), acetyl-CoA carboxylase kinase 2, acetyl-CoA carboxylase kinase-2, acetyl-CoA ... acetyl-CoA carboxylase] phosphate Thus, the two substrates of this enzyme are ATP and acetyl-CoA carboxylase, whereas its two ... acetyl-CoA carboxylase] kinase (EC 2.7.11.27) is an enzyme that catalyzes the chemical reaction ATP + [acetyl-CoA carboxylase ... acetyl-CoA carboxylase bound kinase, acetyl-CoA carboxylase kinase, ...
In bacteria, the acetyl coenzyme A carboxylase (ACC) is a complex consisting of two subunits: alpha and beta. This domain also ... One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this ... All of the members in this family are biotin dependent carboxylases [PMID: 8102604, PMID: 8366018]. The carboxyl transferase ... Molecular evolution of biotin-dependent carboxylases.. Eur. J. Biochem. 215 687-96 1993 ...
Inhibition of acetyl-CoA carboxylase (ACC), which results in inhibition of fatty acid synthesis and stimulation of fatty acid ... Acetyl-CoA carboxylase inhibition for the treatment of metabolic syndrome.. Harwood HJ Jr1. ...
Record removed. This record was removed as a result of standard genome annotation processing. Please see www.ncbi.nlm.nih.gov/genome/annotation_euk/process/ for more information. ...
Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms.. L Abu-Elheiga, A Jayakumar, ... We have cloned and sequenced the cDNA coding for human HepG2 acetyl-CoA carboxylase (ACC; EC 6.4.1.2). The sequence has an open ... Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. ... Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. ...
Acetyl-CoA carboxylase (ACC) regulates synthesis and oxidation of fatty acids, and mice lacking the ACC2 isoform are leaner ... Continuous fat oxidation in acetyl-CoA carboxylase 2 knockout mice increases total energy expenditure, reduces fat mass, and ...
Acetyl CoA Carboxylase Antibody,biological,biology supply,biology supplies,biology product ... Anti-Acetyl CoA Carboxylase Antibody, Unconjugated from Cell Signaling Technology, ... Acetyl CoA Carboxylase Antibody. Info. Cell Signaling Technology. Cell Signaling Technology, Inc. 3 Trask Lane Danvers, MA ... Rat Anti-Acetyl Salicylic Acid conjugated Acetyl Salicylic Acid Polyclonal Antibody, Unconjugated from Cell Sciences. 4. Mouse ...
Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the ... The peptide blocks Acetyl-CoA Carboxylase (C83B10) Rabbit mAb #3676 and Acetyl-CoA Carboxylase Antibody #3662 by dot blot and ... This peptide is used to block Acetyl-CoA Carboxylase (C83B10) Rabbit mAb #3676 or Acetyl-CoA Carboxylase Antibody #3662 ... Acetyl-CoA Carboxylase Blocking Peptide 1062. Toggle Between Dark and Light Modes Filter: ...
... phosphate/acetyl-CoA carboxylase 2 (Ser222) phosphate in the Metabolism research area. ... Monoclonal Antibody for studying acetyl-CoA carboxylase 1 (Ser80) ... Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the ... Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb recognizes endogenous levels of acetyl-CoA carboxylase protein only ...
We found that Acetyl-CoA carboxylase (ACC) inhibitors offer significant potential for the treatment of type 2 diabetes mellitus ... Acetyl-CoA carboxylase (ACC) inhibitors offer significant potential for the treatment of type 2 diabetes mellitus (T2DM), ... Biotin Attachment Domain-Containing Proteins Irreversibly Inhibit Acetyl CoA Carboxylase Journal Article Keereetaweep, Jantana ... Decreasing the Rate of Metabolic Ketone Reduction in the Discovery of a Clinical Acetyl-CoA Carboxylase Inhibitor for the ...
The putative gene encoding acetyl-CoA carboxylase, accA, has been isolated from Aspergillus nidulans. This single-copy gene has ... Based on sequence homology to acetyl-CoA carboxylases from other organisms, putative biotin-, ATP-, HCO3-- and acetyl-CoA- ... Isolation and characterisation of the acetyl-CoA carboxylase gene from Aspergillus nidulans Curr Genet. 1998 Dec;34(5):379-85. ... The putative gene encoding acetyl-CoA carboxylase, accA, has been isolated from Aspergillus nidulans. This single-copy gene has ...
... domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (By similarity). Through the ... Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid ... production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively ... Acetyl-CoA carboxylase 2 (Acacb), Acetyl-CoA carboxylase 1 (Acaca). This subpathway is part of the pathway malonyl-CoA ...
acetyl-CoA carboxylase (ACC), AMP-activated protein kinase (AMPK), biotin, fatty acid synthesis, insulin, malonyl-CoA ... Acetyl-CoA carboxylase (ACC) catalyses the formation of malonyl-CoA, an essential substrate for fatty acid synthesis in ... Regulation of acetyl-CoA carboxylase R.W. Brownsey R.W. Brownsey 1 ... R.W. Brownsey, A.N. Boone, J.E. Elliott, J.E. Kulpa, W.M. Lee; Regulation of acetyl-CoA carboxylase. Biochem Soc Trans 1 April ...
John W. Gronwald; Herbicides inhibiting acetyl-CoA carboxylase. Biochem Soc Trans 1 August 1994; 22 (3): 616-621. doi: https:// ... Herbicides inhibiting acetyl-CoA carboxylase John W. Gronwald John W. Gronwald * 1Plant Science Research Unit, USDA-ARS and ...
... forming malonyl-CoA, which is used in the plastid for fatty acid synthesis and in the cytosol in various biosynthetic pathways ... Multifunctional enzyme that catalyzes the carboxylation of acetyl-CoA, ... Acetyl-CoA carboxylase 1 (ACC1), Acetyl-CoA carboxylase 2 (ACC2). This subpathway is part of the pathway malonyl-CoA ... Acetyl-CoA carboxylase 1Add BLAST. 2267. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view ...
What is acetyl CoA carboxylase? Meaning of acetyl CoA carboxylase medical term. What does acetyl CoA carboxylase mean? ... Looking for online definition of acetyl CoA carboxylase in the Medical Dictionary? acetyl CoA carboxylase explanation free. ... acetyl CoA carboxylase. acetyl CoA carboxylase. a biotin-containing enzyme which participates in the synthesis of fatty acids ... gland of lactating mice was caused by reducing acetyl CoA carboxylase activity and mRNA abundance of acetyl CoA carboxylase, ...
Order Acetyl-CoA Carboxylase beta Proteins from many different species. Find the right product on antibodies-online.com. ... ACC-beta , acetyl-CoA carboxylase 2 , acetyl-Coenzyme A carboxylase beta , acetyl-Coenzyme A carboxylase 2 ... Acetyl-CoA Carboxylase beta (ACACB) Protein Überblick Protein Überblick Acetyl-CoA carboxylase (ACC) is a complex ... Acetyl-CoA Carboxylase beta Proteine 4 Acetyl-CoA Carboxylase beta (ACACB) Proteine von 3 Herstellern verfügbar auf www. ...
Acetyl-CoA Carboxylase alpha ELISA Kits vergleichen und bestellen. ... Acetyl-CoA Carboxylase alpha ELISA Kits für viele Reaktivitäten. Huhn, Rind (Kuh), Hund und weitere. ... acetyl-CoA carboxylase 1 , acetyl-coenzyme A carboxylase alpha , acetyl-CoA carboxylase-alpha , ACC , acetyl-CoA carboxylase , ... Acetyl-CoA Carboxylase alpha (ACACA) Antigen-Profil Protein Überblick Acetyl-CoA carboxylase (ACC) is a complex multifunctional ...
Browse our Acetyl-CoA Carboxylase alpha/ACACA product catalog backed by our Guarantee+. ... Acetyl-CoA Carboxylase alpha/ACACA products available through Novus Biologicals. ... PTMs for Acetyl-CoA Carboxylase alpha/ACACA. Learn more about PTMs related to Acetyl-CoA Carboxylase alpha/ACACA.. Oxidation. ... Diseases related to Acetyl-CoA Carboxylase alpha/ACACA. Discover more about diseases related to Acetyl-CoA Carboxylase alpha/ ...
Rabbit Polyclonal Anti-Acetyl-CoA Carboxylase alpha/ACACA Antibody. Validated: WB, Flow, ICC/IF, IHC, IHC-P. Tested Reactivity ... Acetyl-CoA Carboxylase alpha/ACACA Antibody Summary. Immunogen. Recombinant protein within Human Acetyl CoA Carboxylase 1 (ACC1 ... Blogs on Acetyl-CoA Carboxylase alpha/ACACA. There are no specific blogs for Acetyl-CoA Carboxylase alpha/ACACA, but you can ... Additional Acetyl-CoA Carboxylase alpha/ACACA Products. Array NBP2-89114 * Acetyl-CoA Carboxylase alpha/ACACA Antibodies ...
Invitrogen Anti-Phospho-Acetyl-CoA Carboxylase (Ser79) Polyclonal, Catalog # PA5-17725. Tested in Western Blot (WB), ... Acetyl-CoA carboxylase; Acetyl-CoA carboxylase 1; Acetyl-CoA carboxylase 265; Acetyl-Coenzyme A carboxylase alpha; Biotin ... Western blot analysis of Phospho-Acetyl-CoA Carboxylase (Ser79) using with Phospho-Acetyl-CoA Carboxylase (Ser79) Polyclonal ... of Phospho-Acetyl-CoA Carboxylase pSer79 in paraffin-embedded human breast carcinoma using a Phospho-Acetyl-CoA Carboxylase ...
1988) Regulation of acetyl-coenzyme A carboxylase. I. Purification and properties of two forms of acetyl-coenzyme A carboxylase ... 1988) Insulin stimulates the dephosphorylation and activation of acetyl-CoA carboxylase. Proc Natl Acad Sci USA 85(15):5473- ... 1985) Activation of acetyl-CoA carboxylase. Purification and properties of a Mn2+-dependent phosphatase. J Biol Chem 260(10): ... Acetyl-CoA carboxylase (ACC), the first committed enzyme in fatty acid (FA) synthesis, is regulated by phosphorylation/ ...
Insulin stimulates fatty acid synthesis in adipose and other tissues by increasing acetyl-CoA carboxylase activity. 1,2,3,4, ... R.W. Brownsey, W.A. Hughes, R.M. Denton and R.J. Mayer, Demon stration of the phosphorylation of acetyl-CoA carboxylase within ... A.L. Witters, D. Moriarty, and D.B. Martin, Regulation of hepatic acetyl-CoA carboxylase by insulin and glucagon, Biol. Chem. ... R.W. Brownsey, W.H. Hughes, and R.M. Denton, Adrenaline and the regulation of acetyl-CoA carboxylase in rat epididymal adipose ...
Order Acetyl-CoA Carboxylase alpha ELISA Kit ABIN810228. ... Acetyl-CoA Carboxylase alpha ELISA Kit Human for Plasma, Cell ... Acetyl-CoA Carboxylase alpha ELISA Kit (ACACA) Acetyl-CoA Carboxylase alpha ELISA Kit (ACACA). Details for Product ACACA ELISA ... More product categories related to Acetyl-CoA Carboxylase alpha Kit * 154 anti-Acetyl-CoA Carboxylase alpha Primary Antibodies ... Synonyms: ACAC, ACC, ACC1, ACCA, ACC-alpha,acetyl-CoA carboxylase 1,acetyl-CoA carboxylase-alpha ...
... acetyl-CoA carboxylase alpha) for ICC/IF, IHC-P, WB. Anti-Acetyl-CoA Carboxylase 1 pAb (GTX132081) is tested in Human, Mouse, ... Acetyl CoA Carboxylase 1 antibody , Acetyl CoA Carboxylase 1 antibody , acetyl-CoA carboxylase alpha antibody. ... acetyl-CoA carboxylase alpha. Background. Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a ... Green: Acetyl CoA Carboxylase 1 protein stained by Acetyl CoA Carboxylase 1 antibody (GTX132081) diluted at 1:500.. Blue: ...
Acetyl-coenzyme A (acetyl-CoA) carboxylase (ACC) catalyzes the synthesis of malonyl-CoA, a metabolite that plays a pivotal role ... Malonyl-coenzyme A (malonyl-CoA), generated by acetyl-CoA carboxylases ACC1 and ACC2, is a key metabolite in the regulation of ... Malonyl-CoA in the acid-soluble extract of the indicated tissues was measured by the incorporation of [3H]acetyl-CoA into ... Continuous Fatty Acid Oxidation and Reduced Fat Storage in Mice Lacking Acetyl-CoA Carboxylase 2 ...
2007). Single-site mutations in the carboxyl transferase domain of plastid acetyl-CoA carboxylase confer resistance to grass- ... Study of Fitness Cost in Three Rigid Ryegrass Populations Susceptible and Resistant to Acetyl-CoA Carboxylase Inhibiting ... Nine distinguished aminoacid replacements in the CT domain of plastidic Acetyl-COA carboxylase genes have been identified to ... Study of Fitness Cost in Three Rigid Ryegrass Populations Susceptible and Resistant to Acetyl-CoA Carboxylase Inhibiting ...
Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase.. S Saitoh, K Takahashi ... The cut6+ and lsd1+ genes are essential for viability and encode, respectively, acetyl CoA carboxylase and fatty acid ... Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase. ...
  • 21 Acetyl-CoA Carboxylase alpha (ACACA) ELISA Kits von 7 Herstellern verfügbar auf www.antikoerper-online.de. (antikoerper-online.de)
  • Immunocytochemistry/ Immunofluorescence: Acetyl-CoA Carboxylase alpha/ACACA Antibody [NBP2-89114] - Staining Acetyl CoA Carboxylase 1 (ACC1) in SiHa cells (green). (novusbio.com)
  • Immunohistochemistry-Paraffin: Acetyl-CoA Carboxylase alpha/ACACA Antibody [NBP2-89114] - Analysis of paraffin-embedded human kidney tissue using anti-Acetyl CoA Carboxylase 1 (ACC1) antibody. (novusbio.com)
  • Immunohistochemistry-Paraffin: Acetyl-CoA Carboxylase alpha/ACACA Antibody [NBP2-89114] - Analysis of paraffin-embedded rat skeletal muscle tissue using anti-Acetyl CoA Carboxylase 1 (ACC1) antibody. (novusbio.com)
  • There are two main isoforms of Acetyl-CoA carboxylase expressed in mammals, Acetyl-CoA carboxylase 1 (ACACA) and Acetyl-CoA carboxylase 2 (ACACB). (creative-enzymes.com)
  • Overexpression of HER2 in breast cancer cells is considered to induce the expression of acetyl-CoA carboxylase α (ACACA) and fatty acid synthase (FASN) through activation of mammalian target of rapamycin (mTOR) signaling pathway. (elsevier.com)
  • This peptide is used to block Acetyl-CoA Carboxylase (C83B10) Rabbit mAb #3676 or Acetyl-CoA Carboxylase Antibody #3662 reactivity by dot blot and Western blot. (cellsignal.com)
  • The peptide blocks Acetyl-CoA Carboxylase (C83B10) Rabbit mAb #3676 and Acetyl-CoA Carboxylase Antibody #3662 by dot blot and Western blot. (cellsignal.com)
  • The following product was used in this experiment: Phospho-Acetyl-CoA Carboxylase (Ser79) Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-17725, RRID AB_10981245. (thermofisher.com)
  • Acetyl CoA Carboxylase 1 antibody detects Acetyl CoA Carboxylase 1 protein at cytoplasm by immunofluorescent analysis. (genetex.com)
  • Green: Acetyl CoA Carboxylase 1 protein stained by Acetyl CoA Carboxylase 1 antibody (GTX132081) diluted at 1:500. (genetex.com)
  • Various whole cell extracts (30 µg) were separated by 5% SDS-PAGE, and the membrane was blotted with Acetyl CoA Carboxylase 1 antibody (GTX132081) diluted at 1:1000. (genetex.com)
  • Acetyl CoA Carboxylase 1 antibody detects Acetyl CoA Carboxylase 1 protein at cytoplasm in mouse cervix by immunohistochemical analysis. (genetex.com)
  • Western blot analysis of extracts from 293 cells untreated or treated with AICAR using Acetyl-CoA Carboxylase (Phospho-Ser79) Antibody. (mybiosource.com)
  • Immunohistochemical analysis of paraffin-embedded NIH/3T3 cells, untreated (left) or serum-starved (right), using Phospho-Acetyl-CoA Carboxylase (Ser79) Antibody. (cellsignal.co.uk)
  • Gentaur antibody-antibodies.com The Marketplace for Antibodies : Cloning and characterisation of multiple acetyl-CoA carboxylase transcripts in ovine adipose tissue. (antibody-antibodies.com)
  • Western blot analysis of extracts from SH-SY5Y cells, untreated or treated with Oligomycin #9996 (0.5 μM, 30 min), using Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb (upper) or Acetyl-CoA Carboxylase (C83B10) Rabbit mAb #3676 (lower). (cellsignal.com)
  • Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb. (cellsignal.com)
  • Immunohistochemical analysis of paraffin-embedded mouse liver using Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb. (cellsignal.com)
  • Immunohistochemical analysis of paraffin-embedded human lung carcinoma, untreated (left) or λ phosphatase-treated (right), using Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb. (cellsignal.com)
  • bottom right), using Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb (green). (cellsignal.com)
  • The PathScan ® Phospho-Acetyl-CoA Carboxylase (Ser79) Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of acetyl-CoA carboxylase (ACC) protein phosphorylated at Ser79 with a chemiluminescent readout. (cellsignal.jp)
  • Acetyl-CoA carboxylase (ACC) regulates synthesis and oxidation of fatty acids, and mice lacking the ACC2 isoform are leaner than wild-type animals. (sciencemag.org)
  • While both ACC1 and ACC2 produce malonyl-CoA, ACC1 is predominantly cytosolic and generates malonyl-CoA that is used by FAS to synthesize palmitic acid. (pnas.org)
  • ACC2 is associated with the mitochondrial membrane ( 9 ) and produces malonyl-CoA that serves to allosterically inhibit carnitine palmitoyl transferase I, the protein responsible for transport of long chain FAs into mitochondria for β-oxidation ( 10 ). (pnas.org)
  • Malonyl-coenzyme A (malonyl-CoA), generated by acetyl-CoA carboxylases ACC1 and ACC2, is a key metabolite in the regulation of energy homeostasis. (sciencemag.org)
  • In comparison to the wild type, Acc2-deficient mice had 10- and 30-fold lower levels of malonyl-CoA in heart and muscle, respectively. (sciencemag.org)
  • In animals, including humans, there are two isoforms of acetyl-CoA carboxylase, ACC1 [relative molecular mass ( M r ) ∼ 265,000] and ACC2 ( M r ∼ 280,000), which are encoded by separate genes and display distinct tissue distributions ( 12-16 ). (sciencemag.org)
  • Malonyl-CoA, the product of ACC1 and ACC2, is the key metabolic signal for the control of fatty acid oxidation and synthesis in response to dietary changes. (sciencemag.org)
  • Simultaneous inhibition of the acetyl-CoA carboxylase isozymes, ACC1 and ACC2, results in concomitant inhibition of fatty acid synthesis (FASyn) and stimulation of fatty acid oxidation (FAOxn) in cultured cells and in animals and impedes tumor cell growth in vitro. (aacrjournals.org)
  • We have identified ND-646, a potent, selective, allosteric inhibitor of ACC with broad tissue distribution that binds to the ACC biotin carboxylase domain and potently inhibits the dimerization and enzymatic activity of both ACC1 (IC50 = 3.5nM) and ACC2 (IC50 = 4.1nM). (aacrjournals.org)
  • CP-640186 is a potent and cell-permeable Acetyl-CoA carboxylase (ACC) inhibitor with IC 50 s of 53 nM and 61 nM for rat liver ACC1 and rat skeletal muscle ACC2 respectively. (medchemexpress.com)
  • MK-4074 is a liver-specific inhibitor of acetyl-CoA carboxylase ACC1 and ACC2 with IC 50 values of approximately 3 nM. (medchemexpress.com)
  • PF-05175157 is broad spectrum acetyl-CoA carboxylase ( ACC ) inhibitor with IC 50 s of 27.0, 33.0, 23.5 and 50.4 nM for ACC1 (human), ACC2 (human), ACC1 (rat), ACC2 (rat), respectively. (medchemexpress.com)
  • For some time, our work has focused on understanding the roles of acetyl-CoA carboxylases, ACC1 and ACC2, in the regulation of fatty acid synthesis and oxidation as related to energy homeostasis. (bcm.edu)
  • Acetyl-CoA carboxylase (ACC) in mammals is encoded by two related enzymes ACC1 and ACC2, which catalyze the ATP dependent carboxylation of acetyl-CoA to form malonyl-CoA. (medchemexpress.cn)
  • ACC1 encodes a cytoplasmic isoform that is thought to be the predominant isoform controlling FASyn, whereas ACC2 is tethered to the mitochondrial outer membrane, where localized malonyl-CoA production blocks CPT-1 function to prevent fatty acids from entering the mitochondria to undergo fatty acid oxidation (FAOxn). (medchemexpress.cn)
  • Inhibition of acetyl-CoA carboxylase (ACC), which results in inhibition of fatty acid synthesis and stimulation of fatty acid oxidation, has the potential to favorably affect a multitude of cardiovascular risk factors associated with metabolic syndrome. (nih.gov)
  • Pharmacological inhibition of acetyl-CoA carboxylase (ACC) 2 offers a promising approach to treat insulin resistance through stimulation of mitochondrial fatty acid oxidation (FAO) and reduction of IMCL deposition. (aspetjournals.org)
  • Inhibition of Acetyl-CoA Carboxylase by Phosphorylation or the Inhibitor ND-654 Suppresses Lipogenesis and Hepatocellular Carcinoma. (natureindex.com)
  • Acetyl-CoA carboxylase ( ACC ) is a biotin -dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase (BC) and carboxyltransferase (CT). (wikipedia.org)
  • Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). (cellsignal.com)
  • Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (By similarity). (uniprot.org)
  • Multifunctional enzyme that catalyzes the carboxylation of acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty acid synthesis and in the cytosol in various biosynthetic pathways including fatty acid elongation. (uniprot.org)
  • a biotin-containing enzyme which participates in the synthesis of fatty acids by catalyzing the carboxylation reaction in which acetyl-CoA is converted to malonyl-CoA. (thefreedictionary.com)
  • ACC1 catalyzes acetyl-CoA carboxylation, producing malonyl-CoA, a metabolite involved in energy homeostasis regulation. (novusbio.com)
  • ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. (thermofisher.com)
  • Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. (nih.gov)
  • This enzyme catalzes the formation of Malonyl CoA through the irreversible carboxylation of acetyl CoA. (creative-enzymes.com)
  • One unit will cause the carboxylation of 1 picomole of acetyl-CoA per minute at pH 7.4 at 30 deg C. (creative-enzymes.com)
  • Malonyl Coenzyme A (lithium) is formed by the Acetyl CoA Carboxylase -mediated carboxylation of acetyl CoA . (medchemexpress.com)
  • Cytosolic enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty acid biosynthesis (PubMed:20952656, PubMed:20457939, PubMed:29899443). (rcsb.org)
  • This is a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (PubMed:20952656, PubMed:20457939, PubMed:29899443). (rcsb.org)
  • Consists of an N-terminal biotin carboxylation/carboxylase (BC) domain that catalyzes the ATP-dependent transient carboxylation of the biotin covalently attached to the central biotinyl-binding/biotin carboxyl carrier (BCC) domain (Probable). (rcsb.org)
  • The ATP-dependent carboxylation of acetyl CoA to yield malonyl CoA is a primary reaction that occurs during de novo fatty acid biosynthesis. (plantphysiol.org)
  • 2004) also indicated that reduced lipogenesis in the mammary gland of lactating mice was caused by reducing acetyl CoA carboxylase activity and mRNA abundance of acetyl CoA carboxylase , the critical enzyme in de novo fatty acid synthesis, and also inhibited mammary desaturation by reducing mammary stearoyl-CoA desaturase activity and mRNA abundance. (thefreedictionary.com)
  • During mammary-gland differentiation of control or tumour-carrying animals, the activities of acetyl-CoA carboxylase and fatty acid synthase in the lactating gland increased by about 40-50-fold over the values found in non-pregnant animals. (biochemj.org)
  • However, a comparison of the immunotitration and immunodiffusion experiments indicated that the mammary-gland acetyl-CoA carboxylase might differ from the enzyme present in mammary neoplasms. (biochemj.org)
  • Regulation of acetyl-CoA carboxylase in rat mammary gland. (biochemj.org)
  • The 'initial' (I), endogenous phosphatase-activated (A) and citrate-activated (C) activities of acetyl-CoA carboxylase were measured in mammary-gland extracts of pregnant and lactating rats. (biochemj.org)
  • It is suggested that the initial activity of acetyl-CoA carboxylase in rat mammary gland is regulated by at least two parallel mechanisms: (i) an acute regulation of the proportion of the enzyme in the active state and (ii) a longer-term modulation of enzyme concentration in the gland. (biochemj.org)
  • It is suggested that acetyl-CoA carboxylase activity is rate-limiting for lipogenesis in the mammary gland in normal, fed, suckled or weaned animals but that in starved and short-term diabetic animals changes in the activity of the enzyme by covalent modification alone may not be sufficient to maintain the enzyme in its rate-limiting role. (biochemj.org)
  • Hardie, DG & Cohen, P 1979, ' Dephosphorylation and activation of Acetyl-CoA-carboxylase from lactating rabbit mammary gland ', FEBS Letters , vol. 103, no. 2, pp. 333-338. (dundee.ac.uk)
  • Phosphorylation state of acetyl-coenzyme A carboxylase. (wikipedia.org)
  • In bacteria, the acetyl coenzyme A carboxylase (ACC) is a complex consisting of two subunits: alpha and beta. (ebi.ac.uk)
  • Acetyl-coenzyme A (acetyl-CoA) carboxylase (ACC) catalyzes the synthesis of malonyl-CoA, a metabolite that plays a pivotal role in the synthesis of fatty acids as the donor of "C 2 units" ( 1-3 ) and in the oxidation of fatty acid as the regulator of the mitochondrial shuttle system ( 4 , 5 ). (sciencemag.org)
  • Acetyl-coenzyme A carboxylase (ACCase) inhibitors consist a group of commercially important, very effective and, selective graminicides which are applied postemergence and introduced since 1970s. (frontiersin.org)
  • Antibodies in the Chromocyte database for ACACB / Acetyl Coenzyme A (CoA) Carboxylase 2 / Beta and biotin. (chromocyte.com)
  • The BirA-catalyzed reaction involves the covalent attachment of biotin to AccB, a subunit of acetyl coenzyme (acetyl-CoA) carboxylase. (asm.org)
  • Tong L (2005) Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery. (springer.com)
  • Olumacostat glasaretil is a small molecule inhibitor of acetyl coenzyme A carboxylase (ACC). (adooq.cn)
  • A multisubunit form of acetyl coenzyme A (CoA) carboxylase (ACCase) from soybean ( Glycine max ) was characterized. (plantphysiol.org)
  • Lipogenic enzymes fatty acid synthase and acetyl-coenzyme A carboxylase are coexpressed with sterol regulatory element binding protein and Ki-67 in fetal tissues. (biomedsearch.com)
  • Acetyl-coenzyme A carboxylase α (ACC-alpha) is considered as the key regulatory enzyme in fatty acid biosynthesis. (ac.ir)
  • In a screen for mutants that display synthetic lethal interaction with hpr1 Δ, a hyperrecombination mutant of Saccharomyces cerevisiae , we have isolated a novel cold-sensitive allele of the acetyl coenzyme A (CoA) carboxylase gene, acc1 cs , encoding the rate-limiting enzyme of fatty acid synthesis. (asm.org)
  • This screen yielded a novel cold-sensitive allele of the acetyl coenzyme A (CoA) carboxylase gene, acc1-200 cs , hereafter referred to as acc1 cs ( 14 ). (asm.org)
  • In addition, adiponectin inhibits gluconeogenesis by phosphorylating AMPK and acetyl-CoA carboxylase (ACC) [11]. (thefreedictionary.com)
  • Metformin treatment for 10 weeks significantly increased AMPK α2 activity in the skeletal muscle, and this was associated with increased phosphorylation of AMPK on Thr172 and decreased acetyl-CoA carboxylase-2 activity. (diabetesjournals.org)
  • AICAR increased AMPK and acetyl-CoA carboxylase phosphorylation to a similar extent in skeletal muscle from subjects with type 2 diabetes and nondiabetic subjects. (diabetesjournals.org)
  • This study was designed to compare functional effects of phosphorylation of muscle acetyl-CoA carboxylase (ACC) by adenosine 3',5'-cyclic monophosphate-dependent protein kinase (PKA) and by AMP-activated protein kinase (AMPK). (utmb.edu)
  • Phosphorylation by AMPK increased the K(m) (for) ATP and acetyl-CoA. (utmb.edu)
  • Biocomposition of neurites shows that lipids form a major part of neurites and AMPK is known to regulate lipid metabolism majorly through acetyl CoA carboxylase (ACC). (iisc.ac.in)
  • 17,18 Moreover, the activation of AMPK also leads to phosphorylation of acetyl-CoA carboxylase (ACC) and inhibits its activity. (rsc.org)
  • The cDNAs encoding chloroplastic acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) from three lines of Setaria viridis (L. Beauv. (nih.gov)
  • Kozaki, Akiko 2013-06-04 00:00:00 Plastidic acetyl-CoA carboxylase (ACCase) regulates the rate of fatty acid synthesis. (deepdyve.com)
  • Fluazifop-P-butyl, a graminicide from arylophenoxypropionate group, is a acetyl-CoA carboxylase (ACCase) inhibitor. (medchemexpress.com)
  • The four known components that constitute plastid ACCase are biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and the α- and β-subunits of carboxyltransferase (α- and β-CT). (plantphysiol.org)
  • Acetyl-CoA carboxylase (ACCase) is a key enzyme in the fatty acid synthesis and elongation pathways in algae, where ACCase exists in two locations (cytosol and plastid) and in two forms (homomeric and heteromeric). (edu.au)
  • CARBOXYLASE ACTIVITY ABSTRACT biotin carboxylase, biotin carboxylase carrier protein, and the alpha and beta transcarboxylase domains. (presentica.com)
  • 4 Acetyl-CoA Carboxylase beta (ACACB) Proteine von 3 Herstellern verfügbar auf www.antikoerper-online.de. (antikoerper-online.de)
  • ACACB (Acetyl-CoA Carboxylase Beta) is a Protein Coding gene. (genecards.org)
  • Diseases associated with ACACB include Acetyl-Coa Carboxylase-Beta Deficiency and Biotin Deficiency . (genecards.org)
  • announced results from a Phase 2, randomized, placebo-controlled trial evaluating two doses of GS-0976, an oral, investigational inhibitor of Acetyl-CoA carboxylase , in patients with nonalcoholic steatohepatitis. (thefreedictionary.com)
  • A separate Phase 2 study is investigating treatment with GS-9674, the investigational apoptosis signal-regulating kinase 1 inhibitor selonsertib, and the investigational acetyl-CoA carboxylase inhibitor GS-0976 alone or in combination, in patients with advanced fibrosis due to NASH. (thefreedictionary.com)
  • The study combines the apoptosis signal-regulating kinase 1 inhibitor selonsertib with either the acetyl-CoA carboxylase inhibitor GS-0976 or the selective, non-steroidal Farnesoid X receptor agonist GS-9674. (thefreedictionary.com)
  • Acetyl-CoA carboxylase is responsible for synthesis of Malonyl-CoA which is an inhibitor of fatty acid oxidation in skeletal muscle mitochondria. (creative-enzymes.com)
  • Propaquizafop is a phenoxyisopropionic acid herbicide and an acetyl-coA carboxylase inhibitor. (medchemexpress.com)
  • TOFA (RMI14514;MDL14514) is an allosteric inhibitor of acetyl-CoA carboxylase -α ( ACCA ). (medchemexpress.com)
  • Firsocostat is an acetyl-CoA carboxylase ( ACC ) inhibitor. (medchemexpress.com)
  • ND-646 is an orally bioavailable and steric inhibitor of acetyl-CoA carboxylase ( ACC ) with IC 50 s of 3.5 nM and 4.1 nM for recombinant hACC1 and hACC2, respectively. (medchemexpress.com)
  • Ac-CoA Synthase Inhibitor1 is a potent, reversible acetate-dependent acetyl-CoA synthetase 2 (ACSS2) inhibitor with an IC 50 of 0.6 µM. (medchemexpress.com)
  • CMS-121 is a quinolone derivative and an orally active acetyl-CoA carboxylase 1 (ACC1) inhibitor. (medchemexpress.com)
  • Inhibition of protein phosphatase-1 via phosphorylation of inhibitor-1 is therefore unlikely to be the mechanism by which cyclic-AMP-dependent protein kinase indirectly increases phosphorylation of acetyl-CoA carboxylase. (duke.edu)
  • First, we examined whether protein restriction affected expression of acetyl CoA carboxylase (ACC), a major lipogenic enzyme. (thefreedictionary.com)
  • Acetyl-CoA carboxylase 1 (ACC1) is a biotin dependent lipogenic enzyme that is highly expressed during adipogenesis. (novusbio.com)
  • Here, we define the lipogenic enzyme acetyl-CoA carboxylase (ACC) 1 as a key player in breast cancer metastasis. (tum.de)
  • In Escherichia coli , accA encodes the alpha subunit of the acetyl-CoA carboxylase, [6] and accD encodes its beta subunit. (wikipedia.org)
  • The putative gene encoding acetyl-CoA carboxylase, accA, has been isolated from Aspergillus nidulans. (nih.gov)
  • Screening Pfizer's compound library resulted in the identification of weak acetyl-CoA carboxylase inhibitors, from which were obtained rACC1 CT-domain co-crystal structures. (osti.gov)
  • We found that Acetyl-CoA carboxylase (ACC) inhibitors offer significant potential for the treatment of type 2 diabetes mellitus (T2DM), hepatic steatosis, and cancer. (osti.gov)
  • that show that the company has identified a series of novel, highly potent, and highly selective Acetyl CoA Carboxylase (ACC)1/2 allosteric inhibitors. (thefreedictionary.com)
  • Isozyme-nonselective N-substituted bipiperidylcarboxamide acetyl-CoA carboxylase inhibitors reduce tissue malonyl-CoA concentrations, inhibit fatty acid synthesis, and increase fatty acid oxidation in cultured cells and in experimental animals. (medchemexpress.com)
  • Design, synthesis, and structure-activity relationships of spirolactones bearing 2-ureidobenzothiophene as acetyl-CoA carboxylases inhibitors. (medchemexpress.com)
  • These structural insights into drug-biotin carboxylase interactions will be tested experimentally in in vitro and in vivo systems to increase the potency of amino-oxazole inhibitors towards both Gram-negative as well as Gram-positive species. (mdpi.com)
  • This enzyme is composed of biotin carboxyl carrier protein (BCCP), biotin carboxylase (BC), and carboxyltransferase (CT), which consists of α and β subunits. (deepdyve.com)
  • Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. (mybiosource.com)
  • The Proscan™ and the NetPhos 2.0™ algorithms were used to predict protein kinase phosphorylation sites on the biotin carboxylase and the carboxyltransferase domains of the enzyme. (ukzn.ac.za)
  • In bacteria, the enzyme is composed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. (mdpi.com)
  • They contain biotin carboxylase (BC), carboxyltransferase (CT), and biotin-carboxyl carrier protein components. (springer.com)
  • Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. (pnas.org)
  • Recombinant protein within Human Acetyl CoA Carboxylase 1 (ACC1) aa 1150-1400. (novusbio.com)
  • Recombinant protein encompassing a sequence within the C-terminus region of human Acetyl CoA Carboxylase 1. (genetex.com)
  • R.W. Brownsey, W.A. Hughes, R.M. Denton and R.J. Mayer, Demon stration of the phosphorylation of acetyl-CoA carboxylase within intact rat epididymal fat cells, Biochem. (springer.com)
  • The biotindependent enzyme acetyl-CoA carboxylase catalyses the commitment step in de novo fatty acid biosynthesis in several organisms. (ukzn.ac.za)
  • A key fatty acid synthesis enzyme, acetyl-CoA carboxylase alpha (ACC-alpha), has been shown to be highly expressed in human breast cancer and other tumor types and also to specifically interact with the protein coded by one of two major breast cancer susceptibility genes BRCA1. (ox.ac.uk)
  • Expression of the genes coding for plastidic acetyl-CoA carboxylase subunits is regulated by a. (deepdyve.com)
  • Hydroxycitric acid lactone catalyzes the extramitochondrial cleavage of citrate to oxaloacetate and acetyl-CoA , limits the availability of acetyl-CoA units required for fatty acid synthesis. (medchemexpress.com)
  • The C-terminal carboxyl transferase (CT) domain catalyzes the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA to produce malonyl-CoA (Probable). (rcsb.org)
  • Acetyl-CoA carboxylase catalyzes the committed and regulated step in fatty acid synthesis. (mdpi.com)
  • Acetyl-CoA carboxylase (ACC) is a biotin carboxylase that catalyzes the ATP-dependent condensation of acetyl-CoA and carbonate to form malonyl-CoA. (medchemexpress.cn)
  • The enzyme catalyzes the formation of malonyl CoA from acetyl CoA, a rate-limiting step in fatty acid biosynthesis. (plantphysiol.org)
  • Crystallographic structures of E. coli acetyl-CoA carboxylase Biotin carboxylase subunit of E. coli acetyl-CoA carboxylase Biotin carboxyl carrier protein subunit of E. coli acetyl-CoA carboxylase Carboxyl transferase subunit of E. coli acetyl-CoA carboxylase The polypeptides composing the multi-subunit ACCs of prokaryotes and plants are encoded by distinct genes. (wikipedia.org)
  • 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. (rupress.org)
  • We analyzed Acc-1 (plastid acetyl-CoA carboxylase) and Pgk-1 (plastid 3-phosphoglycerate kinase) genes to determine phylogenetic relationships among Triticum and Aegilops species of the wheat lineage and to establish the timeline of wheat evolution based on gene sequence comparisons. (qxmd.com)
  • The activities of two lipogenic enzymes, acetyl-CoA carboxylase and fatty acid synthase, were determined in two transplantable mammary adenocarcinomas (13762 and R3230AC) carried by non-pregnant, pregnant and lactating rats, and in mammary tissue of control animals (non-tumour-carrying) of comparable physiological states. (biochemj.org)
  • A subset of 9 × 10 6 of these compounds were subjected to structure-based virtual screening against seven biotin carboxylase isoforms using similarity-based docking by e SimDock. (mdpi.com)
  • Mammalian acetyl-CoA carboxylase (ACC) is present in two isoforms , alpha and beta, both of which catalyze formation of malonyl- CoA by fixing CO2 into acetyl-CoA . (bvsalud.org)
  • As a first step to answer this question and to identify the possible role of ACC isoforms in myogenic differentiation, we have investigated in the present study whether the expression and the subcellular distribution of ACC isoforms in H9c2 cardiac myocyte change so that malonyl- CoA produced by each form may modulate fatty acid oxidation . (bvsalud.org)
  • That this second ACC-like gene encodes the 280-kDa carboxylase is not ruled out. (pnas.org)
  • Acetyl-CoA carboxylase mRNA was detected by RT-PCR performed on total RNA isolated from P. yoelii 17XL-infected mouse erythrocytes using primers designed from PY01695 ORF of the Plasmodb-published MALPY00458 gene of P. yoelii 17XNL. (ukzn.ac.za)
  • A 1 kb region of the P. yoelii acetyl-CoA carboxylase gene containing the biotinoyl domain was cloned and expressed in E. coli as 66 kD GST-tag and 45 kD His-tag protein. (ukzn.ac.za)
  • Joezy-Shekalgorabi, S., Moradi Shahr-e-babak, H., Abbasi Firoozjaei, M., Ghorbani, A. Genetic Polymorphism Detection of the Exon 1 Region of Acetyl-CoA Carboxylase Alpha Gene in Iranian Mahabadi Goat Breed. (ac.ir)
  • Haplotype-based analysis of common variation in the acetyl-coA carboxylase alpha gene and breast cancer risk: a case-control study nested within the European Prospective Investigation into Cancer and Nutrition. (ox.ac.uk)
  • The acetyl-CoA carboxylase gene, ACC1 , encodes a biotin-containing enzyme that synthesizes malonyl-CoA from acetyl-CoA and bicarbonate, with the hydrolysis of ATP ( 4 ). (asm.org)
  • Biotin-dependent carboxylases include acetyl-CoA carboxylase (ACC), propionyl-CoA carboxylase (PCC), 3-methylcrotonyl-CoA carboxylase (MCC), geranyl-CoA carboxylase, pyruvate carboxylase (PC), and urea carboxylase (UC). (springer.com)
  • Biotin carboxylase (BC) activity, biotin carboxyl carrier protein (BCCP), and carboxyl transferase (CT) activity are each contained on a different subunit. (wikipedia.org)
  • We report here that bio operon expression is down-regulated by overproduction of AccC, another acetyl-CoA carboxylase subunit known to form a complex with AccB. (asm.org)
  • Cronan JE Jr, Waldrop GL (2002) Multi-subunit acetyl-CoA carboxylases. (springer.com)
  • 3. The (Rp)-[thio]phosphate analogue of cyclic AMP, which is an antagonist of binding of cyclic AMP to the regulatory subunit of cyclic-AMP-dependent protein kinase, opposes the effect of adrenaline on phosphorylation and inactivation of acetyl-CoA carboxylase. (duke.edu)
  • Regulation of purified rat liver acetyl CoA carboxylase by phosphorylation. (thefreedictionary.com)
  • The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. (thermofisher.com)
  • A.P. Halestrap and R.M. Denton, Hormonal regulation of adipose tissue acetyl-CoA carboxylase by changes in the polymeric state of the enzyme, Biochem. (springer.com)
  • A.L. Witters, D. Moriarty, and D.B. Martin, Regulation of hepatic acetyl-CoA carboxylase by insulin and glucagon, Biol. (springer.com)
  • R.W. Brownsey, W.H. Hughes, and R.M. Denton, Adrenaline and the regulation of acetyl-CoA carboxylase in rat epididymal adipose tissue. (springer.com)
  • May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA-dependent inhibition of carnitine palmitoyltransferase 1 (By similarity). (nih.gov)
  • Also in the liver, fructose induces mRNA expression from Glut-2, Glut-5, fatty acid synthase (FAS), and acetyl-CoA carboxylase (ACC1) [29]. (thefreedictionary.com)
  • 4. As shown by okadaic acid inhibition, greater than 95% of the acetyl-CoA carboxylase phosphatase activity in extracts of rat adipocytes or liver is accounted for by protein phosphatase-2A, with less than 5% attributable to protein phosphatase-1. (duke.edu)
  • [5] ACC functional regions, starting from the N-terminus to C-terminus are the biotin carboxylase (BC), biotin binding (BB), carboxyl transferase (CT), and ATP-binding (AB). (wikipedia.org)
  • [9] The carboxybiotin translocates to the carboxyl transferase (CT) active site, where the carboxyl group is transferred to acetyl-CoA. (wikipedia.org)
  • ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine-palmitoyl-CoA transferase I, the rate-limiting step in fatty acid uptake and oxidation by mitochondria. (nih.gov)
  • Acetyl-CoA carboxylase β is expressed primarily in heart and skeletal muscle, where it may play a role in the control of mitochondrial fatty acid uptake and oxidation by controlling carnitine-palmitoyl-CoA transferase 1. (kribb.re.kr)
  • ACC1 is regulated short-term by citrate, CoA, and palmitoyl-CoA through allosteric interactions. (novusbio.com)
  • Citrate is produced in the mitochondria and is used as a substrate by ATP citrate lyase (ACL), which converts citrate to acetyl-CoA, the substrate of ACC. (pnas.org)
  • The Acetyl-CoA Carboxylase enzymes are activated by Citrate, glutamate, and dicarboxylic acids and negatively regulated by long and short chain fatty acyl CoAs. (creative-enzymes.com)
  • The catalytic function of ACCα is regulated by phosphorylation (inactive) and dephosphorylation (active) of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA, which serve as the enzyme's short-term regulatory mechanism. (huabio.com)
  • Roles of the AMP-activated and cyclic-AMP-dependent protein kinases in the adrenaline-induced inactivation of acetyl-CoA carboxylase in rat adipocytes. (duke.edu)
  • Acetyl-CoA carboxylase (ACC) catalyses the formation of malonyl-CoA, an essential substrate for fatty acid synthesis in lipogenic tissues and a key regulatory molecule in muscle, brain and other tissues. (portlandpress.com)
  • These include acetyl CoA carboxylase , the rate limiting enzyme that initiates fatty acid synthesis. (thefreedictionary.com)
  • Malonyl-CoA is a two carbon donor in the synthesis of long-chain fatty acids and the elongation of fatty acids found in the cystol (1). (novusbio.com)
  • Acetyl-CoA carboxylase (ACC), the first committed enzyme in fatty acid (FA) synthesis, is regulated by phosphorylation/dephosphorylation, transcription, and an unusual mechanism of protein polymerization. (pnas.org)
  • Insulin stimulates fatty acid synthesis in adipose and other tissues by increasing acetyl-CoA carboxylase activity. (springer.com)
  • 6,7,8,9 Inhibition of fatty acid synthesis by hormones such as adrenaline and glucagon involves decreases in acetyl-CoA carboxylase activity. (springer.com)
  • Among the critical unanswered questions are whether malonyl-CoA pools exist that differentially control fatty acid oxidation and synthesis, whether these putative pools can be independently manipulated, and if so, what would be the physiological consequences of such manipulation. (sciencemag.org)
  • The rate-limiting enzyme in fatty acid synthesis, acetyl-CoA carboxylase (ACC), has been shown to be highly expressed in human breast cancer. (aacrjournals.org)
  • Acetyl-CoA carboxylase 1 deficiency (ACACAD): An inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth. (nih.gov)
  • Erb TJ, Berg IA, Brecht V, Muller M, Fuchs G, Alber BE (2007) Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway. (springer.com)
  • Intracellular lipid depletion triggers proteolytic cleavage of SREBP, allowing the amino terminus to enter the nucleus and activate the expression of enzymes, including acetyl-CoA carboxylase (ACC) and fatty acid synthase (FAS), major biosynthetic enzymes for fatty acid synthesis. (biomedsearch.com)
  • Acetyl-CoA carboxylase (ACC) is the rate-limiting enzyme in fatty acid synthesis and oxidative metabolism .More and more researches confirm that ACC is highly expressed in many tumors ,and is closely related to tumor progression and prognosis of patients ,which makes ACC as a potential marker for clinical diagnosis and prognosis . (bvsalud.org)
  • 19 Inactivation of ACC reduces the synthesis of malonyl-CoA, which in turn activates carnitine palmitoyltransferase-1A (CPT-1A) and increases fatty acid oxidation. (rsc.org)
  • The most important function of ACC is to provide the malonyl-CoA substrate for the biosynthesis of fatty acids . (wikipedia.org)
  • The carboxyl group is transferred from biotin to acetyl CoA to form malonyl CoA in the second reaction, which is catalyzed by CT. (wikipedia.org)
  • The resulting enolate attacks CO2 to form malonyl CoA. (wikipedia.org)
  • When the enzyme is active, the product, malonyl-CoA, is produced which is a building block for new fatty acids and can inhibit the transfer of the fatty acyl group from acyl CoA to carnitine with carnitine acyltransferase, which inhibits the beta-oxidation of fatty acids in the mitochondria. (wikipedia.org)
  • 6 ) and functions to carboxylate acetyl-CoA to form malonyl-CoA. (pnas.org)
  • The malonyl-CoA produced by ACC can be used by FA synthase (FAS) for the sequential 2-carbon elongation reactions that generate palmitic acid (C16:0) in the cytosol. (pnas.org)
  • The enzyme may be used to study the effect on production of malonyl-CoA as well as fatty acid oxidation during exercise. (creative-enzymes.com)
  • The malonyl-CoA produced by ACC serves two major physiologic functions. (medchemexpress.cn)
  • The second step results in the transfer of the carboxyl from carboxybiotin to acetyl CoA to form malonyl CoA. (plantphysiol.org)
  • The malonyl CoA generated by the cytoplasmic and chloroplast enzymes are used for different purposes. (plantphysiol.org)
  • Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase. (rupress.org)
  • Hence, ACC links fatty acid and carbohydrate metabolism through the shared intermediate acetyl-CoA, the product of pyruvate dehydrogenase. (sciencemag.org)
  • Plasmodium yoelii acetyl-coa carboxylase : detection and characterisation of the recombinant biotinoyl domain. (ukzn.ac.za)
  • This study describes the detection of acetyl-CoA carboxylase and the partial characterisation of the biotinoyl domain of the enzyme of the mouse malaria parasite, Plasmodium yoelii. (ukzn.ac.za)
  • Cloning and characterisation of multiple acetyl-CoA carboxylase transcripts in ovine adipose tissue. (antibody-antibodies.com)
  • The mRNAs encoding several yield-related enzymes including acetyl CoA carboxylase , glucosyltransferase, phosphate translocator, and lipoxygenase were reprogrammed by nucleotide solutions with concomitant changes in the accumulation of cellulosic biomass and vegetable oil in peanut [11, 12, 14]. (thefreedictionary.com)
  • The cDNA inserts that were used as probes were those homologous to rRNA, and to mRNAs encoding acetyl CoA carboxylase (ACC), lipoxygenase (LO), glucosyltransferase, inorganic phosphate translocator, nitrate reductase, and glycinamide ribonucleotide (GAR) synthetase/GAR transformylase. (thefreedictionary.com)
  • Thus, the two substrates of this enzyme are ATP and acetyl-CoA carboxylase , whereas its two products are ADP and acetyl-CoA carboxylase phosphate. (omicsgroup.org)
  • A full-length ovine acetyl-CoA carboxylase-encoding cDNA (ACC) has been cloned from adipose tissue and completely sequenced. (antibody-antibodies.com)
  • All of the members in this family are biotin dependent carboxylases [ PMID: 8102604 , PMID: 8366018 ]. (ebi.ac.uk)
  • Molecular evolution of biotin-dependent carboxylases. (ebi.ac.uk)