Acetyl-CoA Carboxylase: 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.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Pyruvate Carboxylase: 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.Ligases: 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.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Systems Integration: The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Ribulose-Bisphosphate Carboxylase: 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.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Energy Metabolism: The chemical reactions involved in the production and utilization of various forms of energy in cells.Fatty Acids: 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)Obesity: A status with BODY WEIGHT that is grossly above the acceptable or desirable weight, usually due to accumulation of excess FATS in the body. The standards may vary with age, sex, genetic or cultural background. In the BODY MASS INDEX, a BMI greater than 30.0 kg/m2 is considered obese, and a BMI greater than 40.0 kg/m2 is considered morbidly obese (MORBID OBESITY).Insulin: 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).Insulin Resistance: Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS.Adipose Tissue: 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.Mice, Knockout: Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.Methylmalonyl-CoA Decarboxylase: 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.Biotin: 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.Carbon-Carbon Ligases: 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.ATP Citrate (pro-S)-Lyase: 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.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Coenzyme APhosphoenolpyruvate Carboxylase: 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.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Triple Negative Breast Neoplasms: Breast neoplasms that do not express ESTROGEN RECEPTORS; PROGESTERONE RECEPTORS; and do not overexpress the NEU RECEPTOR/HER-2 PROTO-ONCOGENE PROTEIN.Treatment Outcome: Evaluation undertaken to assess the results or consequences of management and procedures used in combating disease in order to determine the efficacy, effectiveness, safety, and practicability of these interventions in individual cases or series.Breast Neoplasms: Tumors or cancer of the human BREAST.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.Receptors, Progesterone: Specific proteins found in or on cells of progesterone target tissues that specifically combine with progesterone. The cytosol progesterone-receptor complex then associates with the nucleic acids to initiate protein synthesis. There are two kinds of progesterone receptors, A and B. Both are induced by estrogen and have short half-lives.Receptors, Estrogen: Cytoplasmic proteins that bind estrogens and migrate to the nucleus where they regulate DNA transcription. Evaluation of the state of estrogen receptors in breast cancer patients has become clinically important.Receptor, erbB-2: A cell surface protein-tyrosine kinase receptor that is overexpressed in a variety of ADENOCARCINOMAS. It has extensive homology to and heterodimerizes with the EGF RECEPTOR, the ERBB-3 RECEPTOR, and the ERBB-4 RECEPTOR. Activation of the erbB-2 receptor occurs through heterodimer formation with a ligand-bound erbB receptor family member.Cell Line, Tumor: A cell line derived from cultured tumor cells.Acetyl Coenzyme A: 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.Carboxyl and Carbamoyl Transferases: A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.Malonyl Coenzyme A: A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.Electronic Mail: Messages between computer users via COMPUTER COMMUNICATION NETWORKS. This feature duplicates most of the features of paper mail, such as forwarding, multiple copies, and attachments of images and other file types, but with a speed advantage. The term also refers to an individual message sent in this way.Rape: Unlawful sexual intercourse without consent of the victim.GlobulinsPolylysine: A peptide which is a homopolymer of lysine.Protamines: A group of simple proteins that yield basic amino acids on hydrolysis and that occur combined with nucleic acid in the sperm of fish. Protamines contain very few kinds of amino acids. Protamine sulfate combines with heparin to form a stable inactive complex; it is used to neutralize the anticoagulant action of heparin in the treatment of heparin overdose. (From Merck Index, 11th ed; Martindale, The Extra Pharmacopoeia, 30th ed, p692)Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Accounts Payable and Receivable: Short-term debt obligations and assets occurring in the regular course of operational transactions.Molecular Sequence Data: 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.Fatty Acid Synthase, Type I: Animal form of fatty acid synthase which is encoded by a single gene and consists of seven catalytic domains and is functional as a homodimer. It is overexpressed in some NEOPLASMS and is a target in humans of some ANTINEOPLASTIC AGENTS and some ANTI-OBESITY AGENTS.Mammary Glands, Animal: MAMMARY GLANDS in the non-human MAMMALS.Pregnancy, Animal: The process of bearing developing young (EMBRYOS or FETUSES) in utero in non-human mammals, beginning from FERTILIZATION to BIRTH.Fatty Acid Synthase, Type II: 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.Pregnancy: The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH.Lactation: The processes of milk secretion by the maternal MAMMARY GLANDS after PARTURITION. The proliferation of the mammary glandular tissue, milk synthesis, and milk expulsion or let down are regulated by the interactions of several hormones including ESTRADIOL; PROGESTERONE; PROLACTIN; and OXYTOCIN.AMP-Activated Protein Kinases: 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.Aminoimidazole Carboxamide: An imidazole derivative which is a metabolite of the antineoplastic agents BIC and DIC. By itself, or as the ribonucleotide, it is used as a condensation agent in the preparation of nucleosides and nucleotides. Compounded with orotic acid, it is used to treat liver diseases.CitratesMultienzyme Complexes: 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.Ribonucleotides: Nucleotides in which the purine or pyrimidine base is combined with ribose. (Dorland, 28th ed)Starvation: Lengthy and continuous deprivation of food. (Stedman, 25th ed)Prolactin: A lactogenic hormone secreted by the adenohypophysis (PITUITARY GLAND, ANTERIOR). It is a polypeptide of approximately 23 kD. Besides its major action on lactation, in some species prolactin exerts effects on reproduction, maternal behavior, fat metabolism, immunomodulation and osmoregulation. Prolactin receptors are present in the mammary gland, hypothalamus, liver, ovary, testis, and prostate.Diabetes Mellitus, Experimental: Diabetes mellitus induced experimentally by administration of various diabetogenic agents or by PANCREATECTOMY.Streptozocin: An antibiotic that is produced by Stretomyces achromogenes. It is used as an antineoplastic agent and to induce diabetes in experimental animals.
(1/960) 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.

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)

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

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)

(3/960) 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.

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)

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

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)

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

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)

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

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)

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

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)

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

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)

*  Fatty acid metabolism
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 ...
*  Acetyl-CoA carboxylase
... (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to ... Lee CK, Cheong HK, Ryu KS, Lee JI, Lee W, Jeon YH, Cheong C (August 2008). "Biotinoyl domain of human acetyl-CoA carboxylase: ... Boone AN, Chan A, Kulpa JE, Brownsey RW (April 2000). "Bimodal Activation of Acetyl-CoA Carboxylase by Glutamate". J Biol Chem ... Brownsey RW, Boone AN, Elliott JE, Kulpa JE, Lee WM (April 2006). "Regulation of acetyl-CoA carboxylase". Biochem. Soc. Trans. ...
*  acetyl-CoA carboxylase)-phosphatase
... acetyl-CoA carboxylase]-phosphatase (EC 3.1.3.44) is an enzyme that catalyzes the chemical reaction [acetyl-CoA carboxylase] ... acetyl-CoA carboxylase] + phosphate Thus, the two substrates of this enzyme are acetyl-CoA carboxylase phosphate and H2O, ... Krakower GR; Kim K-H (1980). "Purification and properties of acetyl-CoA carboxylase phosphatase". J. Biol. Chem. 256 (5): 2408- ... whereas its two products are acetyl-CoA carboxylase and phosphate. This enzyme belongs to the family of hydrolases, ...
*  Biotin-(acetyl-CoA-carboxylase) ligase
... acetyl-CoA carboxylase] synthetase, biotin-[acetyl coenzyme A carboxylase] synthetase, acetyl coenzyme A holocarboxylase ... acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) is an enzyme that catalyzes the chemical reaction ATP + biotin + apo-[acetyl-CoA: ... acetyl-CoA:carbon-dioxide ligase (ADP-forming)] The 3 substrates of this enzyme are ATP, biotin, and apo-[acetyl-CoA:carbon- ... The systematic name of this enzyme class is biotin:apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming). ...
*  Morpheein
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 ...
*  ACACB
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 ...
*  ACACA
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 ...
*  Natalie Strynadka
"Leptin activates hypothalamic acetyl-CoA carboxylase to inhibit food intake". Proceedings of the National Academy of Sciences. ...
*  Biotin carboxylase
This enzyme is also called biotin carboxylase (component of acetyl CoA carboxylase). This enzyme participates in fatty acid ... "Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase". Biochemistry. 33 (34): 10249-10256. ... molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase". Proc. Natl. Acad. Sci. U.S.A. 67 (3): 1353 ... In enzymology, a biotin carboxylase (EC 6.3.4.14) is an enzyme that catalyzes the chemical reaction ATP + biotin-carboxyl- ...
*  Protein kinase A
For example, protein kinase A phosphorylates acetyl-CoA carboxylase and pyruvate dehydrogenase. Such covalent modification has ...
*  AMP-activated protein kinase
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 ...
*  Acetylcarnitine
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 ⇌ {\displaystyle \rightleftharpoons } CoA + acetylcarnitine where the acetyl group displaces the ... acetyl-CoA is the primary substrate for the Krebs cycle, once it is de-acetylated, it must be re-charged with an acetyl-group ...
*  Pantethine
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 ...
*  M. Daniel Lane
... 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 ...
*  Protein kinase, AMP-activated, alpha 1
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 ...
*  PRKAA2
... 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 ...
*  PRKAB2
... 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. ...
*  Long-chain-fatty-acid-CoA ligase
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 ...
*  Schrödinger (company)
"GILEAD SCIENCES ANNOUNCES ACQUISITION OF NIMBUS THERAPEUTICS' ACETYL-COA CARBOXYLASE (ACC) PROGRAM FOR NASH AND OTHER LIVER ... and its Acetyl-CoA Carboxylase (ACC) inhibitor program. Nimbus Therapeutics will receive an upfront payment of $400 million, ... "Gilead Sciences Announces Acquisition of Nimbus Therapeutics' Acetyl-CoA Carboxlyase (ACC) Program for NASH and Other Liver ...
*  Aquatic Species Program
Acetyl-CoA carboxylase (ACCase) is an enzyme which catalyzes a key metabolic step in the synthesis of oils in algae. The ...
*  Adipocyte
By controlling the activity of the pyruvate dehydrogenase and the acetyl-CoA carboxylase enzymes, insulin promotes unsaturated ...
*  Pyruvate cycling
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- ...
*  Tumor metabolome
... 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 ( ...
*  3-Hydroxypropionate bicycle
... 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 ...
*  Randle cycle
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 ...
*  Metabolism
... acetyl-CoA), which releases some energy. Finally, the acetyl group on the CoA is oxidised to water and carbon dioxide in the ... Miziorko H, Lorimer G (1983). "Ribulose-1,5-bisphosphate carboxylase-oxygenase". Annu Rev Biochem. 52: 507-35. doi:10.1146/ ... and this breakdown process involves the release of significant amounts of acetyl-CoA, propionyl-CoA, and pyruvate, which can ... The glycerol enters glycolysis and the fatty acids are broken down by beta oxidation to release acetyl-CoA, which then is fed ...
*  Liang Tong
His lab focuses on enzymes involved in fatty acid metabolism, including Acetyl-CoA carboxylase, carnitine acyltransferase, AMP- ...
Studies on acetyl-CoA carboxylase and fatty acid synthase from rat mammary gland and mammary tumours | Biochemical Journal  Studies on acetyl-CoA carboxylase and fatty acid synthase from rat mammary gland and mammary tumours | Biochemical Journal
Studies on acetyl-CoA carboxylase and fatty acid synthase from rat mammary gland and mammary tumours. P M Ahmad, D S Feltman, F ... Studies on acetyl-CoA carboxylase and fatty acid synthase from rat mammary gland and mammary tumours ... On the other hand, in tumours carried by lactating dams there were only modest increases (1.5-2-fold) in acetyl-CoA carboxylase ... Studies on acetyl-CoA carboxylase and fatty acid synthase from rat mammary gland and mammary tumours ...
more infohttp://www.biochemj.org/content/208/2/443
Genetic Polymorphism Detection of the Exon 1 Region of Acetyl-CoA Carboxylase Alpha Gene in Iranian Mahabadi Goat Breed  Genetic Polymorphism Detection of the Exon 1 Region of Acetyl-CoA Carboxylase Alpha Gene in Iranian Mahabadi Goat Breed
Acetyl-coenzyme A carboxylase α (ACC-alpha) is considered as the key regulatory enzyme in fatty acid biosynthesis. ACC-alpha ... CoA carboxylase α gene (ACC-alpha) and can catalyze irreversible carboxylation of Acetyl-coA for producing malonyl-CoA (Badaoui ... Acetyl-CoA carboxylase α (ACC-alpha) is the key regulatory enzyme in fatty acid biosynthesis. This biotin-dependent enzyme is ... Barber M.C., Price N.T. and Travers M.T. (2005). Structure and regulation of acetyl-CoA carboxylase genes of metazoa. Biochim. ...
more infohttp://ijas.iaurasht.ac.ir/article_516657.html
Structural impact of human and Escherichia coli biotin carboxyl carrier proteins on biotin attachment. - The Kennedy Institute...  Structural impact of human and Escherichia coli biotin carboxyl carrier proteins on biotin attachment. - The Kennedy Institute...
... the biotin-attachment domain fragments from human propionyl-CoA carboxylase and E. coli acetyl-CoA carboxylase, respectively. ... This study suggests that the thumb loop found in bacterial carboxylases interferes with optimal interaction with the mammalian ... that is found in carboxylases in most organisms. Numerous studies have indicated that HCS and BirA, as well as biotin protein ... the biotin-attachment domain fragments from human propionyl-CoA carboxylase and E. coli acetyl-CoA carboxylase, respectively. ...
more infohttps://www.kennedy.ox.ac.uk/publications/108531
Acetyl-CoA carboxylase (IPR034733) | InterPro | EMBL-EBI  Acetyl-CoA carboxylase (IPR034733) | InterPro | EMBL-EBI
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 ...
more infohttps://www.ebi.ac.uk/interpro/entry/IPR034733
Targeting Acetyl-CoA Carboxylase to Stay Lean | Science Signaling  Targeting Acetyl-CoA Carboxylase to Stay Lean | Science Signaling
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 ...
more infohttp://stke.sciencemag.org/content/2007/409/tw387
PREDICTED: acetyl-CoA carboxylase isoform X2 [Microplitis demolitor] - Protein - NCBI  PREDICTED: acetyl-CoA carboxylase isoform X2 [Microplitis demolitor] - Protein - NCBI
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. ...
more infohttps://www.ncbi.nlm.nih.gov/protein/XP_008546338.1
Anti-Acetyl CoA Carboxylase Antibody, Unconjugated from Cell Signaling Technology  Anti-Acetyl CoA Carboxylase Antibody, Unconjugated from Cell Signaling Technology
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 ...
more infohttp://www.bio-medicine.org/biology-products/Anti-Acetyl-CoA-Carboxylase-Antibody--Unconjugated-from-Cell-Signaling-Technology-5285-1/
CST - Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb  CST - Phospho-Acetyl-CoA Carboxylase (Ser79) (D7D11) Rabbit mAb
... 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 ...
more infohttps://www.cellsignal.com/products/primary-antibodies/phospho-acetyl-coa-carboxylase-ser79-d7d11-rabbit-mab/11818?N=102236+4294960669+4294956287&fromPage=plp
Regulation of acetyl-CoA carboxylase | Biochemical Society Transactions | Portland Press  Regulation of acetyl-CoA carboxylase | Biochemical Society Transactions | Portland Press
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 ...
more infohttps://portlandpress.com/biochemsoctrans/article-abstract/34/2/223/63741/Regulation-of-acetyl-CoA-carboxylase
accA acetyl-CoA carboxylase carboxyl transferase subunit alpha [Streptococcus mutans UA159] - Gene - NCBI  accA acetyl-CoA carboxylase carboxyl transferase subunit alpha [Streptococcus mutans UA159] - Gene - NCBI
acetyl-CoA carboxylase carboxyl transferase subunit alpha. Locus tag. SMU_1734. Gene type. protein coding. RefSeq status. ... acetyl-CoA carboxylase carboxyl transferase subunit alpha. NP_722061.1. *Best Blastp Hit: gb,AAF98281.1,AF197933_11 (AF197933) ... accA acetyl-CoA carboxylase carboxyl transferase subunit alpha [ Streptococcus mutans UA159 ] Gene ID: 1028945, updated on 15- ... NP_722061.1 acetyl-CoA carboxylase subunit alpha [Streptococcus mutans UA159]. See identical proteins and their annotated ...
more infohttps://www.ncbi.nlm.nih.gov/gene?term=SMU.1734
Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. | PNAS  Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. | PNAS
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. ...
more infohttps://www.pnas.org/content/92/9/4011?ijkey=af87d607fd0564b7b0fcf32c76edd300b67e7e72&keytype2=tf_ipsecsha
anti-Acetyl-CoA Carboxylase 1 antibody  | GeneTex  anti-Acetyl-CoA Carboxylase 1 antibody | GeneTex
... 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: ...
more infohttp://www.genetex.com/Acetyl-CoA-Carboxylase-1-antibody-GTX132081.html
Acetyl CoA carboxylase | definition of acetyl CoA carboxylase by Medical dictionary  Acetyl CoA carboxylase | definition of acetyl CoA carboxylase by Medical dictionary
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, ...
more infohttps://medical-dictionary.thefreedictionary.com/acetyl+CoA+carboxylase
Discovery of spirocyclic-diamine inhibitors of mammalian acetyl CoA-carboxylase (Journal Article) | DOE PAGES  Discovery of spirocyclic-diamine inhibitors of mammalian acetyl CoA-carboxylase (Journal Article) | DOE PAGES
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 ...
more infohttps://www.osti.gov/pages/biblio/1250604-discovery-spirocyclic-diamine-inhibitors-mammalian-acetyl-coa-carboxylase
ACC1 - Acetyl-CoA carboxylase 1 - Oryza sativa subsp. japonica (Rice) - ACC1 gene & protein  ACC1 - Acetyl-CoA carboxylase 1 - Oryza sativa subsp. japonica (Rice) - ACC1 gene & protein
... 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 ...
more infohttp://www.uniprot.org/uniprot/Q8S6N5
Acetyl-CoA Carboxylase alpha ELISA & Assay Kits  Acetyl-CoA Carboxylase alpha ELISA & Assay Kits
Compare and order Acetyl-CoA Carboxylase alpha ELISA Kits. View citations, images, detection ranges, sensitivity, prices and ... acetyl-CoA carboxylase 1 , acetyl-coenzyme A carboxylase alpha , acetyl-CoA carboxylase-alpha , ACC , acetyl-CoA carboxylase , ... Acetyl-CoA Carboxylase alpha Antigen Profile Antigen Summary Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme ... Acetyl-CoA Carboxylase alpha in AMPK Signaling * Acetyl-CoA Carboxylase alpha in AMPK Signaling ...
more infohttps://www.antibodies-online.com/ampk-signaling-pathway-15/acetyl-coa-carboxylase-alpha-elisa-kit-2004/
Human Acetyl-CoA Carboxylase alpha ELISA Kit | Product No. ABIN810228  Human Acetyl-CoA Carboxylase alpha ELISA Kit | Product No. ABIN810228
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 ...
more infohttps://www.antibodies-online.com/kit/810228/Acetyl-CoA+Carboxylase+alpha+ACACA+ELISA+Kit/
Acetyl-CoA carboxylase - Wikipedia  Acetyl-CoA carboxylase - Wikipedia
Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to ... Lee CK, Cheong HK, Ryu KS, Lee JI, Lee W, Jeon YH, Cheong C (August 2008). "Biotinoyl domain of human acetyl-CoA carboxylase: ... Boone AN, Chan A, Kulpa JE, Brownsey RW (April 2000). "Bimodal Activation of Acetyl-CoA Carboxylase by Glutamate". J Biol Chem ... Brownsey RW, Boone AN, Elliott JE, Kulpa JE, Lee WM (April 2006). "Regulation of acetyl-CoA carboxylase". Biochem. Soc. Trans. ...
more infohttps://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase
acetyl-CoA carboxylase)-phosphatase - Wikipedia  acetyl-CoA carboxylase)-phosphatase - Wikipedia
... acetyl-CoA carboxylase]-phosphatase (EC 3.1.3.44) is an enzyme that catalyzes the chemical reaction [acetyl-CoA carboxylase] ... acetyl-CoA carboxylase] + phosphate Thus, the two substrates of this enzyme are acetyl-CoA carboxylase phosphate and H2O, ... Krakower GR; Kim K-H (1980). "Purification and properties of acetyl-CoA carboxylase phosphatase". J. Biol. Chem. 256 (5): 2408- ... whereas its two products are acetyl-CoA carboxylase and phosphate. This enzyme belongs to the family of hydrolases, ...
more infohttps://en.wikipedia.org/wiki/(acetyl-CoA_carboxylase)-phosphatase
The Role of Phosphorylation in the Regulation of Acetyl-CoA Carboxylase Activity by Insulin and other Hormones | SpringerLink  The Role of Phosphorylation in the Regulation of Acetyl-CoA Carboxylase Activity by Insulin and other Hormones | SpringerLink
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 ...
more infohttps://link.springer.com/chapter/10.1007/978-1-4757-0166-1_31
Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase. | JCB  Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase. | JCB
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. ...
more infohttp://jcb.rupress.org/content/134/4/949?ijkey=2df5e0431da7432a2d0f76d2a8d4effb9634a6dd&keytype2=tf_ipsecsha
Frontiers | Study of Fitness Cost in Three Rigid Ryegrass Populations Susceptible and Resistant to Acetyl-CoA Carboxylase...  Frontiers | Study of Fitness Cost in Three Rigid Ryegrass Populations Susceptible and Resistant to Acetyl-CoA Carboxylase...
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 ...
more infohttps://www.frontiersin.org/articles/10.3389/fevo.2016.00142/full
Abstract 4452: Liver selective acetyl-CoA carboxylase inhibition by ND-654 improves survival in cirrhotic rats with...  Abstract 4452: Liver selective acetyl-CoA carboxylase inhibition by ND-654 improves survival in cirrhotic rats with...
Liver selective acetyl-CoA carboxylase inhibition by ND-654 improves survival in cirrhotic rats with hepatocellular carcinoma ... Simultaneous inhibition of the acetyl-CoA carboxylase isozymes, ACC1 and ACC2, results in concomitant inhibition of fatty acid ... Abstract 4452: Liver selective acetyl-CoA carboxylase inhibition by ND-654 improves survival in cirrhotic rats with ... Abstract 4452: Liver selective acetyl-CoA carboxylase inhibition by ND-654 improves survival in cirrhotic rats with ...
more infohttp://cancerres.aacrjournals.org/content/75/15_Supplement/4452
Abstract 1048: Modulation of lipid metabolism through inhibition of acetyl-CoA carboxylase with ND-646 leads to potent...  Abstract 1048: Modulation of lipid metabolism through inhibition of acetyl-CoA carboxylase with ND-646 leads to potent...
The rate-limiting enzyme in fatty acid synthesis, acetyl-CoA carboxylase (ACC), has been shown to be highly expressed in human ... Modulation of lipid metabolism through inhibition of acetyl-CoA carboxylase with ND-646 leads to potent inhibition of breast ... Abstract 1048: Modulation of lipid metabolism through inhibition of acetyl-CoA carboxylase with ND-646 leads to potent ... Abstract 1048: Modulation of lipid metabolism through inhibition of acetyl-CoA carboxylase with ND-646 leads to potent ...
more infohttp://cancerres.aacrjournals.org/content/76/14_Supplement/1048
  • The regulation of mammalian ACC is complex, in order to control two distinct pools of malonyl CoA that direct either the inhibition of beta oxidation or the activation of lipid biosynthesis. (wikipedia.org)
  • 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. (genetex.com)
  • Regulation of purified rat liver acetyl CoA carboxylase by phosphorylation. (thefreedictionary.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)
  • In April 2016, Nimbus announced that Gilead will acquire Nimbus Apollo, Inc., a wholly owned subsidiary of Nimbus Therapeutics, and its Acetyl-CoA Carboxylase (ACC) inhibitor program. (wikipedia.org)