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.
Coenzyme A is an essential coenzyme that plays a crucial role in various metabolic processes, particularly in the transfer and activation of acetyl groups in important biochemical reactions such as fatty acid synthesis and oxidation, and the citric acid cycle.
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.
"Citrates, in a medical context, are compounds containing citric acid, often used in medical solutions for their chelating properties and as a part of certain types of nutritional support."
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.
Mevalonic acid is a crucial intermediate compound in the HMG-CoA reductase pathway, which is a metabolic route that produces cholesterol, other steroids, and isoprenoids in cells.
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.
Pentosephosphates are monosaccharides, specifically pentoses, that have a phosphate group attached, playing crucial roles in carbohydrate metabolism, such as being intermediates in the pentose phosphate pathway and serving as precursors for nucleotide synthesis.
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.
Pyruvates, in the context of medical and biochemistry definitions, are molecules that result from the final step of glycolysis, containing a carboxylic acid group and an aldehyde group, playing a crucial role in cellular metabolism, including being converted into Acetyl-CoA to enter the Krebs cycle or lactate under anaerobic conditions.
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.
"Malate" is a term used in biochemistry to refer to a salt or ester of malic acid, a dicarboxylic acid found in many fruits and involved in the citric acid cycle, but it does not have a specific medical definition as such.
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)

Acetyl-CoA carboxylase (ACCA) is a biotin-dependent enzyme that plays a crucial role in fatty acid synthesis. It catalyzes the conversion of acetyl-CoA to malonyl-CoA, which is the first and rate-limiting step in the synthesis of long-chain fatty acids. The reaction catalyzed by ACCA is as follows:

acetyl-CoA + HCO3- + ATP + 2H+ --> malonyl-CoA + CoA + ADP + Pi + 2H2O

ACCA exists in two isoforms, a cytosolic form (ACC1) and a mitochondrial form (ACC2). ACC1 is primarily involved in fatty acid synthesis, while ACC2 is responsible for the regulation of fatty acid oxidation. The activity of ACCA is regulated by several factors, including phosphorylation/dephosphorylation, allosteric regulation, and transcriptional regulation. Dysregulation of ACCA has been implicated in various metabolic disorders, such as obesity, insulin resistance, and non-alcoholic fatty liver disease.

Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.

Biotin is a water-soluble vitamin, also known as Vitamin B7 or Vitamin H. It is a cofactor for several enzymes involved in metabolism, particularly in the synthesis and breakdown of fatty acids, amino acids, and carbohydrates. Biotin plays a crucial role in maintaining healthy skin, hair, nails, nerves, and liver function. It is found in various foods such as nuts, seeds, whole grains, milk, and vegetables. Biotin deficiency is rare but can occur in people with malnutrition, alcoholism, pregnancy, or certain genetic disorders.

Pyruvate carboxylase is a biotin-containing enzyme that plays a crucial role in gluconeogenesis, the process of generating new glucose molecules from non-carbohydrate sources. The enzyme catalyzes the conversion of pyruvate to oxaloacetate, an important intermediate in several metabolic pathways, particularly in the liver, kidneys, and brain.

The reaction catalyzed by pyruvate carboxylase is as follows:

Pyruvate + CO2 + ATP + H2O → Oxaloacetate + ADP + Pi + 2H+

In this reaction, pyruvate reacts with bicarbonate (HCO3-) to form oxaloacetate, consuming one molecule of ATP in the process. The generation of oxaloacetate provides a key entry point for non-carbohydrate precursors, such as lactate and certain amino acids, to enter the gluconeogenic pathway.

Pyruvate carboxylase deficiency is a rare but severe genetic disorder that can lead to neurological impairment and developmental delays due to the disruption of energy metabolism in the brain.

Coenzyme A, often abbreviated as CoA or sometimes holo-CoA, is a coenzyme that plays a crucial role in several important chemical reactions in the body, particularly in the metabolism of carbohydrates, fatty acids, and amino acids. It is composed of a pantothenic acid (vitamin B5) derivative called pantothenate, an adenosine diphosphate (ADP) molecule, and a terminal phosphate group.

Coenzyme A functions as a carrier molecule for acetyl groups, which are formed during the breakdown of carbohydrates, fatty acids, and some amino acids. The acetyl group is attached to the sulfur atom in CoA, forming acetyl-CoA, which can then be used as a building block for various biochemical pathways, such as the citric acid cycle (Krebs cycle) and fatty acid synthesis.

In summary, Coenzyme A is a vital coenzyme that helps facilitate essential metabolic processes by carrying and transferring acetyl groups in the body.

Methylmalonyl-CoA decarboxylase is a mitochondrial enzyme that plays a crucial role in the metabolism of certain amino acids and fatty acids. Specifically, it catalyzes the conversion of methylmalonyl-CoA to propionyl-CoA through the decarboxylation of the thioester bond.

The reaction is as follows:

Methylmalonyl-CoA → Propionyl-CoA + CO2

This enzyme requires biotin as a cofactor, and its activity is reduced in individuals with methylmalonic acidemia, a rare inherited metabolic disorder caused by mutations in the MMAB or MCEE genes that encode subunits of the methylmalonyl-CoA decarboxylase enzyme complex.

Deficiency of this enzyme leads to an accumulation of methylmalonic acid and methylmalonyl-CoA, which can cause metabolic acidosis, hyperammonemia, and other symptoms associated with the disorder.

AMP-activated protein kinases (AMPK) are a group of heterotrimeric enzymes that play a crucial role in cellular energy homeostasis. They are composed of a catalytic subunit (α) and two regulatory subunits (β and γ). AMPK is activated under conditions of low energy charge, such as ATP depletion, hypoxia, or exercise, through an increase in the AMP:ATP ratio.

Once activated, AMPK phosphorylates and regulates various downstream targets involved in metabolic pathways, including glycolysis, fatty acid oxidation, and protein synthesis. This results in the inhibition of energy-consuming processes and the promotion of energy-producing processes, ultimately helping to restore cellular energy balance.

AMPK has been implicated in a variety of physiological processes, including glucose and lipid metabolism, autophagy, mitochondrial biogenesis, and inflammation. Dysregulation of AMPK activity has been linked to several diseases, such as diabetes, obesity, cancer, and neurodegenerative disorders. Therefore, AMPK is an attractive target for therapeutic interventions in these conditions.

Fatty acid synthases (FAS) are a group of enzymes that are responsible for the synthesis of fatty acids in the body. They catalyze a series of reactions that convert acetyl-CoA and malonyl-CoA into longer chain fatty acids, which are then used for various purposes such as energy storage or membrane formation.

The human genome encodes two types of FAS: type I and type II. Type I FAS is a large multifunctional enzyme complex found in the cytoplasm of cells, while type II FAS consists of individual enzymes located in the mitochondria. Both types of FAS play important roles in lipid metabolism, but their regulation and expression differ depending on the tissue and physiological conditions.

Inhibition of FAS has been explored as a potential therapeutic strategy for various diseases, including cancer, obesity, and metabolic disorders. However, more research is needed to fully understand the complex mechanisms regulating FAS activity and its role in human health and disease.

Acetyl Coenzyme A, often abbreviated as Acetyl-CoA, is a key molecule in metabolism, particularly in the breakdown and oxidation of carbohydrates, fats, and proteins to produce energy. It is a coenzyme that plays a central role in the cellular process of transforming the energy stored in the chemical bonds of nutrients into a form that the cell can use.

Acetyl-CoA consists of an acetyl group (two carbon atoms) linked to coenzyme A, a complex organic molecule. This linkage is facilitated by an enzyme called acetyltransferase. Once formed, Acetyl-CoA can enter various metabolic pathways. In the citric acid cycle (also known as the Krebs cycle), Acetyl-CoA is further oxidized to release energy in the form of ATP, NADH, and FADH2, which are used in other cellular processes. Additionally, Acetyl-CoA is involved in the biosynthesis of fatty acids, cholesterol, and certain amino acids.

In summary, Acetyl Coenzyme A is a vital molecule in metabolism that connects various biochemical pathways for energy production and biosynthesis.

Malonyl Coenzyme A (CoA) is not a medical term per se, but rather a biochemical concept. Here's the scientific or biochemical definition:

Malonyl Coenzyme A is an important intermediate in various metabolic pathways, particularly in fatty acid synthesis. It is formed through the reaction between malonic acid and coenzyme A, catalyzed by the enzyme acetyl-CoA carboxylase. Malonyl CoA plays a crucial role in the elongation step of fatty acid synthesis, where it provides the two-carbon unit that is added to a growing fatty acid chain.

In a medical context, understanding the function and regulation of Malonyl CoA metabolism can be relevant for several pathological conditions, including metabolic disorders like diabetes and obesity.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Carbon-carbon ligases are a type of enzyme that catalyze the formation of carbon-carbon bonds between two molecules. These enzymes play important roles in various biological processes, including the biosynthesis of natural products and the metabolism of carbohydrates and lipids.

Carbon-carbon ligases can be classified into several categories based on the type of reaction they catalyze. For example, aldolases catalyze the condensation of an aldehyde or ketone with another molecule to form a new carbon-carbon bond and a new carbonyl group. Other examples include the polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs), which are large multienzyme complexes that catalyze the sequential addition of activated carbon units to form complex natural products.

Carbon-carbon ligases are important targets for drug discovery and development, as they play critical roles in the biosynthesis of many disease-relevant molecules. Inhibitors of these enzymes have shown promise as potential therapeutic agents for a variety of diseases, including cancer, infectious diseases, and metabolic disorders.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a crucial enzyme in the Calvin cycle, which is a process that plants use to convert carbon dioxide into glucose during photosynthesis. RuBisCO catalyzes the reaction between ribulose-1,5-bisphosphate and carbon dioxide, resulting in the formation of two molecules of 3-phosphoglycerate, which can then be converted into glucose.

RuBisCO is considered to be the most abundant enzyme on Earth, making up as much as 50% of the soluble protein found in leaves. It is a large and complex enzyme, consisting of eight small subunits and eight large subunits that are arranged in a barrel-shaped structure. The active site of the enzyme, where the reaction between ribulose-1,5-bisphosphate and carbon dioxide takes place, is located at the interface between two large subunits.

RuBisCO also has a secondary function as an oxygenase, which can lead to the production of glycolate, a toxic compound for plants. This reaction occurs when the enzyme binds with oxygen instead of carbon dioxide and is more prevalent in environments with low carbon dioxide concentrations and high oxygen concentrations. The glycolate produced during this process needs to be recycled through a series of reactions known as photorespiration, which can result in significant energy loss for the plant.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

Phosphoenolpyruvate carboxylase (PEP-carboxylase or PEPC) is a biotin-dependent enzyme that plays a crucial role in the carbon fixation process of photosynthesis, specifically in the C4 and CAM (Crassulacean Acid Metabolism) plant pathways. It is also found in some bacteria and archaea.

PEP-carboxylase catalyzes the irreversible reaction between phosphoenolpyruvate (PEP) and bicarbonate (HCO3-) to form oxaloacetate and inorganic phosphate (Pi). This reaction helps to initiate the carbon fixation process by incorporating atmospheric carbon dioxide into an organic molecule, which can then be used for various metabolic processes.

In C4 plants, PEP-carboxylase is primarily located in the mesophyll cells where it facilitates the initial fixation of CO2 onto PEP, forming oxaloacetate. This oxaloacetate is then reduced to malate, which is subsequently transported to bundle sheath cells for further metabolism and additional carbon fixation by another enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO).

In CAM plants, PEP-carboxylase operates at night to fix CO2 into malate, which is stored in vacuoles. During the day, malate is decarboxylated, releasing CO2 for RuBisCO-mediated carbon fixation while conserving water through reduced stomatal opening.

PEP-carboxylase is also found in some non-photosynthetic bacteria and archaea, where it contributes to various metabolic pathways such as gluconeogenesis, anaplerotic reactions, and the glyoxylate cycle.

Lipid metabolism is the process by which the body breaks down and utilizes lipids (fats) for various functions, such as energy production, cell membrane formation, and hormone synthesis. This complex process involves several enzymes and pathways that regulate the digestion, absorption, transport, storage, and consumption of fats in the body.

The main types of lipids involved in metabolism include triglycerides, cholesterol, phospholipids, and fatty acids. The breakdown of these lipids begins in the digestive system, where enzymes called lipases break down dietary fats into smaller molecules called fatty acids and glycerol. These molecules are then absorbed into the bloodstream and transported to the liver, which is the main site of lipid metabolism.

In the liver, fatty acids may be further broken down for energy production or used to synthesize new lipids. Excess fatty acids may be stored as triglycerides in specialized cells called adipocytes (fat cells) for later use. Cholesterol is also metabolized in the liver, where it may be used to synthesize bile acids, steroid hormones, and other important molecules.

Disorders of lipid metabolism can lead to a range of health problems, including obesity, diabetes, cardiovascular disease, and non-alcoholic fatty liver disease (NAFLD). These conditions may be caused by genetic factors, lifestyle habits, or a combination of both. Proper diagnosis and management of lipid metabolism disorders typically involves a combination of dietary changes, exercise, and medication.

Adipose tissue, also known as fatty tissue, is a type of connective tissue that is composed mainly of adipocytes (fat cells). It is found throughout the body, but is particularly abundant in the abdominal cavity, beneath the skin, and around organs such as the heart and kidneys.

Adipose tissue serves several important functions in the body. One of its primary roles is to store energy in the form of fat, which can be mobilized and used as an energy source during periods of fasting or exercise. Adipose tissue also provides insulation and cushioning for the body, and produces hormones that help regulate metabolism, appetite, and reproductive function.

There are two main types of adipose tissue: white adipose tissue (WAT) and brown adipose tissue (BAT). WAT is the more common form and is responsible for storing energy as fat. BAT, on the other hand, contains a higher number of mitochondria and is involved in heat production and energy expenditure.

Excessive accumulation of adipose tissue can lead to obesity, which is associated with an increased risk of various health problems such as diabetes, heart disease, and certain types of cancer.

Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.

Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.

Examples of carboxy-lyases include:

1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

Insulin is a hormone produced by the beta cells of the pancreatic islets, primarily in response to elevated levels of glucose in the circulating blood. It plays a crucial role in regulating blood glucose levels and facilitating the uptake and utilization of glucose by peripheral tissues, such as muscle and adipose tissue, for energy production and storage. Insulin also inhibits glucose production in the liver and promotes the storage of excess glucose as glycogen or triglycerides.

Deficiency in insulin secretion or action leads to impaired glucose regulation and can result in conditions such as diabetes mellitus, characterized by chronic hyperglycemia and associated complications. Exogenous insulin is used as a replacement therapy in individuals with diabetes to help manage their blood glucose levels and prevent long-term complications.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

"Inbred strains of rats" are genetically identical rodents that have been produced through many generations of brother-sister mating. This results in a high degree of homozygosity, where the genes at any particular locus in the genome are identical in all members of the strain.

Inbred strains of rats are widely used in biomedical research because they provide a consistent and reproducible genetic background for studying various biological phenomena, including the effects of drugs, environmental factors, and genetic mutations on health and disease. Additionally, inbred strains can be used to create genetically modified models of human diseases by introducing specific mutations into their genomes.

Some commonly used inbred strains of rats include the Wistar Kyoto (WKY), Sprague-Dawley (SD), and Fischer 344 (F344) rat strains. Each strain has its own unique genetic characteristics, making them suitable for different types of research.

Propionates, in a medical context, most commonly refer to a group of medications that are used as topical creams or gels to treat fungal infections of the skin. Propionic acid and its salts, such as propionate, are the active ingredients in these medications. They work by inhibiting the growth of fungi, which causes the infection. Common examples of propionate-containing medications include creams used to treat athlete's foot, ringworm, and jock itch.

It is important to note that there are many different types of medications and compounds that contain the word "propionate" in their name, as it refers to a specific chemical structure. However, in a medical context, it most commonly refers to antifungal creams or gels.

Acetates, in a medical context, most commonly refer to compounds that contain the acetate group, which is an functional group consisting of a carbon atom bonded to two hydrogen atoms and an oxygen atom (-COO-). An example of an acetate is sodium acetate (CH3COONa), which is a salt formed from acetic acid (CH3COOH) and is often used as a buffering agent in medical solutions.

Acetates can also refer to a group of medications that contain acetate as an active ingredient, such as magnesium acetate, which is used as a laxative, or calcium acetate, which is used to treat high levels of phosphate in the blood.

In addition, acetates can also refer to a process called acetylation, which is the addition of an acetyl group (-COCH3) to a molecule. This process can be important in the metabolism and regulation of various substances within the body.

Acetate-CoA ligase is an enzyme that plays a role in the metabolism of acetate in cells. The enzyme catalyzes the conversion of acetate and coenzyme A (CoA) to acetyl-CoA, which is a key molecule in various metabolic pathways, including the citric acid cycle (also known as the Krebs cycle).

The reaction catalyzed by Acetate-CoA ligase can be summarized as follows:

acetate + ATP + CoA → acetyl-CoA + AMP + PPi

In this reaction, acetate is activated by combining it with ATP to form acetyl-AMP, which then reacts with CoA to produce acetyl-CoA. The reaction also produces AMP and pyrophosphate (PPi) as byproducts.

There are two main types of Acetate-CoA ligases: the short-chain fatty acid-CoA ligase, which is responsible for activating acetate and other short-chain fatty acids, and the acyl-CoA synthetase, which activates long-chain fatty acids. Both types of enzymes play important roles in energy metabolism and the synthesis of various biological molecules.

Carbon-Nitrogen (C-N) ligases are a class of enzymes that catalyze the joining of a carbon atom from a donor molecule to a nitrogen atom in an acceptor molecule through a process called ligase reaction. This type of enzyme plays a crucial role in various biological processes, including the biosynthesis of amino acids, nucleotides, and other biomolecules that contain both carbon and nitrogen atoms.

C-N ligases typically require ATP or another energy source to drive the reaction forward, as well as cofactors such as metal ions or vitamins to facilitate the chemical bond formation between the carbon and nitrogen atoms. The specificity of C-N ligases varies depending on the enzyme, with some acting only on specific donor and acceptor molecules while others have broader substrate ranges.

Examples of C-N ligases include glutamine synthetase, which catalyzes the formation of glutamine from glutamate and ammonia, and asparagine synthetase, which catalyzes the formation of asparagine from aspartate and ammonia. Understanding the function and regulation of C-N ligases is important for understanding various biological processes and developing strategies to modulate them in disease states.

I'd be happy to help! However, I believe there might be a slight misunderstanding in your question. Mitochondria are organelles found in the cells of all complex living organisms, including humans, while the liver is a large, solid organ located in the upper right portion of the abdomen. They don't have a medical definition together. I can certainly provide you with separate definitions for each:

1. Mitochondria: These are double-membrane-bound cellular organelles that generate most of the chemical energy needed to power the cell's biochemical reactions. Commonly known as the "powerhouse of the cell," mitochondria convert organic substrates, such as glucose, fatty acids, and amino acids, into adenosine triphosphate (ATP) through a process called oxidative phosphorylation. Mitochondria are dynamic structures that can change their shape, size, and number through fission (division) and fusion (merging) processes. They play essential roles in various cellular functions, including calcium signaling, apoptosis (programmed cell death), and the regulation of cellular metabolism.

2. Liver: The liver is a large, lobulated organ that lies mainly in the upper right portion of the abdominal cavity, just below the diaphragm. It plays a crucial role in various physiological functions, such as detoxification, protein synthesis, metabolism, and nutrient storage. The liver is responsible for removing toxins from the bloodstream, producing bile to aid in digestion, regulating glucose levels, synthesizing plasma proteins, and storing glycogen, vitamins, and minerals. It also contributes to the metabolism of carbohydrates, lipids, and amino acids, helping maintain energy homeostasis in the body.

I hope this clarifies any confusion! If you have any further questions or need more information, please don't hesitate to ask.

Acetyl-L-carnitine, also known as ALCAR, is a form of the amino acid carnitine. It is a naturally occurring substance in the body that plays a crucial role in energy production in cells, particularly within mitochondria, the "powerhouses" of the cell.

Acetyl-L-carnitine is involved in the transport of fatty acids into the mitochondria, where they can be broken down to produce energy. It also functions as an antioxidant, helping to protect cells from damage caused by free radicals.

This compound has been studied for its potential benefits in various medical conditions, including neurological disorders, cardiovascular diseases, and liver diseases. Some research suggests that Acetyl-L-carnitine may help improve cognitive function, reduce fatigue, and alleviate pain. However, more studies are needed to confirm these findings and establish the optimal dosage and safety profiles for different medical conditions.

It is important to note that while Acetyl-L-carnitine is available as a dietary supplement, its use should be discussed with a healthcare provider before starting any new supplement regimen, especially if you have a medical condition or are taking medication.

Citrates are the salts or esters of citric acid, a weak organic acid that is naturally found in many fruits and vegetables. In a medical context, citrates are often used as a buffering agent in intravenous fluids to help maintain the pH balance of blood and other bodily fluids. They are also used in various medical tests and treatments, such as in urine alkalinization and as an anticoagulant in kidney dialysis solutions. Additionally, citrate is a component of some dietary supplements and medications.

Rhizobium etli is a gram-negative, aerobic, motile, non-spore forming bacteria that belongs to the Rhizobiaceae family. It has the ability to fix atmospheric nitrogen in a symbiotic relationship with certain leguminous plants, particularly common bean (Phaseolus vulgaris). This bacterium infects the roots of these plants and forms nodules where it converts nitrogen gas into ammonia, a form that can be used by the plant for growth. The nitrogen-fixing ability of Rhizobium etli makes it an important bacteria in agriculture and environmental science.

Magnesium compounds refer to substances that contain magnesium (an essential mineral) combined with other elements. These compounds are formed when magnesium atoms chemically bond with atoms of other elements. Magnesium is an alkaline earth metal and it readily forms stable compounds with various elements due to its electron configuration.

Examples of magnesium compounds include:

1. Magnesium oxide (MgO): Also known as magnesia, it is formed by combining magnesium with oxygen. It has a high melting point and is used in various applications such as refractory materials, chemical production, and agricultural purposes.
2. Magnesium hydroxide (Mg(OH)2): Often called milk of magnesia, it is a common antacid and laxative. It is formed by combining magnesium with hydroxide ions.
3. Magnesium chloride (MgCl2): This compound is formed when magnesium reacts with chlorine gas. It has various uses, including as a de-icing agent, a component in fertilizers, and a mineral supplement.
4. Magnesium sulfate (MgSO4): Also known as Epsom salts, it is formed by combining magnesium with sulfur and oxygen. It is used as a bath salt, a laxative, and a fertilizer.
5. Magnesium carbonate (MgCO3): This compound is formed when magnesium reacts with carbon dioxide. It has various uses, including as a fire retardant, a food additive, and a dietary supplement.

These are just a few examples of the many different magnesium compounds that exist. Each compound has its unique properties and applications based on the elements it is combined with.

Acetyltransferases are a type of enzyme that facilitates the transfer of an acetyl group (a chemical group consisting of an acetyl molecule, which is made up of carbon, hydrogen, and oxygen atoms) from a donor molecule to a recipient molecule. This transfer of an acetyl group can modify the function or activity of the recipient molecule.

In the context of biology and medicine, acetyltransferases are important for various cellular processes, including gene expression, DNA replication, and protein function. For example, histone acetyltransferases (HATs) are a type of acetyltransferase that add an acetyl group to the histone proteins around which DNA is wound. This modification can alter the structure of the chromatin, making certain genes more or less accessible for transcription, and thereby influencing gene expression.

Abnormal regulation of acetyltransferases has been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the function and regulation of these enzymes is an important area of research in biomedicine.

Carboxyl transferases and carbamoyl transferases are two types of enzymes that play a crucial role in various metabolic pathways by transferring a carboxyl or carbamoyl group from one molecule to another. Here are the medical definitions for both:

1. Carboxyl Transferases: These are a class of enzymes that catalyze the transfer of a carboxyl group (-COOH) from one molecule to another. They play an essential role in several metabolic processes, such as the synthesis and degradation of amino acids, carbohydrates, lipids, and other biomolecules. One example of a carboxyl transferase is pyruvate carboxylase, which catalyzes the addition of a carboxyl group to pyruvate, forming oxaloacetate in the gluconeogenesis pathway.
2. Carbamoyl Transferases: These are enzymes that facilitate the transfer of a carbamoyl group (-CONH2) from one molecule to another. They participate in various metabolic reactions, including the synthesis of essential compounds like arginine, pyrimidines, and urea. An example of a carbamoyl transferase is ornithine carbamoyltransferase (OCT), which catalyzes the transfer of a carbamoyl group from carbamoyl phosphate to ornithine during the urea cycle.

Both carboxyl and carbamoyl transferases are vital for maintaining proper cellular function and homeostasis in living organisms, including humans. Dysregulation or deficiency of these enzymes can lead to various metabolic disorders and diseases.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Acetyl-CoA C-acetyltransferase (also known as acetoacetyl-CoA thiolase or just thiolase) is an enzyme involved in the metabolism of fatty acids and ketone bodies. Specifically, it catalyzes the reaction that converts two molecules of acetyl-CoA into acetoacetyl-CoA, which is a key step in the breakdown of fatty acids through beta-oxidation.

The enzyme works by bringing together two acetyl-CoA molecules and removing a coenzyme A (CoA) group from one of them, forming a carbon-carbon bond between the two molecules to create acetoacetyl-CoA. This reaction is reversible, meaning that the enzyme can also catalyze the breakdown of acetoacetyl-CoA into two molecules of acetyl-CoA.

There are several different isoforms of Acetyl-CoA C-acetyltransferase found in various tissues throughout the body, with differing roles and regulation. For example, one isoform is highly expressed in the liver and plays a key role in ketone body metabolism, while another isoform is found in mitochondria and is involved in fatty acid synthesis.

Carbon isotopes are variants of the chemical element carbon that have different numbers of neutrons in their atomic nuclei. The most common and stable isotope of carbon is carbon-12 (^{12}C), which contains six protons and six neutrons. However, carbon can also come in other forms, known as isotopes, which contain different numbers of neutrons.

Carbon-13 (^{13}C) is a stable isotope of carbon that contains seven neutrons in its nucleus. It makes up about 1.1% of all carbon found on Earth and is used in various scientific applications, such as in tracing the metabolic pathways of organisms or in studying the age of fossilized materials.

Carbon-14 (^{14}C), also known as radiocarbon, is a radioactive isotope of carbon that contains eight neutrons in its nucleus. It is produced naturally in the atmosphere through the interaction of cosmic rays with nitrogen gas. Carbon-14 has a half-life of about 5,730 years, which makes it useful for dating organic materials, such as archaeological artifacts or fossils, up to around 60,000 years old.

Carbon isotopes are important in many scientific fields, including geology, biology, and medicine, and are used in a variety of applications, from studying the Earth's climate history to diagnosing medical conditions.

Pyruvate carboxylase deficiency disease is a rare inherited metabolic disorder that affects the body's ability to break down proteins, fats, and carbohydrates for energy. It is caused by mutations in the Pyruvate Carboxylase (PC) gene, which provides instructions for making an enzyme called pyruvate carboxylase. This enzyme plays a critical role in gluconeogenesis, a process that takes place in the liver and kidneys to produce glucose, a simple sugar that is a primary source of energy for the body.

In pyruvate carboxylase deficiency disease, the enzyme's activity is significantly reduced or absent, leading to an accumulation of toxic levels of certain metabolic intermediates, such as lactic acid and pyruvic acid, in the blood and other tissues. This accumulation can cause a range of symptoms, including developmental delay, seizures, poor muscle tone, difficulty breathing, and feeding problems.

The severity of pyruvate carboxylase deficiency disease varies widely, depending on the degree of enzyme activity that is affected. Some individuals may have mild symptoms, while others may experience severe, life-threatening complications. Treatment typically involves managing symptoms and providing supportive care to help prevent complications. In some cases, a low-protein diet or supplementation with certain vitamins and minerals may be recommended to help reduce the accumulation of toxic metabolites.

Acyl Coenzyme A (often abbreviated as Acetyl-CoA or Acyl-CoA) is a crucial molecule in metabolism, particularly in the breakdown and oxidation of fats and carbohydrates to produce energy. It is a thioester compound that consists of a fatty acid or an acetate group linked to coenzyme A through a sulfur atom.

Acyl CoA plays a central role in several metabolic pathways, including:

1. The citric acid cycle (Krebs cycle): In the mitochondria, Acyl-CoA is formed from the oxidation of fatty acids or the breakdown of certain amino acids. This Acyl-CoA then enters the citric acid cycle to produce high-energy electrons, which are used in the electron transport chain to generate ATP (adenosine triphosphate), the main energy currency of the cell.
2. Beta-oxidation: The breakdown of fatty acids occurs in the mitochondria through a process called beta-oxidation, where Acyl-CoA is sequentially broken down into smaller units, releasing acetyl-CoA, which then enters the citric acid cycle.
3. Ketogenesis: In times of low carbohydrate availability or during prolonged fasting, the liver can produce ketone bodies from acetyl-CoA to supply energy to other organs, such as the brain and heart.
4. Protein synthesis: Acyl-CoA is also involved in the modification of proteins by attaching fatty acid chains to them (a process called acetylation), which can influence protein function and stability.

In summary, Acyl Coenzyme A is a vital molecule in metabolism that connects various pathways related to energy production, fatty acid breakdown, and protein modification.

Ribulose phosphates are organic compounds that play a crucial role in the Calvin cycle, which is a part of photosynthesis. The Calvin cycle is the process by which plants, algae, and some bacteria convert carbon dioxide into glucose and other simple sugars.

Ribulose phosphates are sugar phosphates that contain five carbon atoms and have the chemical formula C5H10O5P. They exist in two forms: ribulose 5-phosphate (Ru5P) and ribulose 1,5-bisphosphate (RuBP).

Ribulose 1,5-bisphosphate is the starting point for carbon fixation in the Calvin cycle. In this process, an enzyme called RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyzes the reaction between RuBP and carbon dioxide to form two molecules of 3-phosphoglycerate, which are then converted into glucose and other sugars.

Ribulose phosphates are also involved in other metabolic pathways, such as the pentose phosphate pathway, which generates reducing power in the form of NADPH and produces ribose-5-phosphate, a precursor for nucleotide synthesis.

The Citric Acid Cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, is a crucial metabolic pathway in the cell's powerhouse, the mitochondria. It plays a central role in the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins, into carbon dioxide and high-energy electrons. This process generates energy in the form of ATP (adenosine triphosphate), reducing equivalents (NADH and FADH2), and water.

The cycle begins with the condensation of acetyl-CoA with oxaloacetate, forming citrate. Through a series of enzyme-catalyzed reactions, citrate is converted back to oxaloacetate, releasing two molecules of carbon dioxide, one GTP (guanosine triphosphate), three NADH, one FADH2, and regenerating oxaloacetate to continue the cycle. The reduced coenzymes (NADH and FADH2) then donate their electrons to the electron transport chain, driving ATP synthesis through chemiosmosis. Overall, the Citric Acid Cycle is a vital part of cellular respiration, connecting various catabolic pathways and generating energy for the cell's metabolic needs.

Caprylates are the salts or esters of capric acid, a saturated fatty acid with a chain length of 8 carbon atoms. In medical and biological contexts, caprylate refers to the anion (negatively charged ion) form of capric acid, which has the chemical formula C8H17O2-. Caprylates are used in various applications, including as food additives, pharmaceuticals, and personal care products.

Some examples of caprylate compounds include:

* Sodium caprylate (sodium octanoate): a sodium salt commonly used as a preservative and flavor enhancer in foods.
* Calcium caprylate (calcium octanoate): a calcium salt used as an emulsifier in food products and as a stabilizer in cosmetics.
* Caprylic acid/caprylate triglycerides: esters of glycerin with caprylic acid, used as emollients and solvents in skin care products and pharmaceuticals.

Caprylates have antimicrobial properties against certain bacteria, fungi, and viruses, making them useful in various medical applications. For instance, sodium caprylate is sometimes used as an antifungal agent to treat conditions like candidiasis (yeast infections). However, more research is needed to fully understand the potential benefits and risks of using caprylates for medicinal purposes.

Mevalonic acid is not a term that is typically used in medical definitions, but rather it is a biochemical concept. Mevalonic acid is a key intermediate in the biosynthetic pathway for cholesterol and other isoprenoids. It is formed from 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) by the enzyme HMG-CoA reductase, which is the target of cholesterol-lowering drugs known as statins.

In a medical context, mevalonic acid may be mentioned in relation to certain rare genetic disorders, such as mevalonate kinase deficiency (MKD) or hyperimmunoglobulinemia D and periodic fever syndrome (HIDS), which are caused by mutations in the gene encoding mevalonate kinase, an enzyme involved in the metabolism of mevalonic acid. These conditions can cause recurrent fevers, rashes, joint pain, and other symptoms.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

Acetylation is a chemical process that involves the addition of an acetyl group (-COCH3) to a molecule. In the context of medical biochemistry, acetylation often refers to the post-translational modification of proteins, where an acetyl group is added to the amino group of a lysine residue in a protein by an enzyme called acetyltransferase. This modification can alter the function or stability of the protein and plays a crucial role in regulating various cellular processes such as gene expression, DNA repair, and cell signaling. Acetylation can also occur on other types of molecules, including lipids and carbohydrates, and has important implications for drug metabolism and toxicity.

Acetylesterase is an enzyme that catalyzes the hydrolysis of acetyl esters into alcohol and acetic acid. This enzyme plays a role in the metabolism of various xenobiotics, including drugs and environmental toxins, by removing acetyl groups from these compounds. Acetylesterase is found in many tissues, including the liver, intestine, and blood. It belongs to the class of enzymes known as hydrolases, which act on ester bonds.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Fatty acid synthase type II (FASN2) is an alternative form of fatty acid synthase, which is a multi-functional enzyme complex responsible for the de novo synthesis of palmitate, a 16-carbon saturated fatty acid. In contrast to the classical type I fatty acid synthase (FASN), which is found in the cytoplasm and exists as a homodimer, FASN2 is localized in the mitochondria and consists of individual, monofunctional enzymes that catalyze each step of the fatty acid synthesis process.

The type II fatty acid synthase system includes several enzymes: acetyl-CoA carboxylase (ACC), which provides malonyl-CoA; 3-ketoacyl-CoA thiolase, which catalyzes the initial condensation of acetyl-CoA and malonyl-CoA to form acetoacetyl-CoA; 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase (HAD), which catalyzes the reduction, dehydration, and isomerization of acetoacetyl-CoA to form hydroxybutyryl-CoA; 3-ketoacyl-CoA reductase, which reduces hydroxybutyryl-CoA to butyryl-CoA; and enoyl-CoA reductase (ECR), which catalyzes the final reduction of butyryl-CoA to palmitate.

FASN2 is involved in various cellular processes, including energy metabolism, lipid biosynthesis, and protein acetylation. Dysregulation of FASN2 has been implicated in several diseases, such as cancer, obesity, and neurodegenerative disorders.

Vitamin K is a fat-soluble vitamin that plays a crucial role in blood clotting and bone metabolism. It is essential for the production of several proteins involved in blood clotting, including factor II (prothrombin), factor VII, factor IX, and factor X. Additionally, Vitamin K is necessary for the synthesis of osteocalcin, a protein that contributes to bone health by regulating the deposition of calcium in bones.

There are two main forms of Vitamin K: Vitamin K1 (phylloquinone), which is found primarily in green leafy vegetables and some vegetable oils, and Vitamin K2 (menaquinones), which is produced by bacteria in the intestines and is also found in some fermented foods.

Vitamin K deficiency can lead to bleeding disorders such as hemorrhage and excessive bruising. While Vitamin K deficiency is rare in adults, it can occur in newborns who have not yet developed sufficient levels of the vitamin. Therefore, newborns are often given a Vitamin K injection shortly after birth to prevent bleeding problems.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Pentose phosphates are monosaccharides that contain five carbon atoms and one phosphate group. They play a crucial role in various metabolic pathways, including the pentose phosphate pathway (PPP), which is a major source of NADPH and ribose-5-phosphate for the synthesis of nucleotides.

The pentose phosphate pathway involves two main phases: the oxidative phase and the non-oxidative phase. In the oxidative phase, glucose-6-phosphate is converted to ribulose-5-phosphate, producing NADPH and CO2 as byproducts. Ribulose-5-phosphate can then be further metabolized in the non-oxidative phase to produce other pentose phosphates or converted back to glucose-6-phosphate through a series of reactions.

Pentose phosphates are also important intermediates in the synthesis of nucleotides, coenzymes, and other metabolites. Abnormalities in pentose phosphate pathway enzymes can lead to various metabolic disorders, such as defects in erythrocyte function and increased susceptibility to oxidative stress.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Carbon dioxide (CO2) is a colorless, odorless gas that is naturally present in the Earth's atmosphere. It is a normal byproduct of cellular respiration in humans, animals, and plants, and is also produced through the combustion of fossil fuels such as coal, oil, and natural gas.

In medical terms, carbon dioxide is often used as a respiratory stimulant and to maintain the pH balance of blood. It is also used during certain medical procedures, such as laparoscopic surgery, to insufflate (inflate) the abdominal cavity and create a working space for the surgeon.

Elevated levels of carbon dioxide in the body can lead to respiratory acidosis, a condition characterized by an increased concentration of carbon dioxide in the blood and a decrease in pH. This can occur in conditions such as chronic obstructive pulmonary disease (COPD), asthma, or other lung diseases that impair breathing and gas exchange. Symptoms of respiratory acidosis may include shortness of breath, confusion, headache, and in severe cases, coma or death.

Multiple carboxylase deficiency (MCD) is a rare genetic disorder that affects the body's ability to metabolize certain amino acids, particularly those that contain sulfur. It is caused by mutations in the genes responsible for producing enzymes involved in the biotin-dependent carboxylation reactions, which are critical for various metabolic processes in the body.

There are two major types of MCD:

1. Profound multiple carboxylase deficiency (also known as Type II biotinidase deficiency): This form is more severe and is caused by a defect in the holocarboxylase synthetase enzyme, which is responsible for attaching biotin to several carboxylases.
2. Biotin-responsive multiple carboxylase deficiency (also known as Type I biotinidase deficiency): This form is milder and is caused by a defect in the biotinidase enzyme, which recycles biotin in the body. However, it can be treated with biotin supplementation.

Symptoms of MCD may include:

* Developmental delay
* Seizures
* Hypotonia (low muscle tone)
* Ataxia (lack of coordination)
* Rash
* Hair loss
* Acidosis (high levels of acid in the body)
* Coma and even death, if left untreated

Early diagnosis and treatment with biotin supplementation can significantly improve outcomes for individuals with MCD.

Organophosphates are a group of chemicals that include insecticides, herbicides, and nerve gases. They work by inhibiting an enzyme called acetylcholinesterase, which normally breaks down the neurotransmitter acetylcholine in the synapse between nerves. This leads to an overaccumulation of acetylcholine, causing overstimulation of the nervous system and resulting in a wide range of symptoms such as muscle twitching, nausea, vomiting, diarrhea, sweating, confusion, and potentially death due to respiratory failure. Organophosphates are highly toxic and their use is regulated due to the risks they pose to human health and the environment.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

Pyruvate is a negatively charged ion or group of atoms, called anion, with the chemical formula C3H3O3-. It is formed from the decomposition of glucose and other sugars in the process of cellular respiration. Pyruvate plays a crucial role in the metabolic pathways that generate energy for cells.

In the cytoplasm, pyruvate is produced through glycolysis, where one molecule of glucose is broken down into two molecules of pyruvate, releasing energy and producing ATP (adenosine triphosphate) and NADH (reduced nicotinamide adenine dinucleotide).

In the mitochondria, pyruvate can be further metabolized through the citric acid cycle (also known as the Krebs cycle) to produce more ATP. The process involves the conversion of pyruvate into acetyl-CoA, which then enters the citric acid cycle and undergoes a series of reactions that generate energy in the form of ATP, NADH, and FADH2 (reduced flavin adenine dinucleotide).

Overall, pyruvate is an important intermediate in cellular respiration and plays a central role in the production of energy for cells.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

"Rhodospirillum rubrum" is a gram-negative, facultatively anaerobic, photosynthetic bacteria species. It is commonly found in freshwater and soil environments, and it has the ability to carry out both photosynthesis and respiration, depending on the availability of light and oxygen. The bacteria contain bacteriochlorophyll and carotenoid pigments, which give them a pinkish-red color, hence the name "rubrum." They are known to be important organisms in the study of photosynthesis, nitrogen fixation, and other metabolic processes.

I'm sorry for any confusion, but "Malates" is not a recognized term in medical terminology. It's possible there may be a spelling mistake or it could be a slang term or an abbreviation that is not widely recognized. If you have more context or information, I'd be happy to try and help further.

Carbon radioisotopes are radioactive isotopes of carbon, which is an naturally occurring chemical element with the atomic number 6. The most common and stable isotope of carbon is carbon-12 (^12C), but there are also several radioactive isotopes, including carbon-11 (^11C), carbon-14 (^14C), and carbon-13 (^13C). These radioisotopes have different numbers of neutrons in their nuclei, which makes them unstable and causes them to emit radiation.

Carbon-11 has a half-life of about 20 minutes and is used in medical imaging techniques such as positron emission tomography (PET) scans. It is produced by bombarding nitrogen-14 with protons in a cyclotron.

Carbon-14, also known as radiocarbon, has a half-life of about 5730 years and is used in archaeology and geology to date organic materials. It is produced naturally in the atmosphere by cosmic rays.

Carbon-13 is stable and has a natural abundance of about 1.1% in carbon. It is not radioactive, but it can be used as a tracer in medical research and in the study of metabolic processes.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Lipids are a broad group of organic compounds that are insoluble in water but soluble in nonpolar organic solvents. They include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E, and K), monoglycerides, diglycerides, triglycerides, and phospholipids. Lipids serve many important functions in the body, including energy storage, acting as structural components of cell membranes, and serving as signaling molecules. High levels of certain lipids, particularly cholesterol and triglycerides, in the blood are associated with an increased risk of cardiovascular disease.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Avidin is a protein found in the white of eggs (egg whites) and some other animal tissues. It has a high binding affinity for biotin, also known as vitamin B7 or vitamin H, which is an essential nutrient for humans and other organisms. This property makes avidin useful in various biochemical and medical applications, such as immunohistochemistry, blotting techniques, and drug delivery systems.

Biotin-avidin interactions are among the strongest non-covalent interactions known in nature, with a dissociation constant (Kd) of approximately 10^-15 M. This means that once biotin is bound to avidin, it is very difficult to separate them. In some cases, this property can be exploited to create stable and specific complexes for various applications.

However, it's worth noting that the high affinity of avidin for biotin can also have negative effects in certain contexts. For example, raw egg whites contain large amounts of avidin, which can bind to biotin in the gut and prevent its absorption if consumed in sufficient quantities. This can lead to biotin deficiency, which can cause various health problems. Cooking egg whites denatures avidin and reduces its ability to bind to biotin, making cooked eggs a safe source of biotin.

Dietary carbohydrates refer to the organic compounds in food that are primarily composed of carbon, hydrogen, and oxygen atoms, with a general formula of Cm(H2O)n. They are one of the three main macronutrients, along with proteins and fats, that provide energy to the body.

Carbohydrates can be classified into two main categories: simple carbohydrates (also known as simple sugars) and complex carbohydrates (also known as polysaccharides).

Simple carbohydrates are made up of one or two sugar molecules, such as glucose, fructose, and lactose. They are quickly absorbed by the body and provide a rapid source of energy. Simple carbohydrates are found in foods such as fruits, vegetables, dairy products, and sweeteners like table sugar, honey, and maple syrup.

Complex carbohydrates, on the other hand, are made up of long chains of sugar molecules that take longer to break down and absorb. They provide a more sustained source of energy and are found in foods such as whole grains, legumes, starchy vegetables, and nuts.

It is recommended that adults consume between 45-65% of their daily caloric intake from carbohydrates, with a focus on complex carbohydrates and limiting added sugars.

Coenzyme A (CoA) ligases, also known as CoA synthetases, are a class of enzymes that activate acyl groups, such as fatty acids and amino acids, by forming a thioester bond with coenzyme A. This activation is an essential step in various metabolic pathways, including fatty acid oxidation, amino acid catabolism, and the synthesis of several important compounds like steroids and acetylcholine.

CoA ligases catalyze the following reaction:

acyl group + ATP + CoA ↔ acyl-CoA + AMP + PP~i~

In this reaction, an acyl group (R-) from a carboxylic acid is linked to the thiol (-SH) group of coenzyme A through a high-energy thioester bond. The energy required for this activation is provided by the hydrolysis of ATP to AMP and inorganic pyrophosphate (PP~i~).

CoA ligases are classified into three main types based on the nature of the acyl group they activate:

1. Acyl-CoA synthetases (or long-chain fatty acid CoA ligases) activate long-chain fatty acids, typically containing 12 or more carbon atoms.
2. Aminoacyl-CoA synthetases activate amino acids to form aminoacyl-CoAs, which are essential intermediates in the catabolism of certain amino acids.
3. Short-chain specific CoA ligases activate short-chain fatty acids (up to 6 carbon atoms) and other acyl groups like acetate or propionate.

These enzymes play a crucial role in maintaining cellular energy homeostasis, metabolism, and the synthesis of various essential biomolecules.

Crystallographic structures of E. coli acetyl-CoA carboxylase Biotin carboxylase subunit of E. coli acetyl-CoA carboxylase ... coli acetyl-CoA carboxylase Carboxyl transferase subunit of E. coli acetyl-CoA carboxylase The polypeptides composing the multi ... Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme (EC 6.4.1.2) that catalyzes the irreversible carboxylation of acetyl- ... "A conserved mammalian mitochondrial isoform of acetyl-CoA carboxylase ACC1 provides the malonyl-CoA essential for mitochondrial ...
... 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, ...
The enzyme [acetyl-CoA carboxylase]-phosphatase (EC 3.1.3.44) catalyzes the reaction [acetyl-CoA carboxylase] phosphate + H2O ... Krakower GR, Kim KH (March 1981). "Purification and properties of acetyl-CoA carboxylase phosphatase". The Journal of ... acetyl-CoA carboxylase] + phosphate This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric ... The systematic name is [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase. ...
... 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). ...
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 ...
Wang Y, Yu W, Li S, Guo D, He J, Wang Y (March 11, 2022). "Acetyl-CoA Carboxylases and Diseases". Frontiers in Oncology. doi: ... high-energy ATP molecules are produced by the oxidation of acetyl CoA (the Krebs cycle substrate), leading to a rise in the ATP ... Increased glycolysis increases the formation of malonyl-CoA, a molecule that can be shunted into lipogenesis and that ... dephosphorylations affect the enzymes controlling the rate of glycolysis leading to the synthesis of fats via malonyl-CoA in ...
... also inactivates acetyl-CoA carboxylase, which creates malonyl-CoA from acetyl-CoA, through cAMP-dependent and/or cAMP ... Glucagon decreases malonyl-CoA through inhibition of acetyl-CoA carboxylase and through reduced glycolysis through its ... Wang Y, Yu W, Li S, Guo D, He J, Wang Y (March 11, 2022). "Acetyl-CoA Carboxylases and Diseases". Frontiers in Oncology. doi: ... Swenson TL, Porter JW (Mar 25, 1985). "Mechanism of glucagon inhibition of liver acetyl-CoA carboxylase. Interrelationship of ...
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. ...
To some degree, it reverses the action of Acetyl-CoA carboxylase. MCD presents two isoforms which can be transcribed form one ... To avoid it malonyl-CoA decarboxylase (MCD) converts malonyl-CoA into acetyl-CoA through the following reaction: In the cytosol ... The enzyme malonyl-CoA decarboxylase (MCD) functions as an indirect via of conversion from malonic semi aldehyde to acetyl-CoA ... Malonyl-CoA acts as an intermediary between fatty acids and acetyl-CoA in the mitochondria, where MCD is believed to ...
His laboratory also discovered both Acetyl CoA Carboxylase and Fatty Acid Synthetase, the two key enzymes of fatty acid ... Wakil's laboratory discovered both Acetyl CoA Carboxylase and Fatty Acid Synthetase. Wakil was born on August 16, 1927, in ...
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.; ...
Biotin carboxylases are a conserved enzyme present within biotin-dependent carboxylase complexes such as acetyl-CoA carboxylase ... The crystal structure has been determined for the biotin carboxylase (acetyl-CoA carboxylase) of Escherichia coli, but the ... 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. ...
For example, protein kinase A phosphorylates acetyl-CoA carboxylase and pyruvate dehydrogenase. Such covalent modification has ...
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 ...
... is an acetyl-CoA carboxylase inhibitor that functions in the liver. Its original designation was GS-0976. It was ... "Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia ... an investigational liver-directed acetyl-CoA carboxylase (ACC) inhibitor for the treatment of non-alcoholic steatohepatitis ( ...
... such as acetyl-CoA carboxylase EC 6.5 includes ligases used to form phosphoric ester bonds, such as DNA ligase EC 6.6 includes ... Chemistry portal DNA ligase Acetyl-CoA carboxylase Nuclease Protease "IntEnz - EC 6". www.ebi.ac.uk. Retrieved May 2, 2023. " ... There are also some ligases that use the name "carboxylase" to indicate that the enzyme specifically catalyzes a carboxylation ...
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. ...
Citrate also activates acetyl-CoA carboxylase, an enzyme that is essential in the fatty acid synthesis pathway. Citrate-malate ... "Acetyl-CoA - The Definitive Guide". Biology Dictionary. 2020-07-09. Retrieved 2022-03-28. "Acetyl-CoA - Bioblast". www.bioblast ... In the beginning, the acetyl group of Acetyl-CoA combines with oxaloacetate to form citrate, releasing the coenzyme group (CoA ... The acetyl group would join the coenzyme in the cytosol, forming acetyl-CoA. The overall process involves six major steps. A ...
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 ...
"Gilead Sciences Announces Acquisition of Nimbus Therapeutics' Acetyl-CoA Carboxylase (ACC) Program for NASH and Other Liver ...
Crystallographic structures of E. coli acetyl-CoA carboxylase Biotin carboxylase subunit of E. coli acetyl-CoA carboxylase ... coli acetyl-CoA carboxylase Carboxyl transferase subunit of E. coli acetyl-CoA carboxylase The polypeptides composing the multi ... Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme (EC 6.4.1.2) that catalyzes the irreversible carboxylation of acetyl- ... "A conserved mammalian mitochondrial isoform of acetyl-CoA carboxylase ACC1 provides the malonyl-CoA essential for mitochondrial ...
ACC2 inhibitor 2e is a highly potent and selective acetyl-CoA carboxylase 2 (ACC2) inhibitor with IC50 of 1.9 nM and 1950 nM ... ND-630 is an acetyl-CoA carboxylase (ACC) inhibitor; inhibits human ACC1 and ACC2 with IC50 values of 2.1 and 6.1 nM, ... A-908292 is a highly potent and selective acetyl-CoA carboxylase 2 (ACC2) inhibitor with IC50 of 38 nM (hACC2), no activity ... PF-05175157 is a potent and selective inhibitor of both acetyl-CoA carboxylase isoform ACC1 located primarily in liver and ...
You need info about Bovine Acetyl-CoA Carboxylase Synthetase (ACC) ELISA Kit or any other Gentaur produtct? Contact us on Live ...
Acetyl-CoA-carboxylase 1 (ACC1) plays a critical role in glucagon secretion *Anna Veprik ... Acetyl-CoA-carboxylase 1 (ACC1) plays a critical role in glucagon secretion *Anna Veprik ...
STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING ... ACETYL-COA CARBOXYLASE. A. 80. Escherichia coli. Mutation(s): 0 Gene Names: BIOTIN CARBOXYL CARRIER PROTEI. EC: 6.4.1.2. ... Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.. Athappilly, F.K., Hendrickson, W. ... Acetyl-coenzyme A carboxylase catalyzes the first committed step of fatty acid biosynthesis. Universally, this reaction ...
Gibberellic acid (GA) role in acetyl-coA carboxylase enzyme regulation and in improving oil palm yield Authors. * Irma ... 2001). Activation of Acetyl-CoA Carboxylase by a Glutamate and Magnesium-Sensitive Protein Phosphatase in the Islet b-Cell. ... Those composition could be used as an booster of palm oil production which related to acetyl co-A carboxylase activity (ACC). ... Gaussin, V., Hue, L., Stalmans, W. & Bollen, M. (1996). Activation of hepatic acetyl-CoA carboxylase by glutamate and Mg2+ is ...
acetyl-CoA carboxylase subunit A; Validated. Links. ?. Source:. PRK. Taxonomy:. Campylobacterales. Protein:. Representatives. ...
ACC = acetyl-CoA carboxylase; AMP/ATP = adenosine monophosphate/adenosine triphosphate; AMPK = AMP-activated protein kinase; ... ACC = acetyl-CoA carboxylase; AMP/ATP = adenosine monophosphate/adenosine triphosphate; AMPK = AMP-activated protein kinase; ...
... acetyl-CoA carboxylase alpha (ACC-alpha), has been shown to be highly expressed in human breast cancer and other tumor types ... A key fatty acid synthesis enzyme, acetyl-CoA carboxylase alpha (ACC-alpha), has been shown to be highly expressed in human ... Acetyl-CoA Carboxylase, Adult, Aged, Alleles, Breast Neoplasms, Case-Control Studies, Chi-Square Distribution, Europe, Female, ... Haplotype-based analysis of common variation in the acetyl-coA carboxylase alpha gene and breast cancer risk: a case-control ...
acetyl-CoA carboxylase. GLP-1:. glucagon-like peptide-1. GIP:. gastric inhibitory polypeptide ...
... acetyl-CoA carboxylase beta subunit; pink, threonyl-tRNA synthetase; violet, lysS, lysyl-tRNA synthetase; light green, leuS, ...
tion during glucotoxicity via regulation of acetyl-CoA carboxylase. Am J Physiol Endocrinol ... Furthermore, the expression of the liver phosphoenolpyruvate carboxylase (PEPCK) in the DM+H group reduced significantly (P, ...
The mentioned factors, in turn, cause the inhibition of acetyl-CoA carboxylase (ACC). These processes decrease lipid ... acetyl-CoA) is the precursor of cholesterol. Synthesis of acetyl-CoA is regulated by SREBP1a, SREBP2, 3-hydroxy-3- ... FAS, HMG-CoA reductase. ↓Lipid peroxide levels 10 weeks. [118]. Animal study. Male wild-type C57BL/6 J mice (8-10 weeks old) in ... Downregulated or inactivated molecules included SCD (Stearoyl-CoA desaturase), HSL (hormone-sensitive lipase), PPARγ, SREBP-1c ...
Optimizing the Benefit/Risk of Acetyl-CoA Carboxylase Inhibitors through Liver Targeting. Huard K, Smith AC, Cappon G, Dow RL, ...
HRAC Group: 1 : Inhibition of Acetyl CoA Carboxylase Inhibition of Acetyl CoA Carboxylase ... Aryloxyphenoxypropionate (FOPs) and cyclohexanedione (DIMs) herbicides inhibit the enzyme acetylCoA carboxylase (ACCase), the ... A currently viable hypothesis that may link all these effects involves the conjugation of acetyl coenzyme A and other ...
... acetyl-CoA carboxylase; DMEM, Dulbeccos modified Eagles medium; PI-3, phosphatidylinositol-3; PBS, phosphate-buffered saline ...
HRAC 1 (Inhibition of Acetyl CoA Carboxylase ). *HRAC 2 (Inhibition of Acetolactate Synthase ) ...
Inhibition of Acetyl CoA Carboxylase (A/1). 15059. 3 Avena fatua. Wild Oat. Syria. 2015. 69. Inhibition of Acetyl CoA ... Inhibition of Acetyl CoA Carboxylase (A/1). 15058. 2 Phalaris paradoxa. Hood Canarygrass. Syria. 2015. 69. ...
Inhibition of Acetyl CoA Carboxylase Inhibition of Acetyl CoA Carboxylase 1. Small Structure Medium Structure Large Structure ... Inhibition of Acetyl CoA Carboxylase Inhibition of Acetyl CoA Carboxylase 1. Small Structure Medium Structure Large Structure ... Inhibition of Acetyl CoA Carboxylase Inhibition of Acetyl CoA Carboxylase 1. Small Structure Medium Structure Large Structure ... Inhibition of Acetyl CoA Carboxylase Inhibition of Acetyl CoA Carboxylase 1. Small Structure Medium Structure Large Structure ...
The metformin activates intracellular AMPK, which reduces the activity of acetyl CoA carboxylase enzyme (ACC). The low activity ...
Timeline for Species Bakers yeast (Saccharomyces cerevisiae) [TaxId:4932] from b.84.2.1 Acetyl-CoA carboxylase, BC-C subdomain ... Protein Acetyl-CoA carboxylase, BC-C subdomain [117328] (1 species). *. Species Bakers yeast (Saccharomyces cerevisiae) [TaxId ... More info for Species Bakers yeast (Saccharomyces cerevisiae) [TaxId:4932] from b.84.2.1 Acetyl-CoA carboxylase, BC-C ... Species Bakers yeast (Saccharomyces cerevisiae) [TaxId:4932] from b.84.2.1 Acetyl-CoA carboxylase, BC-C subdomain appears in ...
... based on a single-copy nuclear gene encoding plastid acetyl-CoA carboxylase. BMC Evol. Biol. 9: 247-252.10.1186/1471-2148-9-247 ...
We need better replacements than the resistance-prone inhibitors of acetolactate-synthase and acetyl-CoA-carboxylase. Much of ...
Acetyl-CoA-Carboxylase 1-mediated de novo fatty acid synthesis sustains Lgr5+ intestinal stem cell function. Li S, Lu CW, Diem ...
Inhibition of Acetyl CoA Carboxylase (A/1). PS I Electron Diversion (D/22). 112. Lolium rigidum. Rigid Ryegrass. 5489. ... Inhibition of Acetyl CoA Carboxylase (A/1). PSII inhibitors - Serine 264 Binders (C1 C2/5). 112. Lolium rigidum. Rigid Ryegrass ... Inhibition of Acetyl CoA Carboxylase (A/1). Inhibition of Acetolactate Synthase (B/2). 112. Lolium rigidum. Rigid Ryegrass. ... Inhibition of Acetyl CoA Carboxylase (A/1). Inhibition of Acetolactate Synthase (B/2). 112. Lolium rigidum. Rigid Ryegrass. ...
HRAC 1 (Inhibition of Acetyl CoA Carboxylase ). *HRAC 2 (Inhibition of Acetolactate Synthase ) ...
ACC, acetyl-CoA carboxylase; CPT-1, carnitine palmitoyltransferase-1; FACoA, FFA-derived long chain acyl-CoA esters; FAS, fatty ... AcCoAc, cytosolic acetyl-CoA; AcCoAm, mitochondrial acetyl-CoA; DAG, diacylglycerol, LPA, lysophosphatidic acid; βox, β ... AcCoAc, cytosolic acetyl-CoA; AcCoAm, mitochondrial acetyl-CoA; DAG, diacylglycerol, LPA, lysophosphatidic acid; βox, β ... Brun T, Roche E, Kim KH, Prentki M: Glucose regulates acetyl-CoA carboxylase gene expression in a pancreatic beta-cell line ( ...
Protein Acetyl-CoA carboxylase, BC-M subdomain [118120] (1 species). *. Species Bakers yeast (Saccharomyces cerevisiae) [TaxId ... d1w96c3 d.142.1.2 (C:184-450) Acetyl-CoA carboxylase, BC-M subdomain {Bakers yeast (Saccharomyces cerevisiae) [TaxId: 4932]} ... PDB Description: crystal structure of biotin carboxylase domain of acetyl-coenzyme a carboxylase from saccharomyces cerevisiae ... PDB Compounds: (C:) acetyl-coenzyme a carboxylase. SCOPe Domain Sequences for d1w96c3:. Sequence; same for both SEQRES and ATOM ...
... including acetyl-CoA carboxylase and methylcrotonyl-CoA carboxylase. Biotin stimulates the activity of glucokinase in the liver ... Biotin augments acetyl CoA carboxylase 2 gene expression in the hypothalamus, leading to the suppression of food intake in mice ... It has been demonstrated that a combination of lipoic acid, acetyl-l-carnitine, nicotinamide and biotin treatment significantly ... Biotin is an essential cofactor for a number of carboxylases that are important in carbohydrate and lipid metabolism, ...
  • TG production is also decreased via the inhibition of acetyl-CoA carboxylase and fatty acid synthase. (medscape.com)
  • Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme (EC 6.4.1.2) 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)
  • 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)
  • 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 sterol regulatory element binding protein 1 (SREBP-1), ATP-citrate lyase (ACL), fatty acid synthase (FAS), malic enzyme (ME), acetyl-CoA carboxylase (ACC), and stearoyl-CoA (?9) desaturase 1 (SCD1) genes in ad lib birds declined from their highest levels just prior to photo-stimulation to reduced levels as the birds came into and maintained egg production. (usda.gov)
  • Paradoxically, even in the face of hypoglycemia, patients with glycogen-storage disease I do not develop significant ketosis because the abundance of acetyl coenzyme A (CoA) derived from glycolysis activates the acetyl CoA carboxylase enzyme that produces malonyl CoA in the first step of fatty acid synthesis. (medscape.com)
  • Pyruvate dehydrogenase is a multi-enzyme complex responsible for the generation of acetyl CoA from pyruvate for the Krebs cycle. (msdmanuals.com)
  • Pyruvate carboxylase is an enzyme important for gluconeogenesis from pyruvate and alanine generated in muscle. (msdmanuals.com)
  • Biotin carboxylase (BC) activity, biotin carboxyl carrier protein (BCCP), and carboxyl transferase (CT) activity are each contained on a different subunit. (wikipedia.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)
  • In Escherichia coli, accA encodes the alpha subunit of the acetyl-CoA carboxylase, and accD encodes its beta subunit. (wikipedia.org)
  • PF-05175157 is a potent and selective inhibitor of both acetyl-CoA carboxylase isoform ACC1 located primarily in liver and adipose tissue and isoform ACC2 dominant in skeletal and heart muscle, with IC50 values of 27 nM and 33 nM, respectively. (dcchemicals.com)
  • Fluazifop-P-butyl, a graminicide from arylophenoxypropionate group, is a acetyl-CoA carboxylase (ACCase) inhibitor. (dcchemicals.com)
  • CP-610431 is a reversible, ATP-uncompetitive, isozyme-nonselective acetyl-CoA carboxylase (ACC) inhibitor. (dcchemicals.com)
  • A-908292 is a highly potent and selective acetyl-CoA carboxylase 2 (ACC2) inhibitor with IC50 of 38 nM (hACC2), no activity against ACC1 (IC50>30 uM). (dcchemicals.com)
  • ACC2 inhibitor 2e is a highly potent and selective acetyl-CoA carboxylase 2 (ACC2) inhibitor with IC50 of 1.9 nM and 1950 nM for ACC2 and ACC1, respectively.ACC2 inhibitor 2e exhibited good PK profile and in vivo antidiabetic efficacy in C57BL/6 mice. (dcchemicals.com)
  • Soraphen A, an inhibitor of acetyl CoA carboxylase activity, interferes with fatty acid elongation. (oregonstate.edu)
  • GS-0976, an acetyl-CoA carboxylase (ACC) inhibitor being developed by Gilead Sciences, led to significant reductions in liver fat accumulation and fibrosis in people with non-alcoholic steatohepatitis (NASH), according to Phase 2 study results presented at the 2017 AASLD Liver Meeting last week in Washington, DC. (hivandhepatitis.com)
  • Synthetically prepared HMG-CoA reductase inhibitor with some similarities to lovastatin, simvastatin, and pravastatin. (medscape.com)
  • 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)
  • A biotinyl domain shuttles its covalently attached biotin prosthetic group between the active sites of a biotin carboxylase and a carboxyl transferase. (rcsb.org)
  • Biotin is an essential cofactor for a number of carboxylases that are important in carbohydrate and lipid metabolism, including acetyl-CoA carboxylase and methylcrotonyl-CoA carboxylase. (cambridge.org)
  • Acetyl-CoA-Carboxylase 1-mediated de novo fatty acid synthesis sustains Lgr5 + intestinal stem cell function. (nih.gov)
  • You need info about Bovine Acetyl-CoA Carboxylase Synthetase (ACC) ELISA Kit or any other Gentaur produtct? (gentaurshop.com)
  • Fenofibrate activates acetyl-CoA and other enzymes, increasing fatty acid oxidation. (medscape.com)
  • 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)
  • Because malonyl CoA inhibits transport of fatty acid into the mitochondrion, beta-oxidation of fatty acids for energy to support the hypoglycemic cells does not occur. (medscape.com)
  • Acetyl-coenzyme A carboxylase catalyzes the first committed step of fatty acid biosynthesis. (rcsb.org)
  • The carboxybiotin translocates to the carboxyl transferase (CT) active site, where the carboxyl group is transferred to acetyl-CoA. (wikipedia.org)
  • In white adipocytes, mRNA expression of various fat storage-promoting enzymes such as lipoprotein lipase, acetyl-CoA carboxylase α, fatty acid synthase, and stearoyl-CoA desaturase-1 was markedly increased, while that of the rate-limiting step in fat oxidation, carnitine palmitoyl transferase-1α, was decreased. (jci.org)
  • Inhibits HMG-CoA reductase, which, in turn, inhibits cholesterol synthesis and increases cholesterol metabolism. (medscape.com)
  • Competitively inhibits HMG-CoA reductase, which catalyzes the rate-limiting step in cholesterol synthesis. (medscape.com)
  • Activation of hepatic acetyl-CoA carboxylase by glutamate and Mg2+ is mediated by protein phosphatase-2A. (iribb.org)
  • 2001). Activation of Acetyl-CoA Carboxylase by a Glutamate and Magnesium-Sensitive Protein Phosphatase in the Islet b-Cell. (iribb.org)
  • Selective competitive inhibition of HMG-CoA reductase decreases cholesterol synthesis and increases cholesterol metabolism. (medscape.com)
  • Those composition could be used as an booster of palm oil production which related to acetyl co-A carboxylase activity (ACC). (iribb.org)
  • 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)
  • A proposed mechanism is the release of CO2 from biotin, which subsequently abstracts a proton from the methyl group from acetyl CoA carboxylase. (wikipedia.org)
  • Increased fatty acid production in potato by engineering of acetyl-CoA carboxylase. (mpg.de)
  • The sensitive to freezing3 mutation of Arabidopsis thaliana is a cold-sensitive allele of homomeric acetyl-CoA carboxylase that results in cold-induced cuticle deficiencies. (mpg.de)
  • Olumacostat glasaretil is a small molecule inhibitor of acetyl coenzyme A carboxylase (ACC). (targetmol.com)
  • Acetyl coenzyme A carboxylase controls the first, rate-limiting step in fatty acid biosynthesis. (targetmol.com)
  • The purpose of this analysis was to (1) investigate correlations between factors influencing AMPK activation and the magnitude of change in AMPK activity during cycling exercise, (2) investigate correlations between commonly reported measures of AMPK activation (AMPK-α2 activity, phosphorylated (p)-AMPK, and p-acetyl coenzyme A carboxylase (p-ACC), and (3) formulate linear regression models to determine the most important factors for AMPK activation during exercise. (springer.com)
  • Two major isoforms of ACC , ACACA (Acetyl-CoA carboxylase A) and ACACB , which is an intermediate substrate that plays a pivotal role in the regulation of fatty acid metabolism and it is the rate-limiting step in fatty acid synthesis. (arccjournals.com)
  • Simultaneous KD of ACSF3, encoding a mitochondrial malonyl-CoA synthetase previously implicated in the mtFAS process, resulted in almost complete ablation of protein lipoylation, indicating that these enzymes have a redundant function in mtFAS. (nih.gov)
  • Long-chain fatty acid were broken down in to smaller acetyl coA by fatty acid oxidation or mitochondrial beta (β)-oxidation pathway. (arccjournals.com)
  • 17. Myc-dependent mitochondrial generation of acetyl-CoA contributes to fatty acid biosynthesis and histone acetylation during cell cycle entry. (nih.gov)
  • The level of nuclear SREBP-1c, a transcription factor involved in fat synthesis, was increased while significantly decreased protein levels of acetyl-CoA carboxylase, phospho-AMP kinase and PPARα as well as inactivation of 3-keto-acyl-CoA thiolase in the mitochondrial β-oxidation pathway were observed in AZT-exposed mice compared to those in control animals. (nih.gov)
  • Soraphen A, an inhibitor of acetyl CoA carboxylase activity, interferes with fatty acid elongation. (oregonstate.edu)
  • 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. (tum.de)
  • We have investigated the effects of estrogen on three key regulatory enzymes in lipid biosynthesis, 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase, the major regulatory enzyme in cholesterol and isoprenoid synthesis, and acetyl-CoA carboxylase and fatty acid synthetase, which regulate fatty acid biosynthesis. (illinois.edu)
  • 15. Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. (nih.gov)
  • Knock-down of the plastid-encoded acetyl-CoA carboxylase gene uncovers functions in metabolism and development. (mpg.de)
  • Acetyl-CoA carboxylase (ACC) catalyzes the first step in fatty acid biosynthesis: the synthesis of malonyl-CoA from acetyl-CoA. (elsevierpure.com)
  • HMG-CoA reductase activity and cholesterol synthesis increase in parallel following estrogen administration. (illinois.edu)
  • The estrogen-induced increase of fatty acid synthesis is paralleled by a 16- to 20-fold increase of acetyl-CoA carboxylase activity, indicating that estrogen regulates fatty acid synthesis at the level of acetyl-CoA carboxylase. (illinois.edu)
  • However, only α-GOSg significantly decreased the histopathological score for liver steatosis and downregulated hepatic fatty acid synthesis gene acetyl CoA carboxylase-α. (nih.gov)
  • A coenzyme for carboxylase enzymes, needed for synthesis of fatty acids and in gluconeogenesis . (wikipedia.org)
  • Paradoxically, even in the face of hypoglycemia, patients with glycogen-storage disease I do not develop significant ketosis because the abundance of acetyl coenzyme A (CoA) derived from glycolysis activates the acetyl CoA carboxylase enzyme that produces malonyl CoA in the first step of fatty acid synthesis. (medscape.com)
  • The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2. (nih.gov)
  • Poaceae) based on a single-copy nuclear gene encoding plastid acetyl-CoA carboxylase. (degruyter.com)
  • A carboxylating enzyme that catalyzes the conversion of ATP , acetyl-CoA, and HCO3- to ADP , orthophosphate, and malonyl-CoA. (nih.gov)
  • Enzima carboxilante que cataliza la conversión de ATP, acetil-CoA y HCO3- a ADP, ortofosfato y malonil CoA. (bvsalud.org)
  • 12558 2-aminobenzoate-CoA ligase abmG BBZA01000002 CDS ARMA_0024 12542. (go.jp)
  • This region is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain. (embl.de)
  • 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)
  • It chiefly involved in the production of malonyl-coA, a potent inhibitor of carnitine palmitoyl transferase I (CPT-I) enzyme needed in transport of long-chain fatty acyl-coAs to the mitochondria for β-oxidation. (arccjournals.com)
  • AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation. (springer.com)
  • The Acetyl-CoA Carboxylase Beta ( ACACB or ACC-β or ACC2 ) plays a key role in β-oxidation pathway. (arccjournals.com)
  • 3. The yeast AMPK homolog SNF1 regulates acetyl coenzyme A homeostasis and histone acetylation. (nih.gov)
  • 8. Acetyl-CoA carboxylase regulates global histone acetylation. (nih.gov)
  • Acetyl-CoA Carboxylase Beta ( ACACB ) plays a key role in fatty acid oxidation and was known to be involved in production of very-long-chain fatty acid and other compounds needed for proper development. (arccjournals.com)
  • 20. Lysine acetyltransferase NuA4 and acetyl-CoA regulate glucose-deprived stress granule formation in Saccharomyces cerevisiae. (nih.gov)
  • Starvation represses the expression of the carboxylase genes and decreases the activities of the ACC enzymes (Kim 1997) . (arccjournals.com)
  • The induction of HMG-CoA reductase and of acetyl-CoA carboxylase by estradiol-17β provides a useful model for regulation of these enzymes by steroid hormones. (illinois.edu)
  • 6. Acetyl-CoA induces cell growth and proliferation by promoting the acetylation of histones at growth genes. (nih.gov)
  • Complex nested promoters control tissue-specific expression of acetyl-CoA carboxylase genes in wheat. (mpg.de)
  • Philipp, BW & Shapiro, DJ 1981, ' Estrogen regulation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and acetyl-CoA carboxylase in Xenopus laevis ', Journal of Biological Chemistry , vol. 256, no. 6, pp. 2922-2927. (illinois.edu)
  • This ELISA kit is a solid phase ELISA designed for quantitative determination of Phosphorylated acetyl -COA catboxylase. (anticorps-enligne.fr)
  • 5. Yeast phospholipase C is required for normal acetyl-CoA homeostasis and global histone acetylation. (nih.gov)
  • A proposed mechanism is the release of CO2 from biotin, which subsequently abstracts a proton from the methyl group from acetyl CoA carboxylase. (wikipedia.org)
  • In a competing mechanism, proton abstraction is concerted with the attack of acetyl CoA. (wikipedia.org)
  • HPLC analyses of hamster ear extracts shows that olumacostat glasaretil treatment increases ACC levels and the ratio of acetyl-CoA to free CoA in tested animals which suggests increased fatty acid oxidation. (targetmol.com)
  • The increased rate of reduction of HMG-CoA to mevalonic acid is not due to activation of pre-existing HMF-CoA reductase by dephosphorylation, as the fold induction is unchanged when reductase from control and estrogen-stimulated animals is fully activated prior to assay. (illinois.edu)