3-Hydroxyacyl CoA Dehydrogenases: Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Acyl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Acyl Coenzyme A: 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.Diacylglycerol O-Acyltransferase: An enzyme that catalyses the last step of the TRIACYLGLYCEROL synthesis reaction in which diacylglycerol is covalently joined to LONG-CHAIN ACYL COA to form triglyceride. It was formerly categorized as EC 2.3.1.124.Sterol O-Acyltransferase: An enzyme that catalyzes the formation of cholesterol esters by the direct transfer of the fatty acid group from a fatty acyl CoA derivative. This enzyme has been found in the adrenal gland, gonads, liver, intestinal mucosa, and aorta of many mammalian species. EC 2.3.1.26.L-Lactate Dehydrogenase: A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.Acyltransferases: Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.Coenzyme AAlcohol Dehydrogenase: A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.Fatty Acids: Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)Glyceraldehyde-3-Phosphate Dehydrogenases: Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Aldehyde Dehydrogenase: An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.Glutamate Dehydrogenase: An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.Glucosephosphate DehydrogenaseMalate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Isocitrate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Acyl-CoA Oxidase: An enzyme that catalyzes the first and rate-determining steps of peroxisomal beta-oxidation of fatty acids. It acts on COENZYME A derivatives of fatty acids with chain lengths from 8 to 18, using FLAVIN-ADENINE DINUCLEOTIDE as a cofactor.Triazenes: Compounds with three contiguous nitrogen atoms in linear format, H2N-N=NH, and hydrocarbyl derivatives.Kinetics: The rate dynamics in chemical or physical systems.Diazepam Binding Inhibitor: An 86-amino acid polypeptide, found in central and peripheral tissues, that displaces diazepam from the benzodiazepine recognition site on the gamma-aminobutyric acid receptor (RECEPTORS, GABA). It also binds medium- and long-chain acyl-CoA esters and serves as an acyl-CoA transporter. This peptide regulates lipid metabolism.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Succinate Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.Amino Acid Sequence: 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.Carbohydrate Dehydrogenases: Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.L-Iditol 2-Dehydrogenase: An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Glycerolphosphate DehydrogenaseLiver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.NAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)Acyl-CoA Dehydrogenase, Long-Chain: A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Oxidation-Reduction: 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).Glucose 1-Dehydrogenase: A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Ketoglutarate Dehydrogenase ComplexFatty Acids, Unsaturated: FATTY ACIDS in which the carbon chain contains one or more double or triple carbon-carbon bonds.Palmitic Acids: A group of 16-carbon fatty acids that contain no double bonds.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Sugar Alcohol Dehydrogenases: Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.Glucose Dehydrogenases: D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.Cholesterol Esters: Fatty acid esters of cholesterol which constitute about two-thirds of the cholesterol in the plasma. The accumulation of cholesterol esters in the arterial intima is a characteristic feature of atherosclerosis.Phosphogluconate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.NADH Dehydrogenase: A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.Oleic Acids: A group of fatty acids that contain 18 carbon atoms and a double bond at the omega 9 carbon.Esterification: The process of converting an acid into an alkyl or aryl derivative. Most frequently the process consists of the reaction of an acid with an alcohol in the presence of a trace of mineral acid as catalyst or the reaction of an acyl chloride with an alcohol. Esterification can also be accomplished by enzymatic processes.Microsomes: Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)IMP Dehydrogenase: An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Formate Dehydrogenases: Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.TriglyceridesMicrobodies: Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.Xanthine Dehydrogenase: An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.Hydroxybutyrate Dehydrogenase3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide): A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.Acylation: The addition of an organic acid radical into a molecule.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.Carnitine O-Palmitoyltransferase: An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.Pyruvate Dehydrogenase (Lipoamide): The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).NADP: Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)Escherichia coli: 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.Cholesterol: The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.RNA, Messenger: 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.11-beta-Hydroxysteroid Dehydrogenases: Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.Acetyl Coenzyme A: Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.Lipids: 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)Adrenoleukodystrophy: An X-linked recessive disorder characterized by the accumulation of saturated very long chain fatty acids in the LYSOSOMES of ADRENAL CORTEX and the white matter of CENTRAL NERVOUS SYSTEM. This disease occurs almost exclusively in the males. Clinical features include the childhood onset of ATAXIA; NEUROBEHAVIORAL MANIFESTATIONS; HYPERPIGMENTATION; ADRENAL INSUFFICIENCY; SEIZURES; MUSCLE SPASTICITY; and DEMENTIA. The slowly progressive adult form is called adrenomyeloneuropathy. The defective gene ABCD1 is located at Xq28, and encodes the adrenoleukodystrophy protein (ATP-BINDING CASSETTE TRANSPORTERS).Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.Butyryl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Glucosephosphate Dehydrogenase Deficiency: A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.11-beta-Hydroxysteroid Dehydrogenase Type 1: A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Alanine Dehydrogenase: An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.3-alpha-Hydroxysteroid Dehydrogenase (B-Specific): A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Mannitol Dehydrogenases: Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Chromatography, Thin Layer: Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Sphingolipids: A class of membrane lipids that have a polar head and two nonpolar tails. They are composed of one molecule of the long-chain amino alcohol sphingosine (4-sphingenine) or one of its derivatives, one molecule of a long-chain acid, a polar head alcohol and sometimes phosphoric acid in diester linkage at the polar head group. (Lehninger et al, Principles of Biochemistry, 2nd ed)Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Retinal Dehydrogenase: A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.Dietary Fats: Fats present in food, especially in animal products such as meat, meat products, butter, ghee. They are present in lower amounts in nuts, seeds, and avocados.Molecular Weight: The sum of the weight of all the atoms in a molecule.Microsomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.20-Hydroxysteroid Dehydrogenases: A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Esters11-beta-Hydroxysteroid Dehydrogenase Type 2: An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.Isovaleryl-CoA Dehydrogenase: A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Recombinant Proteins: Proteins prepared by recombinant DNA technology.Fatty Acid Transport Proteins: A broad category of membrane transport proteins that specifically transport FREE FATTY ACIDS across cellular membranes. They play an important role in LIPID METABOLISM in CELLS that utilize free fatty acids as an energy source.Chromatography, Gas: Fractionation of a vaporized sample as a consequence of partition between a mobile gaseous phase and a stationary phase held in a column. Two types are gas-solid chromatography, where the fixed phase is a solid, and gas-liquid, in which the stationary phase is a nonvolatile liquid supported on an inert solid matrix.Homoserine Dehydrogenase: An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.

Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death. (1/138)

BACKGROUND: Genetic defects are being increasingly recognized in the etiology of primary cardiomyopathy (CM). Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the first step in the beta-oxidation spiral of fatty acid metabolism, the crucial pathway for cardiac energy production. METHODS AND RESULTS: We studied 37 patients with CM, nonketotic hypoglycemia and hepatic dysfunction, skeletal myopathy, or sudden death in infancy with hepatic steatosis, features suggestive of fatty acid oxidation disorders. Single-stranded conformational variance was used to screen genomic DNA. DNA sequencing and mutational analysis revealed 21 different mutations on the VLCAD gene in 18 patients. Of the mutations, 80% were associated with CM. Severe CM in infancy was recognized in most patients (67%) at presentation. Hepatic dysfunction was common (33%). RNA blot analysis and VLCAD enzyme assays showed a severe reduction in VLCAD mRNA in patients with frame-shift or splice-site mutations and absent or severe reduction in enzyme activity in all. CONCLUSIONS: Infantile CM is the most common clinical phenotype of VLCAD deficiency. Mutations in the human VLCAD gene are heterogeneous. Although mortality at presentation is high, both the metabolic disorder and cardiomyopathy are reversible.  (+info)

The medium-/long-chain fatty acyl-CoA dehydrogenase (fadF) gene of Salmonella typhimurium is a phase 1 starvation-stress response (SSR) locus. (2/138)

Salmonella enterica serovar Typhimurium (S. typhimurium) is an enteric pathogen that causes significant morbidity in humans and other mammals. During their life cycle, salmonellae must survive frequent exposures to a variety of environmental stresses, e.g. carbon-source (C) starvation. The starvation-stress response (SSR) of S. typhimurium encompasses the genetic and physiological realignments that occur when an essential nutrient becomes limiting for bacterial growth. The function of the SSR is to produce a cell capable of surviving long-term starvation. This paper reports that three C-starvation-inducible lac fusions from an S. typhimurium C-starvation-inducible lac fusion library are all within a gene identified as fadF, which encodes an acyl-CoA dehydrogenase (ACDH) specific for medium-/long-chain fatty acids. This identification is supported by several findings: (a) significant homology at the amino acid sequence level with the ACDH enzymes from other bacteria and eukaryotes, (b) undetectable beta-oxidation levels in fadF insertion mutants, (c) inability of fad insertion mutants to grow on oleate or decanoate as a sole C-source, and (d) inducibility of fadF::lac fusions by the long-chain fatty acid oleate. In addition, the results indicate that the C-starvation-induction of fadF is under negative control by the FadR global regulator and positive control by the cAMP:cAMP receptor protein complex and ppGpp. It is also shown that the fadF locus is important for C-starvation-survival in S. typhimurium. Furthermore, the results demonstrate that fadF is induced within cultured Madin-Darby canine kidney (MDCK) epithelial cells, suggesting that signals for its induction (C-starvation and/or long-chain fatty acids) may be present in the intracellular environment encountered by S. typhimurium. However, fadF insertion mutations did not have an overt effect on mouse virulence.  (+info)

Cloning and mapping of three pig acyl-CoA dehydrogenase genes. (3/138)

To investigate the structure of porcine genes involved in the beta-oxidation of fatty acid, we isolated the short-chain acyl-CoA dehydrogenase (SCAD), medium-chain acyl-CoA dehydrogenase (MCAD), and long-chain acyl-CoA dehydrogenase (LCAD) genes from the pig. The cDNA of SCAD, MCAD and LCAD genes were 1899 bp, 1835 bp 1835 bp and 1704 bp long and coded for 413-aa, 422-aa and 430-aa precursor proteins, respectively. Three genes, SCAD, MCAD and LCAD were mapped to 14p16.2-23.2, 6q32.4-33, and 15q24.2-26.3, respectively.  (+info)

Arrhythmias and conduction defects as presenting symptoms of fatty acid oxidation disorders in children. (4/138)

BACKGROUND: The clinical manifestations of inherited disorders of fatty acid oxidation vary according to the enzymatic defect. They may present as isolated cardiomyopathy, sudden death, progressive skeletal myopathy, or hepatic failure. Arrhythmia is an unusual presenting symptom of fatty acid oxidation deficiencies. METHODS AND RESULTS: Over a period of 25 years, 107 patients were diagnosed with an inherited fatty acid oxidation disorder. Arrhythmia was the predominant presenting symptom in 24 cases. These 24 cases included 15 ventricular tachycardias, 4 atrial tachycardias, 4 sinus node dysfunctions with episodes of atrial tachycardia, 6 atrioventricular blocks, and 4 left bundle-branch blocks in newborn infants. Conduction disorders and atrial tachycardias were observed in patients with defects of long-chain fatty acid transport across the inner mitochondrial membrane (carnitine palmitoyl transferase type II deficiency and carnitine acylcarnitine translocase deficiency) and in patients with trifunctional protein deficiency. Ventricular tachycardias were observed in patients with any type of fatty acid oxidation deficiency. Arrhythmias were absent in patients with primary carnitine carrier, carnitine palmitoyl transferase I, and medium chain acyl coenzyme A dehydrogenase deficiencies. CONCLUSIONS: The accumulation of arrhythmogenic intermediary metabolites of fatty acids, such as long-chain acylcarnitines, may be responsible for arrhythmias. Inborn errors of fatty acid oxidation should be considered in unexplained sudden death or near-miss in infants and in infants with conduction defects or ventricular tachycardia. Diagnosis can be easily ascertained by an acylcarnitine profile from blood spots on filter paper.  (+info)

Long-chain acyl-CoA dehydrogenase is a key enzyme in the mitochondrial beta-oxidation of unsaturated fatty acids. (5/138)

The first reaction of mitochondrial beta-oxidation, which is catalyzed by acyl-CoA dehydrogenases, was studied with unsaturated fatty acids that have a double bond either at the 4,5 or 5,6 position. The CoA thioesters of docosahexaenoic acid, arachidonic acid, 4,7,10-cis-hexadecatrienoic acid, 5-cis-tetradecenoic acid, and 4-cis-decenoic acid were effectively dehydrogenated by both rat and human long-chain acyl-CoA dehydrogenases (LCAD), whereas they were poor substrates of very long-chain acyl-CoA dehydrogenases (VLCAD). VLCAD, however, was active with CoA derivatives of long-chain saturated fatty acids or unsaturated fatty acids that have double bonds further removed from the thioester function. Although bovine LCAD effectively dehydrogenated 5-cis-tetradecenoyl-CoA (14:1) and 4,7,10-cis-hexadecatrienoyl-CoA, it was nearly inactive toward the other unsaturated substrates. The catalytic efficiency of rat VLCAD with 14:1 as substrate was only 4% of the efficiency determined with tetradecanoyl-CoA, whereas LCAD acted equally well on both substrates. The conclusion of this study is that LCAD serves an important, if not essential function in the beta-oxidation of unsaturated fatty acids.  (+info)

Effect of endurance training on lipid metabolism in women: a potential role for PPARalpha in the metabolic response to training. (6/138)

Endurance training increases fatty acid oxidation (FAO) and skeletal muscle oxidative capacity. However, the source of the additional fat and the mechanisms for increasing FAO capacity in muscle are not clear. We measured whole body and regional lipolytic activity and whole body and plasma FAO in six lean women during 90 min of bicycling exercise (50% pretraining peak O(2) consumption) before and after 12 wk of endurance training. We also assessed skeletal muscle content of peroxisome proliferator-activated receptor-alpha (PPARalpha) and its target proteins that regulate FAO [medium-chain and very long chain acyl-CoA dehydrogenase (MCAD and VLCAD)]. Despite a 25% increase in whole body FAO during exercise after training (P < 0.05), training did not alter regional adipose tissue lipolysis (abdominal: 0.56 +/- 0.26 and 0.57 +/- 0.10 micromol x 100 g(-1) x min(-1); femoral: 0.13 +/- 0.07 and 0.09 +/- 0.02 micromol x 100 g(-1) x min(-1)), whole body palmitate rate of appearance in plasma (168 +/- 18 and 150 +/- 25 micromol/min), and plasma FAO (554 +/- 61 and 601 +/- 45 micromol/min). However, training doubled the levels of muscle PPARalpha, MCAD, and VLCAD. We conclude that training increases the use of nonplasma fatty acids and may enhance skeletal muscle oxidative capacity by PPARalpha regulation of gene expression.  (+info)

Mitochondrial transcription factor A is increased but expression of ATP synthase beta subunit and medium-chain acyl-CoA dehydrogenase genes are decreased in hearts of copper-deficient rats. (7/138)

The mechanism(s) by which impaired mitochondrial respiratory function and the accumulation of lipid droplets and mitochondria in hearts of copper-deficient rats occur remains unclear. It is not known whether specific components of the regulatory pathway involved in mitochondrial biogenesis, such as mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2), are activated in copper deficiency. Little is known about gene expression of enzymes involved in fatty acid oxidation (FAO) in hearts of copper-deficient rats. Male weanling rats were fed copper-adequate (CuA), copper-deficient (CuD) or pair-fed (CuP) diets for 5 wk. Mitochondria and lipid droplet volume densities from electron micrographs were greater and there was an elevation in the mtTFA protein level in hearts of copper-deficient rats. DNA binding activities of NRF-1 and NRF-2 did not differ among the groups. Northern blot analysis of cardiac tissue revealed that transcripts of F(1)F(0)-ATP synthase subunit c were greater, but mRNA levels of ATP synthase beta subunit and the FAO enzyme, medium-chain acyl-CoA dehydrogenase (MCAD), were lower in hearts of copper-deficient rats. Long-chain acyl-CoA dehydrogenase (LCAD) mRNA levels did not differ among treatment groups. These results suggest that certain components of the mitochondrial biogenesis program are activated in hearts of copper-deficient rats. F(1)F(0)-ATP synthase beta subunit and MCAD transcript levels remain low, which may contribute to impaired mitochondrial respiratory function, decreased fatty acid utilization and lipid droplet accumulation in hearts of copper-deficient rats.  (+info)

Production of fatty acid components of meadowfoam oil in somatic soybean embryos. (8/138)

The seed oil of meadowfoam (Limnanthes alba) and other Limnanthes spp. is enriched in the unusual fatty acid Delta(5)-eicosenoic acid (20:1Delta(5)). This fatty acid has physical and chemical properties that make the seed oil of these plants useful for a number of industrial applications. An expressed sequence tag approach was used to identify cDNAs for enzymes involved in the biosynthesis of 20:1Delta(5)). By random sequencing of a library prepared from developing Limnanthes douglasii seeds, a class of cDNAs was identified that encode a homolog of acyl-coenzyme A (CoA) desaturases found in animals, fungi, and cyanobacteria. Expression of a cDNA for the L. douglasii acyl-CoA desaturase homolog in somatic soybean (Glycine max) embryos behind a strong seed-specific promoter resulted in the accumulation of Delta(5)-hexadecenoic acid to amounts of 2% to 3% (w/w) of the total fatty acids of single embryos. Delta(5)-Octadecenoic acid and 20:1Delta(5) also composed <1% (w/w) each of the total fatty acids of these embryos. In addition, cDNAs were identified from the L. douglasii expressed sequence tags that encode a homolog of fatty acid elongase 1 (FAE1), a beta-ketoacyl-CoA synthase that catalyzes the initial step of very long-chain fatty acid synthesis. Expression of the L. douglassi FAE1 homolog in somatic soybean embryos was accompanied by the accumulation of C(20) and C(22) fatty acids, principally as eicosanoic acid, to amounts of 18% (w/w) of the total fatty acids of single embryos. To partially reconstruct the biosynthetic pathway of 20:1Delta(5) in transgenic plant tissues, cDNAs for the L. douglasii acyl-CoA desaturase and FAE1 were co-expressed in somatic soybean embryos. In the resulting transgenic embryos, 20:1Delta(5) and Delta(5)-docosenoic acid composed up to 12% of the total fatty acids.  (+info)

Very long-chain acyl-CoA dehydrogenase deficiency (VLCAD) is a rare genetic condition resulting from a mutation (change) in a persons DNA. Due to this change, people with VLCAD have problems breaking down certain fats properly. VLCAD occurs when the body either does not make enough or makes non-working enzyme called very long-chain acyl-CoA dehydrogenase. Enzymes are proteins that help break down the food we eat into the pieces our body can use for energy. In this case, the job of the VLCAD enzyme is to break down the very long-chain fatty acids, which are parts of the fat from our food. These fatty acids are important energy sources when there are not enough sugars in the body, such as in between meals. A person with VLCAD cannot use this type of fatty acid for energy because it cant break it down. This also causes a build-up of too many unused very long-chain fatty acids, which can be harmful to the body.. Those affected by VLCAD can show symptoms any time between infancy and adulthood. ...
Three general forms of clinical presentation in VLCAD deficient patients are known.5 6 The severe childhood form of the disease consists of patients with early onset of symptoms, a very high mortality, or a high number of disease episodes, presence of cardiomyopathy, and siblings who have died. The second group is the mild childhood form and includes patients presenting later in infancy and childhood with a generally milder presentation (fasting induced hypoketotic hypoglycaemia) and fewer episodes of disease precipitation. Cardiomyopathy is rare in this group and mortality much lower. The third group of patients presents in adulthood with an isolated muscular form of the disease (myopathy, rhabdomyolysis, and myoglobinuria). It has recently been shown that patients with the severe childhood form of the disease preferentially have "null" mutations that lead to no residual enzyme activity.6 Our patient is considered to have a severe neonatal form with cardiomyopathy and a severe homozygous ...
A role for mitochondrial fatty acid oxidation in the peripheral signaling cascade of leptin, adiponectin and insulin has recently been proposed from animal studies but has not been investigated in humans. Children with trifunctional protein (TFP, including deficiency of long-chain hydroxyacyl-CoA dehydrogenase) and very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency, inherited disorders of long-chain fatty acid ß-oxidation, lack an ability to oxidize fatty acids for energy. They have increased levels of body fat and circulating leptin and a high incidence of obesity. Current therapy for children with these disorders is based on frequent meals and consuming a low fat, very high carbohydrate diet. Despite treatment, exercise induced rhabdomyolysis is a common complication of TFP and VLCAD deficiency that frequently leads to exercise avoidance. The effects of these genetic defects on body composition and weight regulation have not been investigated. The contribution of fatty-acid oxidation ...
Idiopathic pulmonary fibrosis (IPF) is a chronic progressive lung disease of unknown etiology. We previously revealed increased oxidative stress and high expression of antioxidant proteins in culture cell lines established from lesional lung tissues with IPF (Kabuyama Y, Oshima K, Kitamura T, Homma M, Yamaki J, Munakata M, Homma Y. Genes Cells 12: 1235-1244, 2007). In this study, we show that IPF cells contain high levels of free cholesterol and its peroxidized form as compared with normal TIG7 lung fibroblasts, suggesting that radical oxygen species (ROS) are generated within specific organelles. To understand the molecular basis underlying the generation of ROS in IPF cells, we performed proteomic analysis of mitochondrial proteins from TIG and IPF cells. This analysis shows that the phosphorylation of Ser586 of very long chain acyl-CoA dehydrogenase (VLCAD) is significantly reduced in IPF cells. Similar results are obtained from immunoblotting with anti-pS586 antibody. Kinase activity toward ...
Need some antibodies - posted in Immunology: I need antibody against LCHAD, MTP/TFP, VLCAD, SCHAD, MCAD, and dont know which company sells those antibodies. long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) mitochondrial trifunctional protein (MTP/TFP) very long-chain acyl-CoA dehydrogenase (VLCAD) short-chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD) medium-chain 3-hydroxyacyl-CoA dehydrogenase (MCAD) Does anybody know? THANKS!!!
Three mitochondrial metabolic pathways are required for efficient energy production in eukaryotic cells: the electron transfer chain (ETC), fatty acid β-oxidation (FAO), and the tricarboxylic acid cycle. The ETC is organized into inner mitochondrial membrane supercomplexes that promote substrate channeling and catalytic efficiency. Although previous studies have suggested functional interaction between FAO and the ETC, their physical interaction has never been demonstrated. In this study, using blue native gel and two-dimensional electrophoreses, nano-LC-MS/MS, immunogold EM, and stimulated emission depletion microscopy, we show that FAO enzymes physically interact with ETC supercomplexes at two points. We found that the FAO trifunctional protein (TFP) interacts with the NADH-binding domain of complex I of the ETC, whereas the electron transfer enzyme flavoprotein dehydrogenase interacts with ETC complex III. Moreover, the FAO enzyme very-long-chain acyl-CoA dehydrogenase physically interacted ...
Shop Probable very-long-chain ELISA Kit, Recombinant Protein and Probable very-long-chain Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
(2015) Malik et al. Circulation. Background - Circulating very-long-chain saturated fatty acids (VLCSFAs) may play an active role in the origin of cardiometabolic diseases. Methods and Results - We measured 3 VLCSFAs (C20:0, C22:0, and C24:0) in plasma and erythrocytes using gas-liquid chromatogr...
Jerry Vockley and Inform Network describe everything you want to know about CACT deficiency, a rare fatty acid oxidation disorder. Read more about its symptoms and some developing treatments.
Long-chain fatty acid oxidation disorders (LC-FAOD) can cause cardiac hypertrophy and cardiomyopathy, often presenting in infancy, typically leading to death or heart transplant despite ongoing treatment. Previous data on triheptanoin treatment of cardiomyopathy in LC-FAOD suggested a clinical benef …
Inclusion Criteria:. Subjects must give written, signed and dated informed consent. Confirmed diagnosis of FAOD. A diagnostic acylcarnitine profile, in blood or cultured fibroblasts. A stable treatment regimen for at least 30 days prior to enrollment. Exclusion Criteria:. Unstable or poorly controlled disease. Treatment with an investigational drug within 1 month or within 5 half-lives, whichever is longer. Have been hospitalized within 3 months prior to screening for any major medical event. Pregnant or nursing females ...
SLC27A2, very long-chain acyl-CoA synthetase,bile acyl-CoA synthetase,solute carrier family 27 (fatty acid transporter), member 2,solute carrier family 27 member ...
Development of an in vitro Model System for Assessing the Effect of the Adrenoleukodstrophy Protein on Very Long-Chain acyl-CoA Synthetase Activity ...
Fatty acids are one of the bodys fuels: oxidation is the process by which they are broken down to release energy. This process has many steps, each catalysed by a different enzyme. Fatty acid oxidation disorders result from deficiency of one of the enzymes.
Information on the #FADF5A html color code with its RGB and HSL make up, lighter and darker colors, analogous colors, and trinary colors.
Vitamin B2 (Riboflavin) is one of the member of vitamin B complex found abundantly in Venison, Yogurt, Soybeans, Milk,Mushrooms, Spinach, Tempeh etc.. It plays an important role in converting foods (fats, ketone bodies, carbohydrates, and proteins) to energy. B. Vitamin B2 (Riboflavin) Vitamin B2 and short-chain acyl-CoA dehydrogenase deficiency Short-chain acyl-CoA dehydrogenase deficiency (SCADD) is …. ...
Information, Tools, and Resources to aid Primary Care Physicians in caring for Children with Special Health Care Needs (CSHCN) and providing a Medical Home for all of their patients.
Looking for information on Acyl-CoA dehydrogenase, very long chain, deficiency of? Medigest has all you need to know about Acyl-CoA dehydrogenase, very long chain, deficiency of - Symptoms and Signs, Causes, Treatments and definition
Information, Tools, and Resources to aid Primary Care Physicians in caring for Children with Special Health Care Needs (CSHCN) and providing a Medical Home for all of their patients.
Background The origin of eukaryotes remains a fundamental question in evolutionary biology. Although it is clear that eukaryotic genomes are a chimeric combination of genes of eubacterial and archaebacterial ancestry, the specific ancestry of most eubacterial genes is still unknown. The growing availability of microbial genomes offers the possibility of analyzing the ancestry of eukaryotic genomes and testing previous hypotheses on their origins. Methodology/Principal Findings Here, we have applied a phylogenomic analysis to investigate a possible contribution of the Myxococcales to the first eukaryotes. We conducted a conservative pipeline with homologous sequence searches against a genomic sampling of 40 eukaryotic and 357 prokaryotic genomes. The phylogenetic reconstruction showed that several eukaryotic proteins traced to Myxococcales. Most of these proteins were associated with mitochondrial lipid intermediate pathways, particularly enzymes generating reducing equivalents with pivotal roles ...
Aronson R, Uttech S, Soref M: "The Effect of Maternal Cigarette Smoking on Low Birth Weight and Preterm Birth in Wisconsin, 1991" Wisconsin Medical Journal. 1993:92, 613-617.. Aronson RA, Hunt LH: "Cocaine Use during Pregnancy and its Impact on Mothers and Infants: Implications for Physicians". Wisconsin Medical Journal 1990:89, 105-110.. Aronson RA, Griebel D, Cobb J: "Wisconsins Birth and Developmental Outcome Monitoring Program". Wisconsin Medical Journal , 1989:88, 35-36.. Aronson RA, Griebel D, Cobb J: "Wisconsins Birth and Development Outcome Monitoring Program". Wisconsin Medical Journal , 1990: 89, 115-118.. Ciske JB, Hoffman G, Hanson K, Annable KM, Wolff J, Litsheim T, Laessig R, Aronson R: "Newborn Screening in Wisconsin - Program Overview and the Addition of a Test to Screen for Organic Acidemias and Fatty Acid Oxidation Disorders". Wisconsin Medical Journal, 2000:99, 38-42. ...
ALDEN1_2.PE11 Location/Qualifiers FT CDS_pept complement(13882..15045) FT /locus_tag="Alide_0011" FT /gene_family="HOG000131659" [ FAMILY / ALN / TREE ] FT /inference="protein motif:PFAM:PF02771" FT /codon_start="1" FT /product="acyl-CoA dehydrogenase domain-containing protein" FT /transl_table="11" FT /note="PFAM: acyl-CoA dehydrogenase domain-containing FT protein; KEGG: reh:H16_A2143 acyl-CoA dehydrogenase, FT long-chain specific" FT /db_xref="GI:319760749" FT /db_xref="GO:0003995" FT /db_xref="InterPro:IPR006089" FT /db_xref="InterPro:IPR006090" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR006092" FT /db_xref="GeneID:10102034" FT /translation="MMTSDHIALQDSVRKLIEREIEPHVDEWEAAEIFPAHEVFKKLGS FT AGFLGVNKPVEFGGMGLDYSYEIAFCEAIGGISSGGVGMAIAVQTDMATPALTHFGSDE FT LRELFLKPTVAGDMVVCLGVSESGAGSDVASLKTTARKDGDDYVINGSKMWITNGTQAD FT WMCLLANTSEGDVHRNKSLICLPLRENGKLRPGISMQKIKKVGMWASDTAQVFFDEVRV FT PQRYRIGEEGKGFTYQMRQFQEERLSGATRRVTALSNVIDETIAYTRQRKAFGRSILDN FT ...
Actinoalloteichus cyanogriseus strain NRRL B-2194 methyltransferase (caeG2), transporter (caeH3), transcriptional regulator (caeI2), ABC transporter (caeH1), ABC transporter (caeH2), acyl-CoA dehydrogenase (caeB5), methyltransferase (caeG1), aminotransferase (caeC), FAD-dependentt oxidoreductase (caeB6), NrpS (caeA1), L-lysine 2-amino transferase (caeP1), FAD-dependent oxidoreductase (caeP2), PKS/NrpS (caeA2), NrpS (caeA3), acyl-CoA dehydrogenase (caeB1), thioesterase (caeA4), LuxR family two component transcriptional regulator (caeI1), amidohydrolase (caeD), AMP-dependent ligase (caeF), aldehyde dehydrogenase (caeB2), FAD-dependent oxidoreductase (caeB3), F420-dependent NADP oxidoreductase (caeB4), transcriptional regulator (caeI3), and monooxygenase (caeB7) genes, complete ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Disclaimer: The information contained in this site is intended for general reference purposes only. It is not a substitute for professional medical advice or a medical exam. Always seek the advice of your physician or other qualified health professional before starting any new treatment ...
Pathway:Human:Mitochondrial fatty acid betaoxidation]] moved to [[Pathway:Homo sapiens:Mitochondrial fatty acid betaoxidation]]: Renaming ...
Complete information for ACAD10 gene (Protein Coding), Acyl-CoA Dehydrogenase Family Member 10, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Please note: This is a general description and information on the disorder. There are mild, moderate and severe forms of this disorder. In our case we are very lucky that Landon has an extremely mild case and his life will not be as effected as some of the stuff you will read below. Landon also has the "hypoglycemia" form of the disorder. He does not have any of the heart defects, liver, muscle, and kidney issues that go along with the more sever forms of the disorder. With Landon we just have to make sure that he does not get dehydrated, he is not allowed to fast at all, and if he does get the stomach flu or viruses like that he has to go into the hospital and have a glucose IV until he can keep food down for a number of hours. Landons form of the disorder is not fatal unless he does get severly dehydrated and then he can slip into a coma, but it would take a lot for that to happen to him. We count our blessing everyday that he is so mild. With that being said, googling and reading all of this ...
포화 지방의 섭취를 줄이거나 제한하기 위한 권장사항들은 세계보건기구,[71] 미국 심장 협회,[6] 캐나다 보건부,[72] 미국 보건복지부,[73] 영국 국민 건강 서비스,[74] 오스트레일리아 연방 보건복지부,[75] 싱가포르 건강촉진국,[76] 인도 정부 시민건강포털,[77] 뉴질랜드 보건부,[78] 홍콩 식품안전청[79] 등에 의해 만들어졌다. 2003년에 세계보건기구(WHO)와 식량농업기구(FAO)의 전문가 협의 보고서는 포화 지방산의 섭취는 심혈관계 질환의 위험과 직접 관련이 있다고 결론을 내렸다.[80] 기존의 목표는 포화 지방산의 섭취를 일일 에너지 섭취량의 10% 미만, 고위험군의 경우 7% 미만으로 제한하는 것이다. 만약 10% 미만을 섭취하는 경우 섭취량을 늘리지 않아야 한다. 이러한 한계 내에서 미리스트산 및 팔미트산이 풍부한 음식의 섭취는 이러한 특정 지방산의 함량이 ...
Looking for online definition of acyl-CoA dehydrogenase family member 9, mitochondrial in the Medical Dictionary? acyl-CoA dehydrogenase family member 9, mitochondrial explanation free. What is acyl-CoA dehydrogenase family member 9, mitochondrial? Meaning of acyl-CoA dehydrogenase family member 9, mitochondrial medical term. What does acyl-CoA dehydrogenase family member 9, mitochondrial mean?
Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency (OMIM 201450) is the most common inherited disorder of fatty acid metabolism presenting with hypoglycaemia, hepatopathy and Reye-like symptoms during catabolism. In the past, the majority of patients carried the prevalent c.985A|G mutation in the ACADM gene. Since the introduction of newborn screening many other mutations with unknown clinical relevance have been identified in asymptomatic newborns. In order to identify functional effects of these mutant genotypes we correlated residual MCAD (OMIM 607008) activities as measured by octanoyl-CoA oxidation in lymphocytes with both genotype and relevant medical reports in 65 newborns harbouring mutant alleles. We identified true disease-causing mutations with residual activities of 0 to 20%. In individuals carrying the c.199T|C or c.127G|A mutation on one allele, residual activities were much higher and in the range of heterozygotes (31%-60%). Therefore, both mutations cannot clearly be associated with a
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Since the introduction of NBS for MCAD deficiency, a new subgroup of newborns has been identified with variant ACADM genotypes that have not been seen before in clinically ascertained patients with classical ACADM genotypes. It remains unclear whether subjects with these variant ACADM genotypes are at risk for the development of a clinical phenotype. Prevention of prolonged fasting was found to be debatable when MCAD enzyme activities ,10% were measured with PP-CoA [2]. In the current study, additional support was provided to abandon the advice on prevention of prolonged fasting under normal conditions in subjects with residual MCAD enzyme activities ,10%. All included subjects could tolerate an overnight controlled fasting tolerance test for at least 15 hours under healthy conditions. An additional PPA loading test determined in vivo residual MCAD enzyme activity. These functional tests were performed after the age of 6 months in all cases, when weaning naturally occurs and PPA loading tests ...
Yosipof A, Guedes RC, García-Sosa AT. Data Mining and Machine Learning Models for Predicting Drug Likeness and their Disease or Organ Category. Frontiers in Chemistry 2018; accepted for publication.. Bonito CA, Nunes J, Leandro J, Louro F, Leandro P, Ventura FV, and Guedes RC. Unveiling the Pathogenic Molecular Mechanisms of the Most Common Variant (p.K329E) in Medium-Chain Acyl-CoA Dehydrogenase Deficiency by in Vitro and in Silico Approaches. Biochemistry 2016; 55: 7086-7098.. Guerreiro PS, Estácio SG, Antunes F, Fernandes AS, Pinheiro PF, Costa JG, Castro M, Miranda JP, Guedes RC, Oliveira NG. Structure-based virtual screening toward the discovery of novel inhibitors of the DNA repair activity of the human apurinic/apyrimidic endonuclease 1. Chem Biol Drug Des 2016; 88: 915-925.. Guedes RA, Serra P, Salvador JAR, Guedes RC. Computational Approaches forthe Discovery of Human Proteasome Inhibitors: An Overview. Molecules, 2016; 21: 927.. Areias LRP, Ruivo EFP, Goncalves LM, Duarte MT., André ...
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1EGC: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
1EGC: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
If a metabolic crisis is not treated, breathing problems, seizures, coma, brain damage and sometimes death can occur.. Between episodes of metabolic crisis, babies with VLCAD may not show any signs of the disease. Other babies with VLCAD may have problems with their heart, liver and muscles.. Screening and treatment aim to prevent metabolic crises and other symptoms and help children with VLCAD to lead the healthiest lives possible.. ...
Medium chain acyl dehydrogenase deficiency is a fatty acid oxidation disorder associated with inborn errors of metabolism. It is often known as MCAD or MCADD.
Chace DH, Adam BW, Smith SJ, Alexander JR, Hillman SL, Hannon WH. Validation of accuracy-based amino acid reference materials in dried-blood spots by tandem mass spectrometry for newborn screening assays. Clin Chem. 1999;45:1269-77.. Wang SS, Fernhoff PM, Hannon WH, Khoury MJ. Mediumchain acyl-CoA dehydrogenase deficiency: human genome epidemiology review. Genet Med. 1999;1(7):332-9.. Hannon WH, Henderson LO, Bell CJ. Newborn screening quality assurance. In: Khoury MJ, Burke W, Thomson EJ, editors. Genetics and public health in the 21st century: using genetic information to improve health and prevent disease. NewYork: Oxford University Press, 2000:243-58.. Mei JV, Alexander JR, Adam BW, Hannon WH. Use of filter paper for the collection and analysis of human whole blood specimens. J Nutr. 2001;131:1631S-6S.. Centers for Disease Control and Prevention. Using tandem mass spectrometry for metabolic disease screening among newborns: a report of a work group. MMWR Morb Mortal Wkly Rep. ...
CP000667.PE429 Location/Qualifiers FT CDS 488729..489889 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Strop_0429" FT /product="acyl-CoA dehydrogenase domain protein" FT /note="PFAM: acyl-CoA dehydrogenase domain protein; FT Acyl-CoA dehydrogenase, type 2, C-terminal domain" FT /db_xref="EnsemblGenomes-Gn:Strop_0429" FT /db_xref="EnsemblGenomes-Tr:ABP52914" FT /db_xref="GOA:A4X214" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="InterPro:IPR013786" FT /db_xref="InterPro:IPR036250" FT /db_xref="InterPro:IPR037069" FT /db_xref="UniProtKB/TrEMBL:A4X214" FT /protein_id="ABP52914.1" FT /translation="MSPLDLLDVDSSLSAEERQIRAVVRQLVDEQVRPHVAGWYEEGRV FT PARELAREFGRLGLLGMHLTGYGCAGSSAVAYGLACLELEAGDSGVRSLVSVQGALAMY FT AIWRYGSTEQKQHWLPAMAAGETIGCFALTEPDHGSDPASMTTRARRDGDDWVLHGTKM FT WITNATIADVAVIWARTDEGVRGFAVPTSTPGVAVREIRRKMSLRASVTGEISLDDVRL FT PAAARLPDAVGLKAPLGCLTEARHGIVWGALGAARDCLETTLEYAGSRTQFGRPLAGFQ FT ...
Stellaris smFISH probes targeting acdh-1, a short-chain acyl-CoA dehydrogenase, are shown in red (Cal Fluor 610). DAPI/blue marks embryonic nuclei, and PGL-1::GFP shows the corresponding location of P granules surrounding germ cell nuclei (arrowheads, green). During embryogenesis (A), acdh-1 expression begins in the E cells (arrow, red). Expression continues in the developing intestine, shown in red, throughout embryogenesis. Intestinal expression of acdh-1 persists through larval development in the L1 (B) and L2 (C) stages. These results extend previous findings from Arda et al., where acdh-1 was shown to be expressed in the adult intestine. scale = 20µ ...
The liver is an important site of fat oxidation, which participates in the metabolic regulation of food intake. We showed previously that mice with genetically inactivated Acads, encoding short-chain acyl-CoA dehydrogenase (SCAD), shift food consumption away from fat and toward carbohydrate when tested in a macronutrient choice paradigm. This phenotypic eating behavior suggests a link between fat oxidation and nutrient choice which may involve an energy sensing mechanism. To identify hepatic processes that could trigger energy-related signals, we have now performed transcriptional, metabolite and physiological analyses in Acads-/- mice following short-term (2 days) exposure to either high- or low-fat diet. Metabolite analysis revealed 25 acylcarnitine species that were altered by diet and/or genotype. Compared to wild-type mice, phosphorylated AMP-activated protein kinase was 40 % higher in Acads-/- mice after short-term high-fat diet, indicating a low ATP/AMP ratio. Metabolite analyses in isolated
This gene encodes the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Defects in this gene cause medium-chain acyl-CoA dehydrogenase deficiency, a disease characterized by hepatic dysfunction, fasting hypoglycemia, and encephalopathy, which can result in infantile death. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] ...
Ultragenyx Announces Submission of New Drug Application to FDA for UX007 (triheptanoin) for Treatment of Long-Chain Fatty Acid Oxidation Disorders - - Novato (California)
Patient Preparation: A previous bone marrow transplant from an allogenic donor will interfere with testing. Call Mayo Medical Laboratories for instructions for testing patients who have received a bone marrow transplant.. Submit only 1 of the following specimens:. Preferred:. Specimen Type: Whole blood. Container/Tube:. Preferred: Lavender top (EDTA) or yellow top (ACD). Acceptable: Any anticoagulant. Specimen Volume: 3 mL. Collection Instructions:. 1. Invert several times to mix blood.. 2. Send specimen in original tube.. Specimen Stability Information: Ambient (preferred)/Refrigerated. Specimen Type: Cultured fibroblasts. Container/Tube: T-25 flask. Specimen Volume: 2 Full flasks. Specimen Stability Information: Ambient (preferred)/Refrigerated. Specimen Type: Blood spot. Supplies: Card - Blood Spot Collection (Filter Paper) (T493). Container/Tube:. Preferred: Collection card (Whatman Protein Saver 903 Paper). Acceptable: Ahlstrom 226 filter paper, or Blood Spot Collection Card ...
The elevation of synthesis and export of fatty acids from the chloroplast following N deprivation could indicate that TAG is assembled from fatty acids that are synthesized de novo. This step would require the activation of the fatty acids by a long-chain acyl-CoA synthetase. In fact, increased abundance of RNA encoding a putative long-chain acyl-CoA synthetase was observed, and the respective protein has been identified in the lipid droplet proteome (Moellering and Benning, 2010). However, another enzyme that could contribute to the changing spectrum of fatty acids is a putative phospholipid/glycerol acyltransferase, for which the transcript level decreased during N deprivation. Long-chain acyl-CoA synthetases are likely to play a key role in determining the fate of fatty acids in the cell (Shockey et al., 2002). Regulation of the respective genes could be a major factor in controlling the flux of fatty acids toward glycerolipid synthesis and their degradation by β-oxidation.. Major ...
Inborn errors of metabolism (IEM) represent a group of inherited diseases in which genetic defect leads to the block on a metabolic pathway, resulting in a single enzyme dysfunction. As a downstream consequence of the residual or full loss of the enzymatic activity, there is an accumulation of toxic metabolites in the proximity of the metabolic block and/or a deficiency of an essential metabolic product which leads to the clinical presentation of the disease. While individually IEMs are rare, a collectively estimated incidence of metabolic inherited disorders is 1:800. The genetic basis of IEMs can involve abnormalities such as point mutations, deletions or insertions, or more complex genomic rearrangements. Categorization of IEM can be simply made on the basis of the affected metabolic network: fatty acids oxidation disorders, protein/amino acids metabolism disorders, disorders of carbohydrate metabolism, lysosomal storage diseases, peroxisomal disorders, and mitochondrial diseases. This chapter will
Mito New England (MNE) is sponsoring a meeting April 30 to discuss new initiatives at Mass. General Hospital to assist in diagnosis and management of complex medical problems. Dr. Amel Karaa, Dr. Mark Korson, and Tim Boyd from NORD will share their perspectives. This event is open to all affected by complex disease, including but not limited to: Fabry disease, Gaucher disease, Pompe disease, Mucopolysaccahridosis, Mitochondrial disease, Niemann Pick, Fatty acid oxidation disorders, Glycogen storage diseases, Ehler Danlos Syndrome, and other random genetic conditions. Read more. ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (VLCAD) is an enzyme that in humans is encoded by the ACADVL ... This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product ... "Very Long-Chain Acyl-Coenzyme a Dehydrogenase Deficiency". 1993. PMID 20301763. GeneReviews/NCBI/NIH/UW entry on Very long- ... "acyl-CoA dehydrogenase, very long chain". Strauss AW, Powell CK, Hale DE, Anderson MM, Ahuja A, Brackett JC, Sims HF (Nov 1995 ...
... acyl-CoA dehydrogenase, long chain - which is a member of the acyl-CoA dehydrogenase family. The acyl-CoA dehydrogenase family ... "Cardiac hypertrophy in mice with long-chain acyl-CoA dehydrogenase or very long-chain acyl-CoA dehydrogenase deficiency". ... Acyl-CoA dehydrogenase, long chain". Kurtz DM, Tolwani RJ, Wood PA (May 1998). "Structural characterization of the mouse long- ... Acyl-CoA dehydrogenase, long chain is a protein that in humans is encoded by the ACADL gene. ACADL is a gene that encodes LCAD ...
"Long-Chain Acyl CoA Dehydrogenase Deficiency: Background, Pathophysiology, Epidemiology". eMedicine. 24 March 2016. Retrieved ... long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), long-chain enoyl-CoA hydratase, and long-chain thiolase activities. ... Avoiding factors that might precipitate condition Glucose Low fat/high carbohydrate nutrition Long-chain acyl-CoA dehydrogenase ... "HADHA hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit [Homo ...
"Long-chain acyl-CoA dehydrogenase deficiency as a cause of pulmonary surfactant dysfunction". The Journal of Biological ... Wang SS, Fernhoff PM, Hannon WH, Khoury MJ (1999). "Medium chain acyl-CoA dehydrogenase deficiency human genome epidemiology ... "Molecular cloning of cDNAs encoding rat and human medium-chain acyl-CoA dehydrogenase and assignment of the gene to human ... "Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation ...
Acyl-CoA dehydrogenase, C-2 to C-3 short chain is an enzyme that in humans is encoded by the ACADS gene. This gene encodes a ... The coding sequence of this gene is 1239 bp long. The encoded protein has 412 amino acids, and its size is 44.3 kDa (Human) or ... As short-chain acyl-CoA dehydrogenase is involved in beta-oxidation, a deficiency in this enzyme is marked by an increased ... Mutations of the ACADS gene are associated with a deficiency in the encoded protein short chain acyl-CoA dehydrogenase; this is ...
"Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain". Biochemical and ... typically C16-acylCoA and longer. It has been observed that ACAD9 can catalyze acyl-CoAs with very long chains. The specific ... "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients". ... Acyl-CoA dehydrogenase family member 9, mitochondrial is an enzyme that in humans is encoded by the ACAD9 gene. The ACAD9 gene ...
... it interferes with the transport of long-chain fatty acids into the mitochondria. Also, it inhibits acyl-CoA dehydrogenases, so ...
... is broken down into shorter-chain fatty acids in the human liver by the long-chain acyl CoA dehydrogenase enzyme. ... although the long-term use of Lorenzo's oil (oleic acid and erucic acid) in the treatment of adrenoleukodystrophy or ... While there are reports of toxicity from long-term use of Lorenzo's oil (which contains erucic acid and other ingredients), ... Erucic acid is produced by elongation of oleic acid via oleoyl-coenzyme A and malonyl-CoA. ...
"Identification and characterization of new long chain acyl-CoA dehydrogenases". Molecular Genetics and Metabolism. 102 (4): 418 ... Acyl-CoA dehydrogenase family, member 10 is a protein that in humans is encoded by the ACAD10 gene. This gene encodes a member ... Acyl-CoA dehydrogenase family, member 10". Bian L, Hanson RL, Muller YL, Ma L, Kobes S, Knowler WC, Bogardus C, Baier LJ (Jul ... of the acyl-CoA dehydrogenase family of enzymes (ACADs), which participate in the beta-oxidation of fatty acids in mitochondria ...
CoA) hydratase, long-chain 3-hydroxy acyl-coenzyme A dehydrogenase and long-chain 3-ketoacyl CoA thiolase. Fatty acid beta- ... "Long-Chain Acyl CoA Dehydrogenase Deficiency: eMedicine Pediatrics: Genetics and Metabolic Disease". Retrieved 2009-07-11. Wang ...
... deficiency of Acyl-CoA dehydrogenase, short chain, deficiency of Acyl-CoA dehydrogenase, very long chain, deficiency of Acyl- ... promyelocytic leukemia Acute renal failure Acute respiratory distress syndrome Acute tubular necrosis Acyl-CoA dehydrogenase, ... CoA oxidase deficiency Adactylia unilateral dominant ADAM complex Adams-Nance syndrome Adams-Oliver syndrome Addison's disease ... Alpers disease Alpha 1-antitrypsin deficiency Alpha-2 deficient collagen disease Alpha-ketoglutarate dehydrogenase deficiency ...
Trimethoprim Triple A syndrome Tumors Tyrosinaemia type 1 Urea cycle disorder Uremia Very-long-chain acyl-CoA dehydrogenase ... Reye syndrome Ritonavir Saquinavir Sepsis Septic shock Severe hepatitis Sheehan syndrome Short-chain acyl-CoA dehydrogenase ... deficiency Maple syrup urine disease Mcquarrie type infantile idiopathic hypoglycemia Medium chain acyl-CoA dehydrogenase ... Disorders of fatty acid oxidation Medium chain acylCoA dehydrogenase deficiency (MCAD) Familial Leucine sensitive hypoglycemia ...
... displays decreased thermal stability and is overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient patients with ... "Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase". Biochem. Soc. Trans ... 2007). "Transient multiple acyl-CoA dehydrogenation deficiency in a newborn female caused by maternal riboflavin deficiency". ... in electron-transfer-flavoprotein have been implicated in type II glutaricaciduria in which multiple acyl CoA dehydrogenase ...
... displays decreased thermal stability and is overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient patients with ... 2003). "Clear relationship between ETF/ETFDH genotype and phenotype in patients with multiple acyl-CoA dehydrogenation ... 1999). "A polymorphic variant in the human electron transfer flavoprotein alpha-chain (alpha-T171) ... which shuttles electrons between primary flavoprotein dehydrogenases involved in mitochondrial fatty acid and amino acid ...
"Very long-chain fatty acids". X-ald Database. Retrieved 5 January 2013. "Very long-chain acyl-CoA dehydrogenase deficiency". ... A very long chain fatty acid (VLCFA) is a fatty acid with 22 or more carbons. Their biosynthesis occurs in the endoplasmic ... doi:10.1016/j.plipres.2006.01.004 "Very-long-chain fatty acids from the animal and plant kingdoms" Rezanka, Tomas Progress in ... Increased plasma content of saturated very long chain fatty acids". Neurology. 31 (10): 1241-1241. ISSN 0028-3878. doi:10.1212/ ...
... or long-chain fatty acid acyl-CoA substrates. While different dehydrogenases target fatty acids of varying chain length, all ... "Thermal unfolding of medium-chain acyl-CoA dehydrogenase and iso(3)valeryl-CoA dehydrogenase: study of the effect of genetic ... "Mechanism of activation of acyl-CoA substrates by medium chain acyl-CoA dehydrogenase: interaction of the thioester carbonyl ... Acyl CoA Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718- ...
I The mechanism of elongation of long-chain fatty acids by acetyl-CoA". Biochim. Biophys. Acta. 164 (3): 498-517. doi:10.1016/ ... In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction acyl-CoA + ... crotonyl-CoA reductase, and acyl-CoA dehydrogenase (NADP+). As of late 2007, only one structure has been solved for this class ... Other names in common use include 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide, ...
... medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and ... Short-chain acyl-CoA dehydrogenase (EC 1.3.8.1, butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase, butyryl dehydrogenase, ... short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:( ... Short-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ...
... (EC 1.3.8.8, palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, long-chain acyl ... long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase, ACADL (gene).) is an enzyme with systematic name long-chain acyl-CoA: ... medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and ... Long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...
... medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and ... acyl dehydrogenase (ambiguous), fatty-acyl-CoA dehydrogenase (ambiguous), acyl CoA dehydrogenase (ambiguous), general acyl CoA ... Medium-chain acyl-CoA dehydrogenase (EC 1.3.8.7, fatty acyl coenzyme A dehydrogenase (ambiguous), acyl coenzyme A dehydrogenase ... dehydrogenase (ambiguous), medium-chain acyl-coenzyme A dehydrogenase, acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous), ...
... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ... In the mitochondria, acyl-CoA esters are involved in the acylation of mitochondrial NAD+ dependent dehydrogenases; because ... Acyl-CoA thioesterase 9 is a protein that is encoded by the human ACOT9 gene. It is a member of the acyl-CoA thioesterase ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl ...
... (EC 1.3.8.9, ACADVL (gene).) is an enzyme with systematic name very-long-chain acyl-CoA: ... "Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase ... Very-long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase". J. Biol. Chem. 267 (2): 1027-1033. PMID ...
... rarediseases.org/rare-diseases/very-long-chain-acyl-coa-dehydrogenase-deficiency-lcad/. ... Very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCADD) is a fatty-acid metabolism disorder which prevents the body ... Episodes of very long-chain acyl-coenzyme A dehydrogenase deficiency can be triggered by periods of fasting, illness, and ... CoA) dehydrogenase. Without this enzyme, very long-chain fatty acids from food and fats stored in the body cannot be degraded ...
"Medium-Chain Acyl-CoA Dehydrogenase Deficiency". Medscape.. *^ Beermann, C.; Jelinek, J.; Reinecker, T.; Hauenschild, A.; Boehm ... In chemistry, particularly in biochemistry, a fatty acid is a carboxylic acid with a long aliphatic chain, which is either ... Malonyl-CoA is then involved in a repeating series of reactions that lengthens the growing fatty acid chain by two carbons at a ... The cytosolic acetyl-CoA is carboxylated by acetyl CoA carboxylase into malonyl-CoA, the first committed step in the synthesis ...
Dehydrogenase Deficiency (GAII & MADD) 3-Hydroxy-3 Methylglutaryl-CoA Lyase (HMG) Deficiency Very long-chain acyl-coenzyme A ... Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency (LCHAD deficiency) Medium-chain acyl-coenzyme A dehydrogenase ... Short-chain acyl-coenzyme A dehydrogenase deficiency (SCAD deficiency) 3-hydroxyacyl-coenzyme A dehydrogenase deficiency (M/ ... 4 Dienoyl-CoA Reductase Deficiency Electron Transfer Flavoprotein (ETF) ...
3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA ... transferring acyl groups other than amino-acyl groups. • enoyl-CoA hydratase activity. • long-chain-3-hydroxyacyl-CoA ... "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA ... long-chain enoyl-CoA hydratase, and long-chain thiolase. This deficiency can be classified into 3 main clinical phenotypes: ...
... very-long-chain acyl-CoA dehydrogenase deficiency in three patients previously diagnosed with long-chain acyl-CoA dehydrogenase ... 1993) Very-long-chain acyl-CoA dehydrogenase deficiency: identification of a new inborn error of mitochondrial fatty acid ... Very long chain acyl-CoA dehydrogenase (VLCAD) deficiency is a recently identified inborn error of a membrane bound ... 1993) A novel disease with deficiency of mitochondrial very-long-chain acyl-CoA dehydrogenase. Biochem Biophys Res Commun 191: ...
... Common Name(s). Very long chain acyl-CoA dehydrogenase deficiency, VCLAD ... "Very long chain acyl-CoA dehydrogenase deficiency" (open studies are recruiting volunteers) and 9 "Very long chain acyl-CoA ... Very Long-chain Acyl-CoA Dehydrogenase Deficiency; Trifunctional Protein Deficiency; Long-chain 3-hydroxyacyl-CoA Dehydrogenase ... Medium-chain Acyl-CoA Dehydrogenase Deficiency; Multiple Acyl-CoA Dehydrogenase Deficiency; Carnitine Transporter Deficiency; ...
Dysregulation of very long chain acyl-CoA dehydrogenase coupled with lipid peroxidation ... This analysis shows that the phosphorylation of Ser586 of very long chain acyl-CoA dehydrogenase (VLCAD) is significantly ...
Gene encoding medium-chain acyl-CoA dehydrogenase. ACADVL: Gene encoding very long-chain acyl-CoA dehydrogenase ... Production and disposal of medium-chain fatty acids in children with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit ... Measurement of short-chain acyl-CoA dehydrogenase (SCAD) in cultured skin fibroblasts with hexanoyl-CoA as a competitive ... Enzyme analyses were performed in leukocytes with: hexanoyl-CoA (C6-CoA) +/− butyryl-CoA (C4-CoA), and phenylpropionyl-CoA (PP- ...
B. Vitamin B2 (Riboflavin) Vitamin B2 and short-chain acyl-CoA dehydrogenase deficiency Short-chain acyl-CoA dehydrogenase ... Long Dan Cao (Radix Gentianae longdancao) *Long Gu (Fossilia Ossis Mastodi) *Long Kui (Herb Solani nigri) ... Vitamin B2 and short-chain acyl-CoA dehydrogenase deficiency. Posted on September 5, 2012. by kylenorton ...
Long-chain acyl-CoA dehydrogenase (EC 1.3.8.8, palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, long-chain acyl ... long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase, ACADL (gene).) is an enzyme with systematic name long-chain acyl-CoA: ... medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and ... Long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...
Very-long-chain acyl-CoA dehydrogenase (EC 1.3.8.9, ACADVL (gene).) is an enzyme with systematic name very-long-chain acyl-CoA: ... "Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase ... Very-long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase". J. Biol. Chem. 267 (2): 1027-1033. PMID ...
... medlineplus.gov/genetics/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency/ Very long-chain acyl-CoA dehydrogenase ... Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is a condition that prevents the body from converting certain fats to ... This gene provides instructions for making an enzyme called very long-chain acyl-CoA dehydrogenase, which is required to break ... Recurrent ACADVL molecular findings in individuals with a positive newborn screen for very long chain acyl-coA dehydrogenase ( ...
2 patients with very long chain Acyl-CoA dehydrogenase deficiency experience fatigue, insomnia, depressed mood, pain, and ... Find the most comprehensive real-world symptom and treatment data on very long chain Acyl-CoA dehydrogenase deficiency at ... What is very long chain Acyl-CoA dehydrogenase deficiency?. Very long chain acyl-coenzyme A dehydrogenase deficiency is a ... Who has very long chain Acyl-CoA dehydrogenase deficiency on PatientsLikeMe?. * 2 patients have this condition ...
PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. ... PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. ... Very long-chain-specific acyl-CoA dehydrogenase, mitochondrialImported. ,p>Information which has been imported from another ... tr,B1AR28,B1AR28_MOUSE Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadvl PE=1 SV=1 ...
Species about Experts and Doctors on long chain acyl coa dehydrogenase in Düsseldorf, North Rhine Westphalia, Germany ... long chain acyl coa dehydrogenase*inborn errors lipid metabolism*dihydroxyacetone phosphate*fructosephosphates*acyl coa ... Experts and Doctors on long chain acyl coa dehydrogenase in Düsseldorf, North Rhine Westphalia, Germany. Summary. Locale: ... You are here: Locale , Germany , North Rhine Westphalia , Experts and Doctors on long chain acyl coa dehydrogenase in ...
Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the initial rate-limiting step in mitochondrial fatty acid beta- ... Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency Am J Hum Genet. 1999 ... Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the initial rate-limiting step in mitochondrial fatty acid beta- ... clear genotype-phenotype relationship is in sharp contrast to what has been observed in medium-chain acyl-CoA dehydrogenase ...
Rhabdomyolysis is common in very long-chain acyl-CoA dehydrogenase deficiency (VLCADD) and other metabolic myopathies, but its ...
A severe genotype with favourable outcome in very long chain acyl-CoA dehydrogenase deficiency ... A severe genotype with favourable outcome in very long chain acyl-CoA dehydrogenase deficiency ...
Very Long Chain Acyl CoA Dehydrogenase Deficiency (VLCAD)Download version for offline viewing or printing. [480.71kB] ... Very long-chain acyl-CoA dehydrogenase deficiency (VLCAD) is a rare, inherited (genetic) disease. ... Treatment is started as early as possible and is usually life long. Babies with VLCAD have their health and development checked ... Babies with VLCAD cannot make certain fats into energy, especially during long periods without food (fasting). ...
... long chain (ACADL), nuclear gene encoding mitochondrial protein, 200 uL, ,10^7 TU/mL, 200 µl. ... Home » ORF » Human Lenti ORF Particles » Lenti ORF particles, ACADL (mGFP-tagged)-Human acyl-CoA dehydrogenase, long chain ( ... RC206624L2V Lenti ORF particles, ACADL (mGFP-tagged)-Human acyl-CoA dehydrogenase, long chain (ACADL), nuclear gene encoding ... Properties for Lenti ORF particles, ACADL (mGFP-tagged)-Human acyl-CoA dehydrogenase, long chain (ACADL), nuclear gene encoding ...
Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can ... This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product ... HCA RNA Cell Line for Very long-chain specific acyl-CoA dehydrogenase, mitochondrial. ... Compartment GO Terms for Very long-chain specific acyl-CoA dehydrogenase, mitochondrial. ...
Very long chain acyl-coA dehydrogenase deficiency (VLCADD) is an autosomal recessive inborn error of fatty acid oxidation ... Infants suspected to have very-long chain acyl-CoA dehydrogenase deficiency from newborn screening.. *J Lawrence Merritt, ... Positive newborn screen in a normal infant of a mother with asymptomatic very long-chain Acyl-CoA dehydrogenase deficiency.. * ... Very long chain acyl-coA dehydrogenase deficiency (VLCADD) is an autosomal recessive inborn error of fatty acid oxidation ...
... is one of four straight-chain acyl-CoA dehydrogenase (ACD) enzymes, which are all nuclear encoded mitochondrial flavoproteins ... Moreover, human VLCAD and human acyl-CoA oxidase showed extensive sequence homology corroborating the notion that these genes ... Very-long-chain acyl-CoA dehydrogenase (VLCAD) is one of four straight-chain acyl-CoA dehydrogenase (ACD) enzymes, which are ... Molecular and cellular pathology of very-long-chain acyl-CoA dehydrogenase deficiency.. Manuel Schiff, A Mohsen, +3 authors ...
... Critical elevation of C14:1 acylcarnitine.. What does this mean? ... InicioAbnormal Newborn ScreeningFor Healthcare ProvidersFatty Acid Oxidation DisordersVery long chain acyl CoA dehydrogenase ... This infant may have Very Long Chain Acyl-oA Dehydrogenase deficiency. Further testing is required. ... Medium chain acyl CoA dehydrogenase deficiency (MCAD). *Trifunctional protein deficiency (TFP). *Very long chain acyl CoA ...
Long-chain-acyl-CoA dehydrogenase (LCADH) has been produced by recombinant techniques from the human cDNA and purified after ... Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation. * Home ... Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation. Publikationstyp: ... Characterization_of_human_and_pig_kidney_long_chain_acyl_CoA_dehydrogenases_and_their_role_in_beta_oxidation.pdf. 142. ...
Very long-chain acyl-CoA dehydrogenase is required to metabolize a group of fats called very long-chain fatty acids. These ... Very long-chain acyl-CoA dehydrogenase deficiency. More than 100 mutations in the ACADVL gene have been found to cause very ... Very long-chain acyl-CoA dehydrogenase is essential for fatty acid oxidation, which is the multistep process that breaks down ( ... The ACADVL gene provides instructions for making an enzyme called very long-chain acyl-CoA dehydrogenase (VLCAD). This enzyme ...
... which is associated with very long chain acyl-CoA dehydrogenase (VLCAD) deficiency and elevated C14, C14:1 acylcarnitines on ... Invitae Very Long Chain Acyl-CoA Dehydrogenase Deficiency Test. Test description. The Invitae Very Long Chain Acyl-CoA ... Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency. Am. J. Hum. Genet. ... Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency. Am. J. Hum. Genet. ...
very long chain. Very long-chain acyl-coenzyme A dehydrogenase deficiency ("VLCAD") ... Medium-chain acyl-coenzyme A dehydrogenase deficiency ("MCAD") ACADS. C-2 to C-3 short chain. Short-chain acyl-coenzyme A ... long chain. - ACADM. C-4 to C-12 straight chain (medium chain). ... Acyl CoA. External links. *Acyl-CoA+Dehydrogenase at the US ... Acyl CoA dehydrogenase is the enzyme used to catalyze the first step of β-oxidation in Fatty acid metabolism. ...
... very long chain, deficiency of? Medigest has all you need to know about Acyl-CoA dehydrogenase, very long chain, deficiency of ... Discuss Acyl-CoA dehydrogenase, very long chain, deficiency of in our forums Discuss Acyl-CoA dehydrogenase, very long chain, ... Acyl-CoA dehydrogenase, very long chain, deficiency of Below you will find more information about Acyl-CoA dehydrogenase, very ... Very-Long-Chain Acyl-CoA Dehydrogenase Deficiency (VLCADD) is a rare autosomal recessive condition in which the body fails to ...
  • Enzyme analyses with C6-CoA, C6-CoA + C4-CoA, and PP-CoA identified significantly higher residual MCAD enzyme activities in subjects with variant ACADM genotypes when compared to patients with classical ACADM genotypes. (biomedcentral.com)
  • Knowledge of the profile of fatty acids, including the profile of long chain fatty acids, is an important parameter for many areas like human health, food sciences, and the study of gene expression in. (bioportfolio.com)
  • Sodium phenylbutyrate decreases plasma branched-chain amino acids in patients with urea cycle disorders. (ohsu.edu)
  • Although the pediatrician may rarely be called on to be the sole provider of long-term care to patients with these complex disorders, he or she will be responsible for the emergency care and stabilization of the infants and children affected and should be familiar with the fundamental aspects of such care. (aappublications.org)
  • Inside the mitochondrion is a group of proteins that carry electrons along four chain reactions (Complexes I-IV), resulting in energy production. (umdf.org)
  • Proteins are made of amino acids arranged in a linear chain joined together by peptide bonds. (wikipedia.org)
  • Clinical symptoms mainly develop during periods of illness or fasting and affect organs preferring long-chain fat as primary source of energy, such as heart and skeletal muscle. (biomedcentral.com)