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.Alcohol 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.Coenzyme AGlyceraldehyde-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).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.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.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.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.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.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 1.1.1.14Glycerolphosphate DehydrogenaseFatty 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)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)Oxidoreductases: 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)Kinetics: The rate dynamics in chemical or physical systems.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.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 ComplexTriazenes: Compounds with three contiguous nitrogen atoms in linear format, H2N-N=NH, and hydrocarbyl derivatives.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.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.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.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 1.1.99.10.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.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.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.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.Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.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.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.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.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.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).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.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)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.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).Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.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)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.Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.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.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.Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.TriglyceridesOleic Acids: A group of fatty acids that contain 18 carbon atoms and a double bond at the omega 9 carbon.Cholesterol: The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.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.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.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.Microbodies: Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.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.Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)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.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.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.Acylation: The addition of an organic acid radical into a molecule.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.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).11-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.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)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).Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.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.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.
(1/257) Molecular cloning of cDNA encoding mitochondrial very-long-chain acyl-CoA dehydrogenase from bovine heart.

AIM: To clone the cDNA encoding an isoenzyme of mitochondrial very-long-chain acyl-CoA dehydrogenase (VLCAD) from bovine heart lambda gt11 and lambda gt10 cDNA libraries. METHODS: The clone was isolated with immunoscreening technique and validated by (1) the microsequences of the N-terminus and three internal proteolytic fragments from the purified enzyme; (2) identification of the acyl-CoA dehydrogenase (AD) signature sequence; and (3) high homology of the deduced peptide sequences, as expected, with those of rat liver mitochondrial VLCAD. RESULTS: The cDNA (2203 bp) corresponds to a approximately 2.4-kb mRNA band from the same tissue source revealed by a Northern blotting. The deduced peptide sequence of 655 amino acids (70,537 Da) is composed of a 40-amino acid mitochondrial leader peptide moiety (4,346 Da) and a 615-amino acid peptide as a mature protein (66,191 Da). A comparison of the peptide sequences in the AD family shows the major diversity in their signal sequences, suggesting a structural basis for their different mitochondrial locations. The catalytic sites are all highly conserved among VLCAD. Ser-251 analogous to and Cys-215 diversified to other family members. A pseudo-consensus sequence of leucine zipper was found in the C-terminal region from Leu-568 to Leu-589, implying a mechanism whereby the dimer of this protein is formed by zipping these leucine residues from the alpha-helixes of 2 monomers. CONCLUSION: The isolated cDNA clone encodes an isoenzyme of mitochondrial VLCAD in bovine heart.  (+info)

(2/257) The medium-/long-chain fatty acyl-CoA dehydrogenase (fadF) gene of Salmonella typhimurium is a phase 1 starvation-stress response (SSR) locus.

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)

(3/257) Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC.

The activities of beta-oxidation enzymes were measured in extracts of glucose- and triolein-grown cells of Aspergillus niger. Growth on triolein stimulated increased enzyme activity, especially for acyl-CoA dehydrogenase. No acyl-CoA oxidase activity was detected. HPLC analysis after incubation of triolein-grown cell extracts with decanoyl-CoA showed that beta-oxidation was limited to one cycle. Octanoyl-CoA accumulated as the decanoyl-CoA was oxidized. Beta-oxidation enzymes in isolated mitochondrial fractions were also studied. The results are discussed in the context of methyl ketone production by fungi.  (+info)

(4/257) Outcome of medium chain acyl-CoA dehydrogenase deficiency after diagnosis.

BACKGROUND: Medium chain acyl-CoA dehydrogenase (MCAD) deficiency is the most common inborn error of fatty acid metabolism. Undiagnosed, it has a mortality rate of 20-25%. Neonatal screening for the disorder is now possible but it is not known whether this would alter the prognosis. OBJECTIVE: To investigate the outcome of MCAD deficiency after the diagnosis has been established. METHOD: All patients with a proved diagnosis of MCAD deficiency attending one centre in a four year period were reviewed. RESULTS: Forty one patients were identified. Follow up was for a median of 6.7 years (range, 9 months to 14 years). Nearly half of the patients were admitted to hospital with symptoms characteristic of MCAD deficiency before the correct diagnosis was made. After diagnosis, two patients were admitted to hospital with severe encephalopathy but there were no additional deaths or appreciable morbidity. There was a high incidence (about one fifth) of previous sibling deaths among the cohort. CONCLUSIONS: Undiagnosed, MCAD deficiency results in considerable mortality and morbidity. However, current management improves outcome, supporting the view that the disorder should be included in newborn screening programmes.  (+info)

(5/257) A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes.

Short-chain acyl-CoA oxidases are beta-oxidation enzymes that are active on short-chain acyl-CoAs and that appear to be present in higher plant peroxisomes and absent in mammalian peroxisomes. Therefore, plant peroxisomes are capable of performing complete beta-oxidation of acyl-CoA chains, whereas mammalian peroxisomes can perform beta-oxidation of only those acyl-CoA chains that are larger than octanoyl-CoA (C8). In this report, we have shown that a novel acyl-CoA oxidase can oxidize short-chain acyl-CoA in plant peroxisomes. A peroxisomal short-chain acyl-CoA oxidase from Arabidopsis was purified following the expression of the Arabidopsis cDNA in a baculovirus expression system. The purified enzyme was active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Cell fractionation and immunocytochemical analysis revealed that the short-chain acyl-CoA oxidase is localized in peroxisomes. The expression pattern of the short-chain acyl-CoA oxidase was similar to that of peroxisomal 3-ketoacyl-CoA thiolase, a marker enzyme of fatty acid beta-oxidation, during post-germinative growth. Although the molecular structure and amino acid sequence of the enzyme are similar to those of mammalian mitochondrial acyl-CoA dehydrogenase, the purified enzyme has no activity as acyl-CoA dehydrogenase. These results indicate that the short-chain acyl-CoA oxidases function in fatty acid beta-oxidation in plant peroxisomes, and that by the cooperative action of long- and short-chain acyl-CoA oxidases, plant peroxisomes are capable of performing the complete beta-oxidation of acyl-CoA.  (+info)

(6/257) Cloning and mapping of three pig acyl-CoA dehydrogenase genes.

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)

(7/257) Peroxisome proliferator-activated receptor alpha mediates the adaptive response to fasting.

Prolonged deprivation of food induces dramatic changes in mammalian metabolism, including the release of large amounts of fatty acids from the adipose tissue, followed by their oxidation in the liver. The nuclear receptor known as peroxisome proliferator-activated receptor alpha (PPARalpha) was found to play a role in regulating mitochondrial and peroxisomal fatty acid oxidation, suggesting that PPARalpha may be involved in the transcriptional response to fasting. To investigate this possibility, PPARalpha-null mice were subjected to a high fat diet or to fasting, and their responses were compared with those of wild-type mice. PPARalpha-null mice chronically fed a high fat diet showed a massive accumulation of lipid in their livers. A similar phenotype was noted in PPARalpha-null mice fasted for 24 hours, who also displayed severe hypoglycemia, hypoketonemia, hypothermia, and elevated plasma free fatty acid levels, indicating a dramatic inhibition of fatty acid uptake and oxidation. It is shown that to accommodate the increased requirement for hepatic fatty acid oxidation, PPARalpha mRNA is induced during fasting in wild-type mice. The data indicate that PPARalpha plays a pivotal role in the management of energy stores during fasting. By modulating gene expression, PPARalpha stimulates hepatic fatty acid oxidation to supply substrates that can be metabolized by other tissues.  (+info)

(8/257) Evaluating newborn screening programmes based on dried blood spots: future challenges.

A UK national programme to screen all newborn infants for phenylketonuria was introduced in 1969, followed in 1981 by a similar programme for congenital hypothyroidism. Decisions to start these national programmes were informed by evidence from observational studies rather than randomised controlled trials. Subsequently, outcome for affected children has been assessed through national disease registers, from which inferences about the effectiveness of screening have been made. Both programmes are based on a single blood specimen, collected from each infant at the end of the first week of life, and stored as dried spots on a filter paper or 'Guthrie' card. This infrastructure has made it relatively easy for routine screening for other conditions to be introduced at a district or regional level, resulting in inconsistent policies and inequitable access to effective screening services. This variation in screening practices reflects uncertainty and the lack of a national framework to guide the introduction and evaluation of new screening initiatives, rather than geographical variations in disease prevalence or severity. More recently, developments in tandem mass spectrometry have made it technically possible to screen for several inborn errors of metabolism in a single analytical step. However, for each of these conditions, evidence is required that the benefits of screening outweigh the harms. How should that evidence be obtained? Ideally policy decisions about new screening initiatives should be informed by evidence from randomised controlled trials but for most of the conditions for which newborn screening is proposed, large trials would be needed. Prioritising which conditions should be formally evaluated, and developing a framework to support their evaluation, poses an important challenge to the public health, clinical and scientific community. In this chapter, issues underlying the evaluation of newborn screening programmes will be discussed in relation to medium chain acyl CoA dehydrogenase deficiency, a recessively inherited disorder of fatty acid oxidation.  (+info)

*  Fatty acid metabolism
Dehydrogenation by acyl-CoA dehydrogenase, yielding 1 FADH2 Hydration by enoyl-CoA hydratase Dehydrogenation by 3-hydroxyacyl- ... In order for the acyl-CoA to enter the mitochondrion the carnitine shuttle is used: Acyl-CoA is transferred to the hydroxyl ... Acetyl-CoA is formed into malonyl-CoA by acetyl-CoA carboxylase, at which point malonyl-CoA is destined to feed into the fatty ... acetyl-CoA and 1 molecule of propionyl-CoA per molecule of fatty acid. Each beta oxidative cut of the acyl-CoA molecule yields ...
*  Acyl CoA dehydrogenase
Acyl CoA Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718- ... "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 ... An additional class of acyl-CoA dehydrogenase was discovered that catalyzes α,β-unsaturation reactions with steroid-CoA ...
*  Acyl-CoA dehydrogenase (NADP+)
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, ... the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+. This ...
*  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 ... Thorpe, C.; Kim, J.J. (1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718-725. PMID ...
*  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: ... Long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the ...
*  Medium-chain acyl-CoA dehydrogenase
... 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), ... Medium-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ...
*  Very-long-chain acyl-CoA dehydrogenase
... (EC 1.3.8.9, ACADVL (gene).) is an enzyme with systematic name very-long-chain acyl-CoA: ... Very-long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... crystal structure of human very-long-chain acyl-CoA dehydrogenase". J. Biol. Chem. 283 (14): 9435-9443. doi:10.1074/jbc. ... I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase". J. Biol. Chem. 267 (2): 1027-1033. PMID ...
*  Electron-transferring-flavoprotein dehydrogenase
The entire sequence of transfer reactions is as follows: Acyl-CoAAcyl-CoA dehydrogenase → ETF → ETF-QO → UQ → Complex III. ... Deficiency in ETF dehydrogenase causes the human genetic disease multiple acyl-CoA dehydrogenase deficiency. ETQ-QO links the ... Singla M, Guzman G, Griffin AJ, Bharati S (Mar 2008). "Cardiomyopathy in multiple Acyl-CoA dehydrogenase deficiency: a clinico- ... also known as MADD for multiple acyl-CoA dehydrogenase deficiency), in which there is an improper buildup of fats and proteins ...
*  ACADVL
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (VLCAD) is an enzyme that in humans is encoded by the ACADVL ... Acyl CoA dehydrogenase GRCh38: Ensembl release 89: ENSG00000072778 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... "acyl-CoA dehydrogenase, very long chain". Strauss AW, Powell CK, Hale DE, Anderson MM, Ahuja A, Brackett JC, Sims HF (Nov 1995 ... "Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency". American Journal of ...
*  ACADS
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 ... 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 ... GeneReviews/NCBI/NIH/UW entry on Short-Chain Acyl-CoA Dehydrogenase Deficiency Human ACADS genome location and ACADS gene ...
*  Medium-chain acyl-coenzyme A dehydrogenase deficiency
Medium-chain acyl-CoA dehydrogenase deficiency, often known as MCAD deficiency or MCADD, is a disorder of fatty acid oxidation ... Rinaldo, P.; O'Shea, J. J.; Coates, P. M.; Hale, D. E.; Stanley, C. A.; Tanaka, K. (1988). "Medium-Chain Acyl-CoA Dehydrogenase ... "Maternal medium-chain acyl-CoA dehydrogenase deficiency identified by newborn screening". Molecular Genetics and Metabolism. ... "The natural history of medium-chain acyl CoA dehydrogenase deficiency in the Netherlands: Clinical presentation and outcome". ...
*  Very long chain fatty acid
"Very long-chain acyl-CoA dehydrogenase deficiency". Genetics Home Reference, National Institutes of Health. Retrieved 5 January ...
*  ACADL
... 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 is a protein that in humans is encoded by the ACADL gene. ACADL is a gene that encodes LCAD ... Acyl CoA dehydrogenase This article incorporates text from the United States National Library of Medicine, which is in the ...
*  ACAD10
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 ... "Identification and characterization of new long chain acyl-CoA dehydrogenases". Molecular Genetics and Metabolism. 102 (4): 418 ... of the acyl-CoA dehydrogenase family of enzymes (ACADs), which participate in the beta-oxidation of fatty acids in mitochondria ...
*  Mitochondrial trifunctional protein deficiency
"Long-Chain Acyl CoA Dehydrogenase Deficiency: Background, Pathophysiology, Epidemiology". eMedicine. 24 March 2016. Retrieved ... "HADHA hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit [Homo ... "OMIM Entry - * 600890 - HYDROXYACYL-CoA DEHYDROGENASE/3-KETOACYL-CoA THIOLASE/ENOYL-CoA HYDRATASE, ALPHA SUBUNIT; HADHA". omim. ... Avoiding factors that might precipitate condition Glucose Low fat/high carbohydrate nutrition Long-chain acyl-CoA dehydrogenase ...
*  ACADM
Wang SS, Fernhoff PM, Hannon WH, Khoury MJ (1999). "Medium chain acyl-CoA dehydrogenase deficiency human genome epidemiology ... "Long-chain acyl-CoA dehydrogenase deficiency as a cause of pulmonary surfactant dysfunction". The Journal of Biological ... "Molecular cloning of cDNAs encoding rat and human medium-chain acyl-CoA dehydrogenase and assignment of the gene to human ... Exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship". Human Mutation. 18 ...
*  Glutaryl-CoA dehydrogenase
... (GCDH) is an enzyme encoded by the GCDH gene on chromosome 19. The protein belongs to the acyl-CoA ... Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ (August 2004). "Crystal structures of human glutaryl-CoA dehydrogenase with ... Rao KS, Albro M, Dwyer TM, Frerman FE (December 2006). "Kinetic mechanism of glutaryl-CoA dehydrogenase". Biochemistry. 45 (51 ... Chemistry portal Molecular and Cellular Biology portal Biotechnology portal Glutaryl-CoA dehydrogenase at the US National ...
*  ACADSB
Short/branched chain acyl-CoA dehydrogenase(ACADSB) is a member of the acyl-CoA dehydrogenase family of enzymes that catalyze ... an enzyme in the acyl CoA dehydrogenase family. It can cause short/branched-chain acyl-CoA dehydrogenase deficiency. The human ... "Entrez Gene: acyl-CoA dehydrogenase, short/branched chain". Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, ... The cDNA is significantly similar to the cDNA of other members of the acyl-CoA dehydrogenase family; its structure is closest ...
*  Short-chain acyl-coenzyme A dehydrogenase deficiency
"Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ... "Orphanet: Short chain acyl CoA dehydrogenase deficiency". www.orpha.net. Retrieved 2016-10-30. Online Mendelian Inheritance in ... "Short-chain acyl-CoA dehydrogenase deficiency , Genetic and Rare Diseases Information Center(GARD) - an NCATS Program". ... Mutations in the ACADS gene lead to inadequate levels of short-chain acyl-CoA dehydrogenase, which is important for breaking ...
*  Nitroalkane oxidase
"Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily". Proc ... a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase". Arch. Biochem. Biophys. 433 (1): 157-65. doi:10.1016/j. ...
*  Oxidative phosphorylation
Ikeda Y, Dabrowski C, Tanaka K (25 January 1983). "Separation and properties of five distinct acyl-CoA dehydrogenases from rat ... Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". J. Biol. Chem. 258 (2): 1066-76. PMID 6401712. Ruzicka ... as it accepts electrons from multiple acetyl-CoA dehydrogenases. In plants, ETF-Q oxidoreductase is also important in the ... NADH dehydrogenase succinate dehydrogenase Coenzyme Q - cytochrome c reductase cytochrome c oxidase Metabolism portal. ...
*  ETFA
"Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase". Biochem. Soc. Trans ... displays decreased thermal stability and is overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient patients with ... 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 ...
*  Very long-chain acyl-coenzyme A dehydrogenase deficiency
... 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 ...
*  Sodium phenylbutyrate
"Evidence for involvement of medium chain acyl-CoA dehydrogenase in the metabolism of phenylbutyrate". Molecular Genetics and ... In the human body it is first converted to phenylbutyryl-CoA and then metabolized by mitochondrial beta-oxidation, mainly in ...
*  Hydrogen
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
*  Metabolism
Fatty acids are made by fatty acid synthases that polymerize and then reduce acetyl-CoA units. The acyl chains in the fatty ... Hundreds of separate types of dehydrogenases remove electrons from their substrates and reduce NAD+ into NADH. This reduced ... and this breakdown process involves the release of significant amounts of acetyl-CoA, propionyl-CoA, and pyruvate, which can ... Finally, the acetyl group on the CoA is oxidised to water and carbon dioxide in the citric acid cycle and electron transport ...
*  Methylene cyclopropyl acetic acid
MCPA is a potent inhibitor of acyl CoA dehydrogenase, thus preventing the metabolism of fatty acids. The intolerance to ...
Functional Effects of Different Medium-Chain Acyl-CoA Dehydrogenase Genotypes and Identification of Asymptomatic Variants  Functional Effects of Different Medium-Chain Acyl-CoA Dehydrogenase Genotypes and Identification of Asymptomatic Variants
The octanoyl-CoA oxidation rate, therefore, allows a risk assessment at birth and the identification of new ACADM genotypes ... This demonstrates a correlation between the octanoyl-CoA oxidation rate in lymphocytes and the clinical outcome. With newborn ... activities as measured by octanoyl-CoA oxidation in lymphocytes with both genotype and relevant medical reports in 65 newborns ... Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency (OMIM 201450) is the most common inherited disorder of fatty acid ...
more infohttp://journals.plos.org/plosone/article?id=10.1371/journal.pone.0045110
77 Mutations of Human Medium-Chain Acyl-CoA Dehydrogenase | Biochemical Society Transactions  77 Mutations of Human Medium-Chain Acyl-CoA Dehydrogenase | Biochemical Society Transactions
77 Mutations of Human Medium-Chain Acyl-CoA Dehydrogenase. SZABOLCS UDVARI, PETER BROSS, BRAGE S ANDRESEN, NIELS GREGERSEN, ... 77 Mutations of Human Medium-Chain Acyl-CoA Dehydrogenase. SZABOLCS UDVARI, PETER BROSS, BRAGE S ANDRESEN, NIELS GREGERSEN, ... 77 Mutations of Human Medium-Chain Acyl-CoA Dehydrogenase Message Subject (Your Name) has forwarded a page to you from ...
more infohttp://www.biochemsoctrans.org/content/26/1/S65
The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other...  The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other...
Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 ... The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other ... The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other ... The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other ...
more infohttp://www.biochemj.org/content/224/2/577
acyl-CoA dehydrogenase deficiency  acyl-CoA dehydrogenase deficiency
B. Vitamin B2 (Riboflavin) Vitamin B2 and short-chain acyl-CoA dehydrogenase deficiency Short-chain acyl-CoA dehydrogenase ... Vitamin B2 and short-chain acyl-CoA dehydrogenase deficiency. Posted on September 5, 2012. by kylenorton ...
more infohttp://kylenorton.healthblogs.org/category/acyl-coa-dehydrogenase-deficiency/
Medical Home Portal - Short-Chain Acyl-CoA Dehydrogenase Deficiency (SCADD)  Medical Home Portal - Short-Chain Acyl-CoA Dehydrogenase Deficiency (SCADD)
Short-Chain Acyl-CoA acyl-CoA Dehydrogenase Deficiency - Information for Professionals (STAR-G). Structured list of information ... Short-Chain Acyl-CoA Dehydrogenase Deficiency - Information for Parents (STAR-G). A fact sheet, written by a genetic counselor ... Because short-chain acyl-CoA dehydrogenase deficiency (SCADD) (the result of an intramitochondrial defect in the beta-oxidation ... Short-chain Acyl-CoA Dehydrogenase Deficiency (Genetics Home Reference). Excellent, detailed review of condition for patients ...
more infohttps://www.medicalhomeportal.org/newborn/short-chain-acyl-coa-dehydrogenase-deficiency
Acyl CoA dehydrogenase deficiency synonyms, acyl CoA dehydrogenase deficiency antonyms - FreeThesaurus.com  Acyl CoA dehydrogenase deficiency synonyms, acyl CoA dehydrogenase deficiency antonyms - FreeThesaurus.com
Antonyms for acyl CoA dehydrogenase deficiency. 1 synonym for acyl: acyl group. What are synonyms for acyl CoA dehydrogenase ... Synonyms for acyl CoA dehydrogenase deficiency in Free Thesaurus. ... acyl. (redirected from acyl CoA dehydrogenase deficiency). Also found in: Dictionary, Medical, Encyclopedia.. Related to acyl ... Acyl CoA dehydrogenase deficiency synonyms, acyl CoA dehydrogenase deficiency antonyms - FreeThesaurus.com https://www. ...
more infohttps://www.freethesaurus.com/acyl+CoA+dehydrogenase+deficiency
In vitro and in vivo consequences of variant medium-chain acyl-CoA dehydrogenase genotypes | Orphanet Journal of Rare Diseases ...  In vitro and in vivo consequences of variant medium-chain acyl-CoA dehydrogenase genotypes | Orphanet Journal of Rare Diseases ...
Enzyme analyses were performed in leukocytes with: hexanoyl-CoA (C6-CoA) +/− butyryl-CoA (C4-CoA), and phenylpropionyl-CoA (PP- ... Enzyme analyses with C6-CoA, C6-CoA + C4-CoA, and PP-CoA identified significantly higher residual MCAD enzyme activities in ... Measurement of short-chain acyl-CoA dehydrogenase (SCAD) in cultured skin fibroblasts with hexanoyl-CoA as a competitive ... Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is the most common inherited disorder of the mitochondrial fatty acid ...
more infohttps://ojrd.biomedcentral.com/articles/10.1186/1750-1172-8-43
Short-chain specific acyl-CoA dehydrogenase, mitochondrial - DrugBank  Short-chain specific acyl-CoA dehydrogenase, mitochondrial - DrugBank
Short-chain specific acyl-CoA dehydrogenase, mitochondrial. Details. Name. Short-chain specific acyl-CoA dehydrogenase, ... Short-chain specific acyl-CoA dehydrogenase, mitochondrial. P16219. Details. Drug Relations. Drug Relations. DrugBank ID. Name ...
more infohttps://www.drugbank.ca/bio_entities/BE0000762
RCSB PDB - Protein Feature View 









 - Putative acyl-CoA dehydrogenase - B4EGC8 (B4EGC8 BURCJ)  RCSB PDB - Protein Feature View - Putative acyl-CoA dehydrogenase - B4EGC8 (B4EGC8 BURCJ)
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
more infohttps://www.rcsb.org/pdb/protein/B4EGC8
RCSB PDB - Protein Feature View 









 - Probable acyl-CoA dehydrogenase FadE26 - I6YCA3 (I6YCA3 MYCTU)  RCSB PDB - Protein Feature View - Probable acyl-CoA dehydrogenase FadE26 - I6YCA3 (I6YCA3 MYCTU)
Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA (3-OCS-CoA) to yield (24E)-3 ... 3-OCO-CoA) as well as 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) (PubMed:26161441). It dehydrogenates only (25S)-OCS-CoA ... 25S-3-oxo-cholest-4-en-26-oyl-CoA + acceptor = 3-oxo-cholest-4,24-dien-26-oyl-CoA + reduced acceptor. UniProt ... cholest-4,24-dien-26-oyl-CoA (PubMed:26348625, PubMed:26161441). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en ...
more infohttp://www.rcsb.org/pdb/protein/I6YCA3
PatientsLikeMe | Very long chain Acyl-CoA dehydrogenase deficiency symptoms, treatments & patient forums | PatientsLikeMe  PatientsLikeMe | Very long chain Acyl-CoA dehydrogenase deficiency symptoms, treatments & patient forums | PatientsLikeMe
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 ... Very long chain Acyl-CoA dehydrogenase deficiency We're all in this for good.. ...
more infohttps://www.patientslikeme.com/conditions/2525-very-long-chain-acyl-coa-dehydrogenase-deficiency
Acyl-CoA dehydrogenase | definition of acyl-CoA dehydrogenase by Medical dictionary  Acyl-CoA dehydrogenase | definition of acyl-CoA dehydrogenase by Medical dictionary
What is acyl-CoA dehydrogenase? Meaning of acyl-CoA dehydrogenase medical term. What does acyl-CoA dehydrogenase mean? ... Looking for online definition of acyl-CoA dehydrogenase in the Medical Dictionary? acyl-CoA dehydrogenase explanation free. ... acyl-CoA dehydrogenase. acyl-CoA dehydrogenase. /ac·yl-CoA de·hy·dro·gen·ase/ (de-hi´dro-jen-ās) any of several enzymes that ... long-chain acyl-CoA dehydrogenase (ACADL), acyl-CoA synthetase (ACSL1), very long chain acyl-CoA dehydrogenase (ACADVL), ...
more infohttp://medical-dictionary.thefreedictionary.com/acyl-CoA+dehydrogenase
Acyl-CoA dehydrogenases | definition of acyl-CoA dehydrogenases by Medical dictionary  Acyl-CoA dehydrogenases | definition of acyl-CoA dehydrogenases by Medical dictionary
What is acyl-CoA dehydrogenases? Meaning of acyl-CoA dehydrogenases medical term. What does acyl-CoA dehydrogenases mean? ... Looking for online definition of acyl-CoA dehydrogenases in the Medical Dictionary? acyl-CoA dehydrogenases explanation free. ... acyl-CoA dehydrogenases. acyl-CoA dehydrogenases. Enzymes that activate the first stage of the oxidation of fatty acids.. ... Selective Inhibition of Acyl-CoA Dehydrogenases by a Metabolite of Hypoglycin.. Inactivation of General Acyl-CoA Dehydrogenase ...
more infohttp://medical-dictionary.thefreedictionary.com/acyl-CoA+dehydrogenases
Full text] Screening for medium-chain acyl CoA dehydrogenase deficiency: current  | RRN  Full text] Screening for medium-chain acyl CoA dehydrogenase deficiency: current | RRN
Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is the most common disorder associated with fatty acid oxidation. The ... Screening for medium-chain acyl CoA dehydrogenase deficiency: current perspectives Claudia Soler-Alfonso,1 Michael J Bennett,2 ... Medium chain acyl-CoA dehydrogenase deficiency caused by a deletion of exons 11 and 12. Hum Mol Genet. 1995;4(4):747-749. ... Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: diagnosis by acylcarnitine analysis in blood. Am J Hum Genet. 1993;52(5 ...
more infohttps://www.dovepress.com/screening-for-medium-chain-acyl-coa-dehydrogenase-deficiency-current-p-peer-reviewed-fulltext-article-RRN
Acyl CoA dehydrogenase - Wikipedia  Acyl CoA dehydrogenase - Wikipedia
Acyl CoA Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718- ... "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 ... An additional class of acyl-CoA dehydrogenase was discovered that catalyzes α,β-unsaturation reactions with steroid-CoA ...
more infohttps://en.wikipedia.org/wiki/Acyl_CoA_dehydrogenase
Acadvl - Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial - Mus musculus (Mouse) - Acadvl gene & protein  Acadvl - Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial - Mus musculus (Mouse) - Acadvl gene & protein
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. ... IPR006089. Acyl-CoA_DH_CS. IPR006091. Acyl-CoA_Oxase/DH_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. ... IPR006089. Acyl-CoA_DH_CS. IPR006091. Acyl-CoA_Oxase/DH_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. ...
more infohttp://www.uniprot.org/uniprot/B1AR28
Acyl-CoA dehydrogenase (NADP+) - Wikipedia  Acyl-CoA dehydrogenase (NADP+) - Wikipedia
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, ... the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+. This ...
more infohttps://en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase_(NADP+)
ACADSB - Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial precursor - Pongo abelii (Sumatran orangutan) -...  ACADSB - Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial precursor - Pongo abelii (Sumatran orangutan) -...
... isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA ... Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of ... Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, ... PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. ...
more infohttp://www.uniprot.org/uniprot/Q5RF40
Experts and Doctors on long chain acyl coa dehydrogenase in Düsseldorf, North Rhine Westphalia, Germany  Experts and Doctors on long chain acyl coa dehydrogenase in Düsseldorf, North Rhine Westphalia, Germany
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 ...
more infohttp://www.labome.org/locale/germany/north/experts-and-doctors-on-long-chain-acyl-coa-dehydrogenase-in-d--sseldorf--north-rhine-westphalia--germany-2056993.html
Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. Effects of starvation | Biochemical Journal  Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. Effects of starvation | Biochemical Journal
Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. Effects of starvation. N S Ross, C L Hoppel ... The activity of this enzyme is increased such that the ratio of short-chain acyl-CoA dehydrogenase apoenzyme to holoenzyme does ... We conclude that short-chain acyl-CoA dehydrogenase activity is limiting for fatty acid oxidation when its activity falls below ... Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. Effects of starvation ...
more infohttp://www.biochemj.org/content/244/2/387
  • This enzyme's action represents the first step in fatty acid metabolism (the process of breaking long chains of fatty acids into acetyl CoA molecules). (wikipedia.org)
  • Evidence for impaired gluconeogenesis in very long-chain acyl-CoA dehydrogenase-deficient mice. (labome.org)
  • ter Veld F, Primassin S, Hoffmann L, Mayatepek E, Spiekerkoetter U. Corresponding increase in long-chain acyl-CoA and acylcarnitine after exercise in muscle from VLCAD mice. (labome.org)
  • VLCAD is specific to very long-chain fatty acids, typically C16-acylCoA and longer. (wikipedia.org)
  • It is a temporary compound formed when coenzyme A (CoA) attaches to the end of a long-chain fatty acid inside living cells. (wikipedia.org)