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.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
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.
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.
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.
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.
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.
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.
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.
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.
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
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.
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.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
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.
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).
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.
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.
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.
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.
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.
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 1.1.1.14
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)
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)
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)
The rate dynamics in chemical or physical systems.
Oxidoreductases that are specific for ALDEHYDES.
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.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
Compounds with three contiguous nitrogen atoms in linear format, H2N-N=NH, and hydrocarbyl derivatives.
A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.
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.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
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.
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.
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.
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.
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.
An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.
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.
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.
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.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
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).
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.
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.
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)
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.
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).
Oxidoreductases that are specific for KETONES.
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)
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.
An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.
A group of 16-carbon fatty acids that contain no double bonds.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
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.
Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.
A group of fatty acids that contain 18 carbon atoms and a double bond at the omega 9 carbon.
The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.
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.
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.
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.
Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.
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.
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 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.
The addition of an organic acid radical into a molecule.
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.
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).
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.
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)
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).
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
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.
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 cloning of cDNA encoding mitochondrial very-long-chain acyl-CoA dehydrogenase from bovine heart. (1/168)

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)

Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death. (2/168)

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)

Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC. (3/168)

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)

Outcome of medium chain acyl-CoA dehydrogenase deficiency after diagnosis. (4/168)

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)

A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. (5/168)

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)

Evaluating newborn screening programmes based on dried blood spots: future challenges. (6/168)

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)

A critical role for the peroxisome proliferator-activated receptor alpha (PPARalpha) in the cellular fasting response: the PPARalpha-null mouse as a model of fatty acid oxidation disorders. (7/168)

We hypothesized that the lipid-activated transcription factor, the peroxisome proliferator-activated receptor alpha (PPARalpha), plays a pivotal role in the cellular metabolic response to fasting. Short-term starvation caused hepatic steatosis, myocardial lipid accumulation, and hypoglycemia, with an inadequate ketogenic response in adult mice lacking PPARalpha (PPARalpha-/-), a phenotype that bears remarkable similarity to that of humans with genetic defects in mitochondrial fatty acid oxidation enzymes. In PPARalpha+/+ mice, fasting induced the hepatic and cardiac expression of PPARalpha target genes encoding key mitochondrial (medium-chain acyl-CoA dehydrogenase, carnitine palmitoyltransferase I) and extramitochondrial (acyl-CoA oxidase, cytochrome P450 4A3) enzymes. In striking contrast, the hepatic and cardiac expression of most PPARalpha target genes was not induced by fasting in PPARalpha-/- mice. These results define a critical role for PPARalpha in a transcriptional regulatory response to fasting and identify the PPARalpha-/- mouse as a potentially useful murine model of inborn and acquired abnormalities of human fatty acid utilization.  (+info)

The functions of the flavin contact residues, alphaArg249 and betaTyr16, in human electron transfer flavoprotein. (8/168)

Arg249 in the large (alpha) subunit of human electron transfer flavoprotein (ETF) heterodimer is absolutely conserved throughout the ETF superfamily. The guanidinium group of alphaArg249 is within van der Waals contact distance and lies perpendicular to the xylene subnucleus of the flavin ring, near the region proposed to be involved in electron transfer with medium chain acyl-CoA dehydrogenase. The backbone amide hydrogen of alphaArg249 is within hydrogen bonding distance of the carbonyl oxygen at the flavin C(2). alphaArg249 may modulate the potentials of the two flavin redox couples by hydrogen bonding the carbonyl oxygen at C(2) and by providing delocalized positive charge to neutralize the anionic semiquinone and anionic hydroquinone of the flavin. The potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples decrease in an alphaR249K mutant ETF generated by site directed mutagenesis and expression in Escherichia coli, without major alterations of the flavin environment as judged by spectral criteria. The steady state turnover of medium chain acyl-CoA dehydrogenase and glutaryl-CoA dehydrogenase decrease greater than 90% as a result of the alphaR249Ks mutation. In contrast, the steady state turnover of short chain acyl-CoA dehydrogenase was decreased about 38% when alphaR249K ETF was the electron acceptor. Stopped flow absorbance measurements of the oxidation of reduced medium chain acyl-CoA dehydrogenase/octenoyl-CoA product complex by wild type human ETF at 3 degrees C are biphasic (t(1/2)=12 ms and 122 ms). The rate of oxidation of this reduced binary complex of the dehydrogenase by the alphaR249K mutant ETF is extremely slow and could not be reasonably estimated. alphaAsp253 is proposed to function with alphaArg249 in the electron transfer pathway from medium chain acyl-CoA dehydrogenase to ETF. The steady state kinetic constants of the dehydrogenase were not altered when ETF containing an alphaD253A mutant was the substrate. However, t(1/2) of the rapid phase of oxidation of the reduced medium chain acyl-CoA dehydrogenase/octenoyl-CoA charge transfer complex almost doubled. betaTyr16 lies on a loop near the C(8) methyl group, and is also near the proposed site for interflavin electron transfer with medium chain acyl-CoA dehydrogenase. The tyrosine residue makes van der Waals contact with the C(8) methyl group of the flavin in human ETF and Paracoccus denitrificans ETF (as betaTyr13) and lies at a 30 degrees C angle with the plane of the flavin. Human betaTyr16 was substituted with leucine and alanine residues to investigate the role of this residue in the modulation of the flavin redox potentials and in electron transfer to ETF. In betaY16L ETF, the potentials of the flavin were slightly reduced, and steady state kinetic constants were modestly altered. Substitution of an alanine residue for betaTyr16 yields an ETF with potentials very similar to the wild type but with steady state kinetic properties similar to betaY16L ETF. It is unlikely that the beta methyl group of the alanine residue interacts with the flavin C(8) methyl. Neither substitution of betaTyr16 had a large effect on the fast phase of ETF reduction by medium chain acyl-CoA dehydrogenase.  (+info)

Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins. ...
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
Synonyms for acyl CoA dehydrogenase deficiency in Free Thesaurus. Antonyms for acyl CoA dehydrogenase deficiency. 1 synonym for acyl: acyl group. What are synonyms for acyl CoA dehydrogenase deficiency?
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.
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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 ...
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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
Background: Mitochondrial acyl-CoA dehydrogenase family member 9 (ACAD9) is essential for the assembly of mitochondrial respiratory chain complex I. Disease causing biallelic variants in ACAD9 have been reported in individuals presenting with lactic acidosis and cardiomyopathy. Results: We describe the genetic, clinical and biochemical findings in a cohort of 70 patients, of whom 29 previously unpublished. We found 34 known and 18 previously unreported variants in ACAD9. No patients harbored biallelic loss of function mutations, indicating that this combination is unlikely to be compatible with life. Causal pathogenic variants were distributed throughout the entire gene, and there was no obvious genotype-phenotype correlation. Most of the patients presented in the first year of life. For this subgroup the survival was poor (50% not surviving the first 2 years) comparing to patients with a later presentation (more than 90% surviving 10 years). The most common clinical findings were cardiomyopathy ...
TY - JOUR. T1 - Defective folding and rapid degradation of mutant proteins is a common disease mechanism in genetic disorders. AU - Gregersen, N. AU - Bross, P. AU - Jørgensen, M M. AU - Corydon, T J. AU - Andresen, B S. PY - 2000/7. Y1 - 2000/7. N2 - Many disease-causing point mutations do not seriously compromise synthesis of the affected polypeptide but rather exert their effects by impairing subsequent protein folding or stability of the folded protein. This often results in rapid degradation of the affected protein. The concepts of such conformational disease are illustrated by reference to cystic fibrosis, phenylketonuria and short-chain acyl-CoA dehydrogenase deficiency. Other cellular components such as chaperones and proteases, as well as environmental factors, may combine to modulate the phenotype of such disorders and this may open up new therapeutic approaches.. AB - Many disease-causing point mutations do not seriously compromise synthesis of the affected polypeptide but rather ...
The lipopeptide antibiotic friulimicin, produced by Actinoplanes friuliensis, is an effective drug against Gram-positive bacteria, such as methicillin-resistant Staphylococcus epidermidis and Staphylococcus aureus strains. Friulimicin consists of a cyclic peptide core of ten amino acids and an acyl residue linked to an exocyclic amino acid. The acyl residue is essential for antibiotic activity, varies in length from C13 to C15, and carries a characteristic double bond at position Δcis3. Sequencing of a DNA fragment adjacent to a previously described fragment encoding some of the friulimicin biosynthetic genes revealed several genes whose gene products resemble enzymes of lipid metabolism. One of these genes, lipB, encodes an acyl-CoA dehydrogenase homologue. To elucidate the function of the LipB protein, a lipB insertion mutant was generated and the friulimicin derivative (FR242) produced by the mutant was purified. FR242 had antibiotic activity lower than friulimicin in a bioassay. Gas chromatography
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.. ...
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 ...
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 ...
CP000667.PE136 Location/Qualifiers FT CDS complement(147749..148963) FT /codon_start=1 FT /transl_table=11 FT /locus_tag=Strop_0136 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_0136 FT /db_xref=EnsemblGenomes-Tr:ABP52621 FT /db_xref=GOA:A4X171 FT /db_xref=InterPro:IPR006089 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:A4X171 FT /protein_id=ABP52621.1 FT /translation=MAEFSLDLTEEQRDLRDWVHGFASEVVRPAAAEWDAREETPWPII FT QEAAKVGLYGFEFLATCWGDPSGLSLPVACEELFWGDSGIGLSIFGTGLAVAAIYGTGT FT PEQLMEWVPQCFGDLDSPAVAAFCTSEPEAGSDVGAMRTRAVYDEAADEWVLSGQKSYA FT TNGGIAGVHVVTASVDPELGSRGQAAFVVPPGTPGLAATRKLRKLGLRASHTADVFLDD FT ...
ACAD9 Full-Length MS Protein Standard (NP_054768), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. This gene encodes a member of the acyl-CoA dehydrogenase family. Members of this family of proteins localize to the mitochondria and catalyze the rate-limiting step in the beta-oxidation of fatty acyl-CoA. The encoded protein is specifically active toward palmitoyl-CoA and long-chain unsaturated substrates. Mutations in this gene cause acyl-CoA dehydrogenase family member type 9 deficiency. Alternate splicing results in multiple transcript variants.
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 ...
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
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.
224715 /locus_tag=OA238_c02230 /note=Domain of unknown function (DUF4189); Region: DUF4189; pfam13827 /db_xref=CDD:222402 gene complement(224805..226487) /locus_tag=OA238_c02240 /db_xref=GeneID:15089524 CDS complement(224805..226487) /locus_tag=OA238_c02240 /codon_start=1 /transl_table=11 /product=acyl-CoA dehydrogenase /protein_id=YP_007697952.1 /db_xref=GI:478176879 /db_xref=GeneID:15089524 /translation=MPRDAHDQNAKSTPVLPDLLATTAATIAPLRALLETAKDCVRDK VMVDGRASGALVEAEQTAAHGLAWLATYVEALAQMQVWAEKLLADSKFGEVEQLIHQI AFGEYLWQIYGGIPMNQGEILRLQDIGLTQDQMRIMMEPSVKALTQHANTQAARLRLV DLMQERSAEVTVGATGLDDELDMIREQFRRYAVEKVEPFAHEWHLKDELIPTSVIDEL AEMGVFGLTIPEEYGGLGLSKASMCVVSEELSRGYIGVGSLGTRTEIAAELIIAGGTE EQKQKWLPALASAEKLPTAVFTEPNTGSDLGALRARAVKDGDDYRVTGNKTWITHASR THVMTLLARTNPDSSDYKGLSMFLAEKTPGDDAHPFPTEGMTGGEIEVLGYRGMKEHE LAFDNFHVKGENLLGGEEGKGFKQLMETFESARIQTAARAIGVACSALDVAMQYAQDR KQFGKSLIEFPRVANKLAMMAVEIMIARQLTYFSAFEKDEGRRCDVEAGMAKLLGARV AWAAADNALQIHGGNGFALEYKVSRILCDARILNIFEGAAEIQAQVIARRIL ...
Our study has confirmed that the most important criterion for the detection of MCAD deficiency is the presence in the blood spot of octanoylcarnitine at a concentration , 0.3 μM (in this study , 0.38 μM). However, we have also shown that blood spot octanoylcarnitine concentrations are higher in neonates with MCAD deficiency and that there is an association between low octanoylcarnitine and low free carnitine. There are two possible explanations for the latter association. The first is that the volume of blood in the 6 mm disc was substantially less than 10 μl or that the elution was much less efficient for this group of blood spots. We consider this to be very unlikely; all the Guthrie cards that were received were made from approved brands of filter paper, all blood spots were inspected visually to make sure that the 6 mm disc was completely filled, and a standardised procedure was adopted for the elution step. The second and more likely explanation for the association is that these patients ...
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 …. ...
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
TY - JOUR. T1 - Genetic deficiency of short-chain acyl-coenzyme A dehydrogenase in cultured fibroblasts from a patient with muscle carnitine deficiency and severe skeletal muscle weakness. AU - Coates, P. M.. AU - Hale, D. E.. AU - Finocchiaro, G.. AU - Tanaka, K.. AU - Winter, S. C.. PY - 1988/1/1. Y1 - 1988/1/1. N2 - Genetic deficiency of short-chain acyl-coenzyme A (CoA) dehydrogenase activity was demonstrated in cultured fibroblasts from a 2-yr-old female whose early postnatal life was complicated by poor feeding, emesis, and failure to thrive. She demonstrated progressive skeletal muscle weakness and developmental delay. Her plasma total carnitine level (35 nmol/ml) was low-normal, but was esterified to an abnormal degree (55% vs. controls of , 10%). Her skeletal muscle total carnitine level was low (7.6 nmol/mg protein vs. controls of 14 ± 2 nmol/mg protein) and was 75% esterified. Mild lipid deposition was noted in type I muscle fibers. Fibroblasts from this patient had 50% of control ...
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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.
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?
Related Gene(s): ACADM, CFTR, DHCR7, DMD, FMR1, HBA1, HBA2, HBB, PAH, PMM2, SMN1. The high frequency pan-ethnic panel provides carrier screening for the following genetic disorders due to the relatively elevated carrier frequencies and high detection rates in most ethnic groups with severe, early onset clinical presentation: Alpha-thalassemia, beta-thalassemia, beta-globin-related hemoglobinopathies: HbC variant, sickle cell disease, congenital disorder of glycosylation: type Ia, cystic fibrosis, Duchenne muscular dystrophy/Becker muscular dystrophy, fragile x syndrome, medium chain acyl-CoA dehydrogenase deficiency, phenylalanine hydroxylase deficiency, Smith-Lemli-Opitz syndrome, and spinal muscular atrophy.. Although this testing can detect the majority of disease-causing pathogenic variants, a negative result does not eliminate the possibility that an individual is a carrier of a rare pathogenic variant that was not identified. Please refer to the residual risk table to determine the risk ...
Variant summary: ACADM c.449_452delCTGA (p.Thr150ArgfsX4) results in a premature termination codon, predicted to cause a truncation of the encoded protein or absence of the protein due to nonsense mediated decay, which are commonly known mechanisms for disease. The variant allele was found at a frequency of 2e-05 in 251336 control chromosomes (gnomAD). c.449_452delCTGA has been reported in the literature in compound heterozygous and homozygous individuals affected with Medium Chain Acyl-CoA Dehydrogenase Deficiency (Ensenauer_2005, Purevsuren_2009). These data indicate that the variant is very likely to be associated with disease. Three clinical diagnostic laboratories have submitted clinical-significance assessments for this variant to ClinVar after 2014 without evidence for independent evaluation. All laboratories classified the variant as pathogenic. Based on the evidence outlined above, the variant was classified as pathogenic ...
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 ...
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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] ...
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 ...
An isolated defect of respiratory chain complex I activity is a frequent biochemical abnormality in mitochondrial disorders. Despite intensive investigation in recent years, in most instances, the molecular basis underpinning complex I defects remains unknown. We report whole-exome sequencing of a single individual with severe, isolated complex I deficiency. This analysis, followed by filtering with a prioritization of mitochondrial proteins, led us to identify compound heterozygous mutations in ACAD9, which encodes a poorly understood member of the mitochondrial acyl-CoA dehydrogenase protein family. We demonstrated the pathogenic role of the ACAD9 variants by the correction of the complex I defect on expression of the wildtype ACAD9 protein in fibroblasts derived from affected individuals. ACAD9 screening of 120 additional complex I-defective index cases led us to identify two additional unrelated cases and a total of five pathogenic ACAD9 alleles.
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.
Dr. Bennett is professor of pathology and laboratory medicine at the University of Pennsylvania and director of the metabolic disease laboratory at The Childrens Hospital of Philadelphia. He also holds the Evelyn Willing Bromley Endowed Chair in Clinical Laboratories and Pathology at The Childrens Hospital of Philadelphia. The main focus of Dr. Bennetts research has been the investigation of inborn errors of mitochondrial energy metabolism with a special emphasis on disorders of fatty acid metabolism. He was among the first to describe the fatal clinical phenotype and the first to identify neonatal metabolite abnormalities in medium-chain acyl-CoA dehydrogenase (MCAD) deficiency. These observations led to the expansion of newborn screening by tandem mass spectrometry, in which most newborns are now screened for MCAD deficiency and a number of other inborn errors of metabolism. He is currently studying the hyperinsulinism associated with deficiency of short-chain L-3-hydroxyacyl-CoA ...
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 ...
TY - JOUR. T1 - Fibroblast Fatty-Acid Oxidation Flux Assays Stratify Risk in Newborns with Presumptive-Positive Results on Screening for Very-Long Chain Acyl-CoA Dehydrogenase Deficiency. AU - Olpin, Simon. AU - Clark, Shirley. AU - Dalley, Jane. AU - Andresen, Brage Storstein. AU - Croft, Joanne. AU - Scott, Camilla. AU - Khan, Aneal. AU - Kirk, Richard J.. AU - Sparks, Rebecca. AU - Chard, Marisa. AU - Chan, Alicia. AU - Glamuzina, Emma. AU - Bastin, Jean. AU - Manning, Nigel J.. AU - Pollitt, Rodney J.. PY - 2017. Y1 - 2017. U2 - 10.3390/ijns3010002. DO - 10.3390/ijns3010002. M3 - Journal article. VL - 3. JO - International Journal of Neonatal Screening. JF - International Journal of Neonatal Screening. SN - 2409-515X. IS - 1. M1 - 2. ER - ...
Free, official coding info for 2018 ICD-10-CM E71.311 - includes detailed rules, notes, synonyms, ICD-9-CM conversion, index and annotation crosswalks, DRG grouping and more.
ACADSB Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, 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 toxicity of this agent. Defects in ACADSB are the cause of short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD); also known as 2-methylbutyryl-CoA dehydrogenase deficiency or 2- methylbutyryl glycinuria. SBCADD is an autosomal recessive disorder and consists of a defect in catabolism of L-isoleucine which is characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine. Affected individuals have seizures and psychomotor delay as the main clinical features. Belongs to the acyl-CoA dehydrogenase family. Note: This description may include information from UniProtKB ...
Accepted name: acyl-CoA dehydrogenase (NADP+). Reaction: acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+. Other name(s): 2-enoyl-CoA reductase; dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate); enoyl coenzyme A reductase; crotonyl coenzyme A reductase; crotonyl-CoA reductase; acyl-CoA dehydrogenase (NADP). Systematic name: acyl-CoA:NADP+ 2-oxidoreductase. Comments: The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)].. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-07-3. References:. 1. Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335-341. [PMID: ...
6.. Fanin M, Anichini A, Cassandrini D, Fiorillo C, Scapolan S, Minetti C, Cassanello M, Donati MA, Siciliano G, DAmico A, Lilliu F, Bruno C, Angelini C (2012) Allelic and phenotypic heterogeneity in 49 Italian patients with the muscle form of CPT-II deficiency. Clin Genet 82:232-239. https://doi.org/10.1111/j.1399-0004.2011.01786.x ...
MCADD is inherited in an autosomal recessive manner, meaning an affected individual must inherit a mutated allele from both of their parents. ACADM is the gene involved, located at 1p31, with 12 exons and coding for a protein of 421 amino acids. There is a common mutation, rs77931234(C) (in dbSNP orientation), among Northern European Caucasians, which results in a lysine being replaced by a glutamic acid at position 304 of the protein (note: numbering may vary depending on reference). Other mutations have been identified more commonly since newborn screening has expanded the mutation spectrum. The 985A,G (rs77931234C) common mutation is present in the homozygous state in 80% of Caucasian individuals who presented clinically with MCADD and in 60% of the population identified by screening.Wikipedia ...
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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. ...
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 ...
The synthesis of a (fluorine-18) fluoroaryl estrogen in no-carrier-added form requires the use of ($\sp{18}$F) F$\sp-$. A great amount of effort has been made toward incorporation of ($\sp{18}$F) F$\sp-$onto an electron-rich aromatic ring, but none have found general application. Several strategies were explored for the synthesis of a (fluorine-18) fluoroaryl estrogen. The synthesis of 2- ($\sp{18}$F) fluoroestradiol (12) required the use of a trimethylammonium salt as a leaving group and a ketone as an activating group. Incorporation yields of fluorine-18 were low, between 10 and 20%, but reproducible. This allowed the testing of 2-($\sp{18}$F) fluoroestradiol in immature female rats. The only information that could be reliably taken from this study was that uptake of 12 was receptor mediated. In order to more accurately assess the ability of 12 to localize selectively in target tissue and resist metabolism, it must be administered to animals possessing SHBG ...
MalaCards based summary : Muscular Lipidosis, also known as lipid storage myopathy, is related to acyl-coa dehydrogenase, short-chain, deficiency of and carnitine deficiency, systemic primary. An important gene associated with Muscular Lipidosis is ACADS (Acyl-CoA Dehydrogenase Short Chain). Affiliated tissues include heart, skeletal muscle and kidney, and related phenotypes are Decreased viability and Decreased viability ...
LYS304GLU; In 9 patients with MCAD deficiency, Matsubara et al. [Lancet 335: 1589 (1990)] found an A-to-G transition which resulted in the substitution of lysine (AAA) by glutamic acid (GAA) at residue 329 of the enzyme (K329E). This A-to-G transition occurred at position 985 (G985) of the coding region of the MCAD gene ...
Parents of another patient-in-waiting were afraid to pursue an out-of-state job opportunity because they were uncertain about the quality of medical care that would be available for their child with potential medium-chain acyl-coenzyme A dehydrogenase deficiency (MCADD), a condition that prevents babies from being able to turn fat into energy. Without treatment, MCADD babies can experience seizures, extreme sleepiness or comas, and even die. And several parents decided either to give up a job or not return to a job in the hopes of keeping a closer eye on their children in case symptoms of the rare diseases did eventually surface ...
Next-day shipping cDNA ORF clones derived from ACADVL acyl-CoA dehydrogenase very long chain available at GenScript, starting from $99.00.
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"acyl-CoA dehydrogenase, very long chain". Strauss AW, Powell CK, Hale DE, Anderson MM, Ahuja A, Brackett JC, Sims HF (Nov 1995 ... 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: ... "Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency". American Journal of ...
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 ... "Entrez Gene: Acyl-CoA dehydrogenase, C-2 to C-3 short chain". Tein I, Elpeleg O, Ben-Zeev B, Korman SH, Lossos A, Lev D, Lerman ... As short-chain acyl-CoA dehydrogenase is involved in beta-oxidation, a deficiency in this enzyme is marked by an increased ... GeneReviews/NCBI/NIH/UW entry on Short-Chain Acyl-CoA Dehydrogenase Deficiency Human ACADS genome location and ACADS gene ...
"Very long-chain acyl-CoA dehydrogenase deficiency". Genetics Home Reference, National Institutes of Health. Retrieved 5 January ...
"Multiple acyl-CoA dehydrogenase deficiency". Orphanet. INSERM and the European Commission. Retrieved 30 August 2018. "Glutaric ... "Highly efficient ketone body treatment in multiple acyl-CoA dehydrogenase deficiency-related leukodystrophy". Pediatr Res. 77 ( ... L-3-hydroxybutyrate treatment of multiple acyl-CoA dehydrogenase deficiency (MADD)". The Lancet. 361 (9367): 1433-5. doi: ... while the ETFDH gene encodes the enzyme electron transfer flavoprotein dehydrogenase. When one of these enzymes is defective or ...
"Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase". Biochemical Society ... A crystal structure of the complex of one of its interactors, medium-chain acyl-CoA dehydrogenase (MCAD; gene name ACADM) has ... Crane FL, Beinert H (September 1954). "A Link Between Fatty Acyl CoA Dehydrogenase and Cytochrome C: A New Flavin Enzyme". ... Defects in either of the ETF subunits or ETFDH cause multiple acyl CoA dehydrogenase deficiency (OMIM # 231680), earlier called ...
"Long-Chain Acyl CoA Dehydrogenase Deficiency: Background, Pathophysiology, Epidemiology". eMedicine. 24 March 2016. Retrieved ... CS1 maint: discouraged parameter (link) "HADHA hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase ( ... HYDROXYACYL-CoA DEHYDROGENASE/3-KETOACYL-CoA THIOLASE/ENOYL-CoA HYDRATASE, ALPHA SUBUNIT; HADHA". omim.org. Retrieved 5 ... Avoiding factors that might precipitate condition Glucose Low fat/high carbohydrate nutrition Long-chain acyl-CoA dehydrogenase ...
Roth, Karl S. (2013-12-19). "Medium-Chain Acyl-CoA Dehydrogenase Deficiency". Medscape. Beermann, C.; Jelinek, J.; Reinecker, T ... The cytosolic acetyl-CoA is carboxylated by acetyl CoA carboxylase into malonyl-CoA, the first committed step in the synthesis ... Pyruvate is then decarboxylated to form acetyl-CoA in the mitochondrion. However, this acetyl CoA needs to be transported into ... To obtain cytosolic acetyl-CoA, citrate (produced by the condensation of acetyl-CoA with oxaloacetate) is removed from the ...
Acyl-CoA dehydrogenase family, member 10 is a protein that in humans is encoded by the ACAD10 gene. This gene encodes a member ... "Entrez Gene: Acyl-CoA dehydrogenase family, member 10". Bian L, Hanson RL, Muller YL, Ma L, Kobes S, Knowler WC, Bogardus C, ... "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 ...
Acyl-CoA dehydrogenases are enzymes that catalyze formation of a double bond between C2 (α) and C3 (β) of the acyl-CoA ... Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718-25 ... Plant stearoyl-acyl-carrier-protein desaturase (EC 1.14.19.1), an enzyme that catalyzes the introduction of a double bond at ... Family 1 includes Stearoyl-CoA desaturase-1 (SCD) (EC 1.14.19.1). Family 2 is composed of: Bacterial fatty acid desaturases. ...
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 ...
"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. ...
The inhibition of one in particular, butyryl CoA dehydrogenase (a short-chain acyl-CoA dehydrogenase), causes β-oxidation to ... MCPA also inhibits the dehydrogenation of a number of Acyl-CoA dehydrogenases. ... MCPA forms non-metabolizable esters with coenzyme A (CoA) and carnitine, causing a decrease in their bioavailability and ... it also limits Acyl and carnitine cofactors, which are instrumental in the oxidation of large fatty acids. Hypoglycin A ...
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. doi:10.1016/S0021- ... 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. ...
... 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 ... "Entrez Gene: Acyl-CoA dehydrogenase, long chain". Kurtz DM, Tolwani RJ, Wood PA (May 1998). "Structural characterization of the ...
"Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain". Biochemical and ... Acyl-CoA dehydrogenase family member 9, mitochondrial is an enzyme that in humans is encoded by the ACAD9 gene. Mitochondrial ... "Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids". The Journal ... "Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I". Cell Metabolism. 12 (3): 283- ...
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 ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
Also, it inhibits acyl-CoA dehydrogenases, so that only unsaturated fatty acids can be fully oxidized. Fatty acids accumulate ...
"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 ...
Medium chain acyl-CoA dehydrogenase deficiency (MCADD), which had been implicated in several cases of sudden infant death ... Prior to its inclusion in newborn screening, short-chain acyl-CoA dehydrogenase deficiency (SCADD) was thought to be life- ... "Homozygosity for a severe novel medium-chain acyl-CoA dehydrogenase (MCAD) mutation IVS3-1G>C that leads to introduction of a ... "Prenatal diagnosis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in a family with a previous fatal case of sudden ...
... is broken down into shorter-chain fatty acids in the human liver by the long-chain acyl CoA dehydrogenase enzyme. ... Erucic acid is produced by elongation of oleic acid via oleoyl-coenzyme A and malonyl-CoA. ...
caiA RNAs are found upstream of genes whose protein products function as acyl CoA dehydrogenases, although in one case the ... annotated substrate is butyryl-CoA. caiA RNAs might regulate these genes (i.e. function as cis-regulatory elements), but it is ...
... is not an appropriate substrate for acyl CoA dehydrogenase, or enoyl CoA hydratase: If the acyl CoA contains a cis-Δ3 bond, ... Cn-acyl-CoA + FAD + NAD+ + H 2O + CoA → Cn-2-acyl-CoA + FADH 2 + NADH + H+ + acetyl-CoA Free fatty acids cannot penetrate any ... The final cycle produces two separate acetyl CoAs, instead of one acyl CoA and one acetyl CoA. For every cycle, the Acyl CoA ... This is catalyzed by acyl CoA dehydrogenase to produce trans-delta 2-enoyl CoA. It uses FAD as an electron acceptor and it is ...
FAD accepts two protons and two electrons to form FADH2 under the catalysis of acyl-CoA dehydrogenase. The mechanism involves ... In the dehydrogenation reaction of acyl-CoA to form enoyl-CoA, ... formation of acyl-CoA β-radical that undergo elimination to ... form the enoyl-CoA product (See Fig. 3). Ansylen, E. V.; Dougherty, D. A. Modern Physical Organic Chemistry. p. 586, ISBN 978-1 ...
"Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA ... Mutations in ACAD8 have been linked to isobutyryl-CoA dehydrogenase deficiency. Most patients with isobutyryl-CoA dehydrogenase ... "Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA ... The protein encoded by ACAD8 is a mitochondrial protein belongs to the acyl-CoA dehydrogenase family of enzymes, which function ...
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 ...
... a gene Medium-chain acyl-CoA dehydrogenase, an enzyme used in lipid metabolism Medium-chain acyl-coenzyme A dehydrogenase ...
... the upper lip Mediastinal endodermal sinus tumors Mediastinal syndrome Mediterranean fever Medium-chain Acyl-CoA dehydrogenase ... Multiple p Multiple acyl-CoA deficiency Multiple carboxylase deficiency, biotin responsive Multiple carboxylase deficiency, ... mixed Müllerian tumor Malignant paroxysmal ventricular tachycardia Mallory-Weiss syndrome Malonic aciduria Malonyl-CoA ... disorder Mal de debarquement Malakoplakia Malaria Male pseudohermaphroditism due to 17-beta-hydroxysteroid dehydrogenase ...
... and medium-chain acyl-CoA dehydrogenase (MCAD). ATGL deficient mice administered pirinixic acid demonstrated reduced cardiac ...
It is flanked by Ras-related protein Rab-43 and several pseudogenes and on the opposite strand Acyl CoA dehydrogenase family ...
Dihydroorotate dehydrogenase. *Coproporphyrinogen III oxidase. *Protoporphyrinogen oxidase. *Bilirubin oxidase. *Acyl-CoA ...
ACSF3: encoding enzyme Acyl-CoA synthetase family member 3. *ACSM2B: encoding enzyme Acyl-coenzyme A synthetase ACSM2B, ... PDPR: encoding protein Pyruvate dehydrogenase phosphatase regulatory subunit. *PKDTS: Polycystic kidney disease, infantile ... ACSM3: encoding enzyme Acyl-coenzyme A synthetase ACSM3, mitochondrial 2. *ADHD1: Attention deficit-hyperactivity disorder, ...
transferase activity, transferring acyl groups. • 3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C- ... HADHB, ECHB, MSTP029, MTPB, TP-BETA, hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional ... transferring acyl groups other than amino-acyl groups. • enoyl-CoA hydratase activity. • long-chain-3-hydroxyacyl-CoA ... The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons ...
"Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling". 》The Biochemical Journal》 323 ... 효소의 이름은 보통 효소의 기질이나 효소가 촉매하는 화학 반응에서 유래된 단어 끝에 접미사 "-에이스(-ase)"를 붙여서 짓는다.[2] 락테이스(lactase), 알코올 탈수소효소(alcohol dehydrogenase), ... "The discovery and development of HMG-CoA reductase inhibitors" (PDF). 》J. Lipid Res.》 33 (11): 1569-82. PMID 1464741 ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
Pyruvate is oxidized to acetyl-CoA and CO2 by the pyruvate dehydrogenase complex (PDC). The PDC contains multiple copies of ... When oxygen is present, acetyl-CoA is produced from the pyruvate molecules created from glycolysis. Once acetyl-CoA is formed, ... Out of the cytoplasm it goes into the Krebs cycle with the acetyl CoA. It then mixes with CO2 and makes 2 ATP, NADH, and FADH. ... The citric acid cycle is an 8-step process involving 18 different enzymes and co-enzymes.[6] During the cycle, acetyl-CoA (2 ...
Fatty acyl CoA dehydrogenase requires FAD in fatty acid oxidation. *FAD is required to convert retinol (vitamin A) to retinoic ... and branched-chain amino acids requires FAD in the shared E3 portion of their respective dehydrogenase complexes ... acid via cytosolic retinal dehydrogenase. *Synthesis of an active form of folate (5-methyltetrahydrofolate) from 5,10- ...
isovaleryl-CoA dehydrogenase Ja 1.3.99.13 long-chain-acyl-CoA dehydrogenase Ja ... oxoglutarate dehydrogenase (succinyl-transferring) Ja 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl- ... L-iditol 2-dehydrogenase Ja 1.1.1.15 D-iditol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-sorbose + NADH + H+ D-iditol 2- ... D-arabitol 4-dehydrogenase 1.1.1.12 L-arabitol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. L-xylulose + NADH + H+ L-arabitol ...
Dor warrt denn Acyl-CoA for an Carnitin andockt un dör de Binnenmembran dörslüüst un dor denn in Acetyl-CoA umwannelt. In den ... En sunnerlichen Enzymkomplex (Pyruvat-Dehydrogenase) hölpt denn dor to, dat Pyruvat up to spleten un in Acetyl-CoA um to ... Anners kann Acetyl-CoA ok tostanne brocht weern dör den Afbo vun Fettsüer (β-Oxidation). Bi Deerter passeert dat ok in de ... Citratcyklus warrt ut dat Acetyl-CoA de gröttste Deel vun de Reduktschoonsäquivalente (NADH+H+, FADH2) herstellt, de denn ...
Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase. „J. Biol. Chem.". 258 (2), s. 1066-76, 1983. PMID: ... Ikeda Y, Dabrowski C, Tanaka K. Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria ... Alternative NAD(P)H dehydrogenases of plant mitochondria. „Annual review of plant biology". 55, s. 23-39, 2004. DOI: 10.1146/ ... Dervartanian DV, Veeger C.. Studies on succinate dehydrogenase. I. Spectral properties of the purified enzyme and formation of ...
... and the regulation of pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl CoA. Transferases are also utilized ... Transfer of acyl groups or acyl groups that become alkyl groups during the process of being transferred are key aspects of EC ... Succinyl-CoA:3-ketoacid CoA transferase deficiency (or SCOT deficiency) leads to a buildup of ketones. Ketones are created upon ... "Succinyl-CoA:3-ketoacid CoA transferase deficiency". Genetics Home Reference. National Institute of Health. Retrieved 4 ...
... namely acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and thiolase. The cycle produces a new ... Fatty acids are first converted to acyl-CoA. Acyl-CoA is then degraded in a four-step cycle of dehydrogenation, hydration, ... The cytosolic acetyl-CoA can also condense with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) which is the ... Acetyl-CoA can be carboxylated in the cytosol by acetyl-CoA carboxylase, giving rise to malonyl-CoA, a substrate required for ...
to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer. • citrate (Si)-synthase activity ... The enzyme is inhibited by high ratios of ATP:ADP, acetyl-CoA:CoA, and NADH:NAD, as high concentrations of ATP, acetyl-CoA, and ... This induces the enzyme to change its conformation, and creates a binding site for the acetyl-CoA. Only when this citroyl-CoA ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
... is produced which is a building block for new fatty acids and can inhibit the transfer of the fatty acyl group from acyl CoA to ... Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to ... The carboxyl group is transferred from biotin to acetyl CoA to form malonyl CoA in the second reaction, which is catalyzed by ... Malonyl-CoA decarboxylase. References[edit]. *^ a b c Tong L (August 2005). "Acetyl-coenzyme A carboxylase: crucial metabolic ...
Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". J. Biol. Chem. 258 (2): 1066-76. PMID 6401712. ... "Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. ... as it accepts electrons from multiple acetyl-CoA dehydrogenases.[31][32] In plants, ETF-Q oxidoreductase is also important in ... Competitive inhibitors of succinate dehydrogenase (complex II).[91]. Antimycin A Piscicide Complex III Binds to the Qi site of ...
Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". 《J. Biol. Chem.》 258 (2): 1066-76. PMID 6401712. 29 ... "Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. ... 포유류에서 ETF:Q 산화환원효소 대사 경로는 여러 아실-CoA 탈수소효소로부터 전자를 받아들일 수 있기 때문에 지방산의 β 산화와 아미노산과 콜린의 이화작용에서 중요하다.[30][31] 식물에서 ETF:Q 산화환원효소는 ... 예를 들어, 식물에는 미토콘드리아 기질 쪽이 아닌 막 사이 공간 쪽에서 NADH를 산화시키는 외부 NAD(P)H 탈수소효소(external NAD(P)H dehydrogenase)가 있으며, 전자를 유비퀴논 풀에 전달한다.[41 ...
Acyl-CoA → Lysophosphatidic acid + CoA. Glycerol-1-phosphatase removes the phosphate group of glycerol 3-phosphate to generate ... Glycerol-3-phosphate dehydrogenases are located both in the cytosol and the intermembrane face of mitochondrial inner membrane ... and another acyl group is then added on the sn-2 position making phosphatidic acids. ... with glycerol-3-phosphate dehydrogenase. DHAP and thus glycerol 3-phosphate is also possible to be synthesized from amino acids ...
3-hydroxyacyl-CoA dehydrogenase. *3-hydroxybutyryl-CoA dehydrogenase. *Alcohol dehydrogenase. *Aldo-keto reductase *1A1 ... 3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ ⇌. {\displaystyle \rightleftharpoons }. 3-oxoacyl-[acyl-carrier-protein] + ... Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP ... In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction ...
3-Hydroxybutyryl-CoA dehydrogenase. *Branched-chain amino acid aminotransferase. *Branched-chain alpha-keto acid dehydrogenase ... Glutamine is formed if an ammonium ion attacks the acyl-phosphate intermediate, while glutamate is remade if water attacks the ... Methylglutaconyl-CoA hydratase. (See Template:Leucine metabolism in humans - this diagram does not include the pathway for β- ... Ammonium binds strongly to GS only if the acyl-phosphate intermediate is present. Ammonium, rather than ammonia, binds to GS ...
Dozens of ATP equivalents are generated by the beta-oxidation of a single long acyl chain.[20] The acetyl-CoA produced by beta- ... In the mitochondrion, pyruvate is oxidized by the pyruvate dehydrogenase complex to the acetyl group, which is fully oxidized ... In the presence of air and various cofactors and enzymes, fatty acids are degraded to acetyl-CoA. The pathway is called beta- ... Another malate dehydrogenase-catalyzed reaction occurs in the opposite direction, producing oxaloacetate and NADH from the ...
Acetyl-coA inhibits pyruvate dehydrogenase, while succinyl-CoA inhibits alpha-ketoglutarate dehydrogenase and citrate synthase ... Acyl-CoA is oxidized to trans-Enoyl-CoA while FAD is reduced to FADH2, which is similar to the oxidation of succinate to ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... Succinyl-CoA + GDP + Pi Succinate + CoA-SH + GTP Succinyl-CoA synthetase substrate-level. phosphorylation or ADP→ATP instead of ...
The reaction is catalysed by the enzymes pyruvate decarboxylase and alcohol dehydrogenase.[13] ... Acyl-CoA Fatty. acids Glyco-. sphingolipids Sphingolipids Waxes Polyunsaturated. fatty acids Neurotransmitters. & thyroid ...
In higher eukaryotes, δ-aminolevulinic acid, the key precursor to porphyrins, is biosynthesized from glycine and succinyl-CoA ... Glyoxylate is then oxidized by hepatic lactate dehydrogenase to oxalate in an NAD+-dependent reaction.[26] ... The acyl radical is glycyl. Contents. *1 History and etymology. *2 Production ...
Elovson J, Vagelos PR (1968). „Acyl carrier protein. X. Acyl carrier protein synthetase". J. Biol. Chem. 243 (13): 3603-11. ... Koenzim A (CoA, CoASH, HSCoA) je koenzim, poznat po svojoj ulozi u sintezi i oksidaciji masnih kiselina, i oksidaciji piruvata ... phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase". J. Biol. Chem. 285 (3): 1627-33. PMC ... acetil-CoA) kao supstrat.[5] On se sastoji od cistamina, pantotenata, i adenozin-trifosfata. ...
ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. Lipids are important in making up the cell membrane. ... For example, alcohol dehydrogenase which catalyses the transfer of a hydride ion from ethanol to NAD+ interacts with the ... The resulting hydroxide anion nucleophilically attacks the acyl-enzyme complex to form a second tetrahedral oxyanion ... Cyclohexanedione targets the Acetyl-CoA carboxylase which is involved in the first step of fat synthesis: ...
"Medium-Chain Acyl-CoA Dehydrogenase Deficiency". Medscape.. *^ Beermann, C.; Jelinek, J.; Reinecker, T.; Hauenschild, A.; Boehm ... The cytosolic acetyl-CoA is carboxylated by acetyl CoA carboxylase into malonyl-CoA, the first committed step in the synthesis ... To obtain cytosolic acetyl-CoA, citrate (produced by the condensation of acetyl-CoA with oxaloacetate) is removed from the ... Pyruvate is then decarboxylated to form acetyl-CoA in the mitochondrion. However, this acetyl CoA needs to be transported into ...
Dihydroorotate dehydrogenase. *Coproporphyrinogen III oxidase. *Protoporphyrinogen oxidase. *Bilirubin oxidase. *Acyl-CoA ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... Succinate dehydrogenase cytochrome b560 subunit, mitochondrial. Pfam PF01127 4. SdhD. DHSD_HUMAN. Succinate dehydrogenase [ ...
3-Hydroxybutyryl-CoA dehydrogenase. *Branched-chain amino acid aminotransferase. *Branched-chain alpha-keto acid dehydrogenase ... This is followed by Cβ-Cγ bond cleavage to generate an acyl-enzyme intermediate together with a tautomerized Ala-PLP adduct. ... Methylglutaconyl-CoA hydratase. (See Template:Leucine metabolism in humans - this diagram does not include the pathway for β- ... tryptophan catabolic process to acetyl-CoA. • L-kynurenine catabolic process. • tryptophan catabolic process. • tryptophan ...
Although these enzymes catalyze similar reactions and share a similar acyl-CoA dehydrogenase fold, the FMN-dependent enzyme is ...
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) Biology portal. ... crystal structure of human very-long-chain acyl-CoA dehydrogenase". The Journal of Biological Chemistry. 283 (14): 9435-43. doi ... I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase". The Journal of Biological Chemistry. 267 (2 ...
Acyl CoA Beta oxidation Thorpe, C.; Kim, J. J. (June 1995). "Structure and Mechanism of Action of the Acyl-CoA Dehydrogenases ... "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 ...
Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is a condition that prevents the body from converting certain fats to ... medlineplus.gov/genetics/condition/medium-chain-acyl-coa-dehydrogenase-deficiency/ Medium-chain acyl-CoA dehydrogenase ... Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is a condition that prevents the body from converting certain fats to ... This gene provides instructions for making an enzyme called medium-chain acyl-CoA dehydrogenase, which is required to break ...
Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a condition that prevents the body from converting certain fats into ... medlineplus.gov/genetics/condition/short-chain-acyl-coa-dehydrogenase-deficiency/ Short-chain acyl-CoA dehydrogenase deficiency ... Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ... Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a condition that prevents the body from converting certain fats into ...
Comment on: "Multiple acylCoA dehydrogenase deficiency in elderly carriers". *Yılmaz Yıldız. ORCID: orcid.org/0000-0001-9076- ... Yıldız, Y., Tokatlı, A. Comment on: "Multiple acylCoA dehydrogenase deficiency in elderly carriers". J Neurol (2020). https:// ... Grunert SC (2014) Clinical and genetical heterogeneity of late-onset multiple acyl-coenzyme A dehydrogenase deficiency. ... Multiple acyl-COA dehydrogenase deficiency in elderly carriers. J Neurol. https://doi.org/10.1007/s00415-020-09729-z ...
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.
VLCAD; Very long chain acyl-CoA dehydrogenase. COG1960. Location:80 → 451. CaiA; Acyl-CoA dehydrogenase related to the ... VLCAD; Very long chain acyl-CoA dehydrogenase. COG1960. Location:125 → 496. CaiA; Acyl-CoA dehydrogenase related to the ... VLCAD; Very long chain acyl-CoA dehydrogenase. COG1960. Location:26 → 397. CaiA; Acyl-CoA dehydrogenase related to the ... VLCAD; Very long chain acyl-CoA dehydrogenase. COG1960. Location:102 → 473. CaiA; Acyl-CoA dehydrogenase related to the ...
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 ...
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 ...
Compare acyl-CoA dehydrogenase family member 9 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, ... acyl-CoA dehydrogenase family member 9 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a widely used application ... Your search returned 13 acyl-CoA dehydrogenase family member 9 ELISA ELISA Kit across 2 suppliers. ...
Acyl CoA dehydrogenase is the enzyme used to catalyze the first step of β-oxidation in Fatty acid metabolism. ... Medium-chain acyl-coenzyme A dehydrogenase deficiency ("MCAD") ACADS. C-2 to C-3 short chain. Short-chain acyl-coenzyme A ... Acyl-CoA+Dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) ... Retrieved from "https://www.wikidoc.org/index.php?title=Acyl_CoA_dehydrogenase&oldid=264418" ...
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 ...
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 Were all in this for good.. ...
Multiple acyl-CoA dehydrogenase deficiency (MADD) is a life-threatening, ultrarare inborn error of metabolism. Case reports ... Multiple acyl-CoA dehydrogenase deficiency (MADD; also known as glutaric aciduria type II, OMIM 231680) is an ultrarare (i.e ... Efficacy and safety of D,L-3-hydroxybutyrate (D,L-3-HB) treatment in multiple acyl-CoA dehydrogenase deficiency. *Willemijn J. ... Multiple acyl-CoA dehydrogenase deficiency (MADD) is a life-threatening, ultrarare inborn error of metabolism. Case reports ...
3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA), 1beta-(2-propanoyl-CoA)-3a ... propanoyl-CoA ester side chains of 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene-20-carboxyl-CoA ... H-7a-beta-methylhexahydro-4-indanone (indanone-CoA ester), hexahydroindanone and pregenenone (PubMed:22045806, PubMed:23560677 ... IPR009100 AcylCoA_DH/oxidase_NM_dom. Pfami. View protein in Pfam. PF00441 Acyl-CoA_dh_1, 1 hit. PF02771 Acyl-CoA_dh_N, 1 hit ...
Handbook of Genetic Counseling/Short Chain Acyl-CoA Dehydrogenase (SCAD). From Wikibooks, open books for an open world ... lab results: skeletal muscle carnitine low, deficiency of skeletal muscle mitochondrial short-chain acyl-CoA (butyryl-CoA) ... during which time the long and medium acyl-CoA dehydrogenases are unable to compensate for the lack of SCAD ... Retrieved from "https://en.wikibooks.org/w/index.php?title=Handbook_of_Genetic_Counseling/Short_Chain_Acyl-CoA_Dehydrogenase_( ...
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 ...
Very long-chain-specific acyl-CoA dehydrogenase, mitochondrialImported. ,p>Information which has been imported from another ... tr,J3QKU9,J3QKU9_HUMAN Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial (Fragment) OS=Homo sapiens OX=9606 GN= ... Very long-chain specific acyl-CoA dehydrogenase, mitochondrial, VLCAD, EC 1.3.8.9 ... IPR013786, AcylCoA_DH/ox_N. IPR037069, AcylCoA_DH/ox_N_sf. IPR009100, AcylCoA_DH/oxidase_NM_dom. ...
Acyl-CoA dehydrogenases catalyze the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-eno… ... Mammalian Co-A dehydrogenases (EC:1.3.99.3) are enzymes that catalyse the first step in each cycle of beta-oxidation in ...
Late-onset multiple acyl-CoA dehydrogenase deficiency (MADD) with electron transfer flavoprotein dehydrogenase (ETFDH) gene ... Multiple Acyl Coenzyme A Dehydrogenase Deficiency/diagnostic imaging. *Multiple Acyl Coenzyme A Dehydrogenase Deficiency/ ... Multiple Acyl Coenzyme A Dehydrogenase Deficiency/metabolism. *Multiple Acyl Coenzyme A Dehydrogenase Deficiency/ ... Clinical heterogeneity; ETFDH; Late-onset multiple acyl-CoA dehydrogenase deficiency; Lipid storage myopathy; Variants ...
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), ...
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 ...
N2 - PURPOSE: To evaluate the Dutch newborn screening (NBS) for Medium-Chain Acyl-CoA Dehydrogenase (MCAD) deficiency since ... AB - PURPOSE: To evaluate the Dutch newborn screening (NBS) for Medium-Chain Acyl-CoA Dehydrogenase (MCAD) deficiency since ... abstract = "PURPOSE: To evaluate the Dutch newborn screening (NBS) for Medium-Chain Acyl-CoA Dehydrogenase (MCAD) deficiency ... A Nationwide Retrospective Observational Study Of Population Newborn Screening For Medium-Chain Acyl-CoA Dehydrogenase (MCAD) ...
... ... is the substrate for histone butyrylation and its abundance is regulated by acyl-CoA dehydrogenase short chain (ACADS). The ... Thus, we hypothesized that the fatty acid intermediate, butyryl-CoA, ... signifying that fatty acid synthesis from carbohydrates substitutes for dietary fat as a source of butyryl-CoA. A high-fat diet ...
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 ...
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 ...
"Acyl-CoA Dehydrogenase, Long-Chain" by people in this website by year, and whether "Acyl-CoA Dehydrogenase, Long-Chain" was a ... "Acyl-CoA Dehydrogenase, Long-Chain" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ... Long-term correction of very long-chain acyl-coA dehydrogenase deficiency in mice using AAV9 gene therapy. Mol Ther. 2012 Jun; ... A near-miss: very long chain acyl-CoA dehydrogenase deficiency with normal primary markers in the initial well-timed newborn ...
  • Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is a condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). (medlineplus.gov)
  • The natural history of medium-chain acyl CoA dehydrogenase deficiency in the Netherlands: clinical presentation and outcome. (medlineplus.gov)
  • Dezateux C. Newborn screening for medium chain acyl-CoA dehydrogenase deficiency: evaluating the effects on outcome. (medlineplus.gov)
  • Spectrum of medium-chain acyl-CoA dehydrogenase deficiency detected by newborn screening. (medlineplus.gov)
  • Joy P, Black C, Rocca A, Haas M, Wilcken B. Neuropsychological functioning in children with medium chain acyl coenzyme a dehydrogenase deficiency (MCADD): the impact of early diagnosis and screening on outcome. (medlineplus.gov)
  • Biochemical, molecular, and clinical characteristics of children with short chain acyl-CoA dehydrogenase deficiency detected by newborn screening in California. (medlineplus.gov)
  • Jethva R, Bennett MJ, Vockley J. Short-chain acyl-coenzyme A dehydrogenase deficiency. (medlineplus.gov)
  • The most common fatty acid oxidation disorder, medium chain acyl-CoA dehydrogenase deficiency (MCADD), has become the focal point for the adoption of tandem mass spectrometry to detect it and related inborn errors of metabolism. (cdc.gov)
  • Despite the increase in screening, understanding of the nat dehydrogenase deficiency" or "tandem mass spectrometry" to ural history of unscreened MCADD remains limited.1,3,4 gether with "newborn screening. (cdc.gov)
  • Grunert SC (2014) Clinical and genetical heterogeneity of late-onset multiple acyl-coenzyme A dehydrogenase deficiency. (springer.com)
  • Antozzi C, Garavaglia B, Mora M, Rimoldi M, Morandi L, Ursino E, DiDonato S (1994) Late-onset riboflavin-responsive myopathy with combined multiple acyl coenzyme A dehydrogenase and respiratory chain deficiency. (springer.com)
  • Olsen RK, Andresen BS, Christensen E, Bross P, Skovby F, Gregersen N (2003) Clear relationship between ETF/ETFDH genotype and phenotype in patients with multiple acyl-CoA dehydrogenation deficiency. (springer.com)
  • One potential hotspot ACADVL mutation in Chinese patients with very-long-chain acyl-coenzyme A dehydrogenase deficiency. (nih.gov)
  • Analysis of ACADVL gene variations among nine neonates with very long chain acyl-coA dehydrogenase deficiency]. (nih.gov)
  • The diagnostic challenge in very-long chain acyl-CoA dehydrogenase deficiency (VLCADD). (nih.gov)
  • Sequencing of the ACADVL gene revealed that all individuals with activities below 24% were true Very long-chain acyl-CoA dehydrogenase deficiency (VLCADD) patients, individuals with residual activities between 24 and 27% carried either one or two mutations. (nih.gov)
  • Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: iden tification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. (thefreedictionary.com)
  • As a newborn-screening assay, MS/MS is not merely a method for detecting medium-chain acyl-CoA dehydrogenase (MCAD) deficiency (7), nor is it simply an improved method for accurate neonatal detection of PKU with a false-positive rate 10-fold lower than the best method previously available (8). (thefreedictionary.com)
  • When you share what it's like to have very long chain Acyl-CoA dehydrogenase deficiency through your profile, those stories and data appear here too. (patientslikeme.com)
  • Got a question about living with very long chain Acyl-CoA dehydrogenase deficiency? (patientslikeme.com)
  • Multiple acyl-CoA dehydrogenase deficiency (MADD) is a life-threatening, ultrarare inborn error of metabolism. (nature.com)
  • Clinical and biochemical characterization of short-chain acyl-coenzyme A dehydrogenase deficiency. (wikibooks.org)
  • Significant clinical heterogeneity with similar ETFDH genotype in three Chinese patients with late-onset multiple acyl-CoA dehydrogenase deficiency. (nih.gov)
  • Late-onset multiple acyl-CoA dehydrogenase deficiency (MADD) with electron transfer flavoprotein dehydrogenase (ETFDH) gene mutations is the most common lipid storage myopathy (LSM) in China. (nih.gov)
  • Background: Clinically, it is difficult to differentiate multiple acyl-CoA dehydrogenase deficiency (MADD) from immune-mediated necrotizing myopathy (IMNM) because they display similar symptoms. (thefreedictionary.com)
  • As Max discovers, he has medium chain acyl-CoA dehydrogenase deficiency, or MCADD. (thefreedictionary.com)
  • This infant has an autosomal recessive disorder described as multiple acyl-CoA dehydrogenase deficiency (MADD). (thefreedictionary.com)
  • Molecular and cellular pathology of very-long-chain acyl-CoA dehydrogenase deficiency. (thefreedictionary.com)
  • Conditions currently screened for in Wales are congenital hypothyroidism, cystic fibrosis, medium chain acyl-CoA dehydrogenase deficiency (MCADD), phenylketonuria and sickle cell disorders. (thefreedictionary.com)
  • Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency (MIM 201475) was first described in 1993. (thefreedictionary.com)
  • We were able to save about 15 babies with medium-chain acyl-CoA dehydrogenase or MCAD deficiency, a condition that prevents the body from converting certain fats in food to energy," Dr al-Rifai said, adding: "The early detection has allowed for early treatment. (thefreedictionary.com)
  • Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is the most common disorder associated with fatty acid oxidation. (dovepress.com)
  • abstract = "PURPOSE: To evaluate the Dutch newborn screening (NBS) for Medium-Chain Acyl-CoA Dehydrogenase (MCAD) deficiency since 2007.METHODS: A nationwide retrospective, observational study of clinical, laboratory and epidemiological parameters of patients with MCAD deficiency born between 2007-2015. (rug.nl)
  • A novel tandem mass spectrometry method for rapid confirmation of medium- and very long-chain acyl-CoA dehydrogenase deficiency in newborns. (labome.org)
  • This clear genotype-phenotype relationship is in sharp contrast to what has been observed in medium-chain acyl-CoA dehydrogenase deficiency, in which no correlation between genotype and phenotype can be established. (nih.gov)
  • Long-term correction of very long-chain acyl-coA dehydrogenase deficiency in mice using AAV9 gene therapy. (umassmed.edu)
  • A near-miss: very long chain acyl-CoA dehydrogenase deficiency with normal primary markers in the initial well-timed newborn screening specimen. (umassmed.edu)
  • Spiekerkoetter U, Sun B, Zytkovicz T, Wanders R, Strauss AW, Wendel U. MS/MS-based newborn and family screening detects asymptomatic patients with very-long-chain acyl-CoA dehydrogenase deficiency. (umassmed.edu)
  • 49 Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a rare genetic condition that prevents the body from converting certain fats (called short-chain fatty acids) into energy. (malacards.org)
  • These mutations lead to a shortage (deficiency) of an enzyme known as short-chain acyl-CoA dehydrogenase, which is involved in the breakdown of short-chain fatty acids. (malacards.org)
  • Acyl-Coa Dehydrogenase, Short-Chain, Deficiency of, also known as scad deficiency , is related to acyl-coa dehydrogenase, very long-chain, deficiency of and myopathy , and has symptoms including seizures , lethargy and failure to thrive . (malacards.org)
  • An important gene associated with Acyl-Coa Dehydrogenase, Short-Chain, Deficiency of is ACADS (Acyl-CoA Dehydrogenase Short Chain), and among its related pathways/superpathways are Fatty acid degradation and Fatty acid metabolism . (malacards.org)
  • 71 Acyl-CoA dehydrogenase short-chain deficiency: An inborn error of mitochondrial fatty acid beta-oxidation resulting in acute acidosis and muscle weakness in infants, and a form of lipid- storage myopathy in adults. (malacards.org)
  • A patient with very long chain acyl-CoA dehydrogenase (VLCAD) deficiency is reported. (bmj.com)
  • Very long chain acyl-CoA dehydrogenase (VLCAD) deficiency is a recently identified inborn error of a membrane bound mitochondrial enzyme. (bmj.com)
  • Very long-chain acyl-CoA dehydrogenase deficiency (VLCAD) is a rare, inherited (genetic) disease. (newbornscreening.on.ca)
  • Molecular test to confirm a diagnosis or identify carriers of medium chain acyl-CoA dehydrogenase (MCAD) deficiency for individuals with suggestive clinical and/or biochemical findings. (aruplab.com)
  • Acyl-Coa Dehydrogenase Deficiency is related to multiple acyl-coa dehydrogenase deficiency, severe neonatal type and multiple acyl-coa dehydrogenase deficiency, mild type . (malacards.org)
  • An important gene associated with Acyl-Coa Dehydrogenase Deficiency is ACADSB (Acyl-CoA Dehydrogenase Short/Branched Chain), and among its related pathways/superpathways are Metabolism and Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha) . (malacards.org)
  • A genetic disorder characterized by deficiency of the enzyme medium-chain acyl-coenzyme a dehydrogenase that metabolizes medium-chain fatty acids. (icd10data.com)
  • Very long-chain acyl-CoA dehydrogenase deficiency (VLCAD) is a rare genetic condition resulting from a mutation (change) in a person's DNA. (diseaseinfosearch.org)
  • Following organizations serve the condition "Very long chain acyl-CoA dehydrogenase deficiency" for support, advocacy or research. (diseaseinfosearch.org)
  • Clinical symptoms are consistent with acquired multiple acyl-CoA dehydrogenase deficiency (MADD). (usda.gov)
  • Recurrent ACADVL molecular findings in individuals with a positive newborn screen for very long chain acyl-coA dehydrogenase (VLCAD) deficiency in the United States. (semanticscholar.org)
  • Very long chain acyl-coA dehydrogenase deficiency (VLCADD) is an autosomal recessive inborn error of fatty acid oxidation detected by newborn screening (NBS). (semanticscholar.org)
  • Infants suspected to have very-long chain acyl-CoA dehydrogenase deficiency from newborn screening. (semanticscholar.org)
  • Positive newborn screen in a normal infant of a mother with asymptomatic very long-chain Acyl-CoA dehydrogenase deficiency. (semanticscholar.org)
  • Deficiency of 2-methylbutyryl-CoA dehydrogenase results in the inability to break down isoleucine causing an organic acidemia. (medicalhomeportal.org)
  • Short/Branched Chain Acyl-CoA Dehydrogenase Deficiency - Information for Professionals (STAR-G) ] More and more cases have been identified by neonatal screening, but they are not published given the benign clinical course. (medicalhomeportal.org)
  • Educate the family regarding signs, symptoms, and the need for urgent care when the infant becomes ill (see 2-Methylbutyryl CoA Dehydrogenase Deficiency - Information for Parents (STAR-G) for additional information). (medicalhomeportal.org)
  • Because short-chain acyl-CoA dehydrogenase deficiency (SCADD) (the result of an intramitochondrial defect in the beta-oxidation of fatty acids) may impair this form of energy production, metabolic crisis may result. (medicalhomeportal.org)
  • Educate the family regarding the benign clinical course of this condition (see Short-Chain Acyl-CoA Dehydrogenase Deficiency - Information for Parents (STAR-G) ). (medicalhomeportal.org)
  • Based on this proposition, the current study addressed the metabolic consequences of short-chain acyl-coenzyme A (CoA) dehydrogenase (SCAD) deficiency and dietary fat content on liver metabolism, including effects on tissue acylcarnitines, mitochondrial oxidative metabolism, hepatic pAMPK level, and genome-wide transcription. (biomedcentral.com)
  • A heterozygous missense mutation in adolescent-onset very long-chain acyl-CoA dehydrogenase deficiency with exercise-induced rhabdomyolysis. (semanticscholar.org)
  • Clinical features and mutations in seven Chinese patients with very long chain acyl-CoA dehydrogenase deficiency. (semanticscholar.org)
  • This infant may have Very Long Chain Acyl-oA Dehydrogenase deficiency. (archildrens.org)
  • In order to determine which are useful early diagnostic markers for medium-chain acyl-CoA dehydrogenase (MCAD) deficiency, we have analysed urine from an asymptomatic neonate. (elsevier.com)
  • The Invitae Very Long Chain Acyl-CoA Dehydrogenase Deficiency Test analyzes the ACADVL gene, which is associated with very long chain acyl-CoA dehydrogenase ( VLCAD ) deficiency. (invitae.com)
  • E71.312 is a billable ICD code used to specify a diagnosis of short chain acyl CoA dehydrogenase deficiency. (icd.codes)
  • Increased antioxidant response in medium-chain acyl-CoA dehydrogenase deficiency: does lipoic acid have a protective role? (regionh.dk)
  • BACKGROUND: Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency (MCADD) is the most frequent fatty acid oxidation (FAO) defect in humans. (regionh.dk)
  • The symptoms of the short chain acyl co enzyme A dehydrogenase which is referred as the SCADD deficiency are triggered by the periods of fasting or illness which includes the viral infections. (alldiseases.org)
  • This disorder includes the mutations in ACDAS gene which causes the short chain acyl co enzyme A dehydrogenase deficiency which is referred as the SCADD. (alldiseases.org)
  • Medium chain acyl-CoA dehydrogenase deficiency human genome epidemiology review. (cdc.gov)
  • More than 55 mutations in the ACADS gene have been found to cause short-chain acyl-CoA dehydrogenase (SCAD) deficiency. (nih.gov)
  • Mutations of ACADS gene associated with short-chain acyl-coenzyme A dehydrogenase deficiency. (nih.gov)
  • Mutations in this gene have been associated with short-chain acyl-CoA dehydrogenase (SCAD) deficiency. (genecards.org)
  • Population spectrum of ACADM genotypes correlated to biochemical phenotypes in newborn screening for medium-chain acyl-CoA dehydrogenase deficiency. (nih.gov)
  • Below you will find more information about Acyl-CoA dehydrogenase, very long chain, deficiency of from Medigest. (medigest.uk)
  • If you believe that you are suffering from any of the symptoms of Acyl-CoA dehydrogenase, very long chain, deficiency of it is important that you obtain an accurate diagnosis from a medical professional to ensure that you obtain the correct medication or treatment for your condition. (medigest.uk)
  • There are medical conditions that carry similar symptoms associated with Acyl-CoA dehydrogenase, very long chain, deficiency of and therefore the information provided by Medigest is offered as a guideline only and should never be used in preference to seeking professional medical advice. (medigest.uk)
  • The information relating to Acyl-CoA dehydrogenase, very long chain, deficiency of comes from a third party source and Medigest will not be held liable for any inaccuracies relating to the information shown. (medigest.uk)
  • Very-Long-Chain Acyl-CoA Dehydrogenase Deficiency (VLCADD) is a rare autosomal recessive condition in which the body fails to oxidize fatty acids because an enzyme is either missing or not functioning correctly. (medigest.uk)
  • A major component of the medical treatment of medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) deficiency is a diet that permits adequate nutrition and avoids any fasting period longer than 4-5 hours. (medscape.com)
  • Medium-chain acyl-CoA dehydrogenase deficiency in children with non- ketotic hypoglycemia and low carnitine levels. (medscape.com)
  • Newborn screening for medium chain acyl-CoA dehydrogenase deficiency in England: prevalence, predictive value and test validity based on 1.5 million screened babies. (medscape.com)
  • Medium-chain acyl-CoA dehydrogenase deficiency in Saudi Arabia: incidence, genotype, and preventive implications. (medscape.com)
  • Newborn screening for medium-chain acyl-CoA dehydrogenase deficiency: a global perspective. (medscape.com)
  • Medium-chain acyl-coA dehydrogenase deficiency: evaluation of genotype-phenotype correlation in patients detected by newborn screening. (medscape.com)
  • Deficiency in ETF dehydrogenase causes the human genetic disease multiple acyl-CoA dehydrogenase deficiency. (wikipedia.org)
  • Deficiency of ETF-QO results in a disorder known as glutaric acidemia type II (also known as MADD for multiple acyl-CoA dehydrogenase deficiency), in which there is an improper buildup of fats and proteins in the body. (wikipedia.org)
  • Very-Long-Chain Acyl-CoA Dehydrogenase (VLCAD) deficiency is a disorder of fatty acid oxidation included in the recommended uniform newborn screening (NBS) panel in the USA. (cdc.gov)
  • Medium-chain acyl-CoA dehydrogenase deficiency is an inherited condition characterized by inadequate levels of an enzyme required to break down medium-chain fatty acids. (nih.gov)
  • The five most commonly diagnosed conditions in the United States are 1) hearing loss, 2) primary congenital hypothyroidism, 3) cystic fibrosis, 4) sickle cell disease, and 5) medium-chain acyl-CoA dehydrogenase deficiency ( Table ) (3.6). (cdc.gov)
  • Coates PM, Hale DE, Stanley CA, Corkey BE, Cortner JA , Genetic deficiency of medium-chain acyl coenzyme A dehydrogenase: studies in cultured skin fibroblasts and peripheral mononuclear leukocytes. (coriell.org)
  • Newborn screening for medium- and very long-chain acyl-CoA dehydrogenase (MCAD and VLCAD, respectively) deficiency, using acylcarnitine profiling with tandem mass spectrometry, has increased the number of patients with fatty acid oxidation disorders due to the identification of additional milder, and so far silent, phenotypes. (cdc.gov)
  • To investigate the clinical and laboratory features of very long chain acyl-CoA dehydrogenase deficiency ( VLCADD ) and the correlations between its genotype and phenotype . (bvsalud.org)
  • Medium chain acyl-CoA dehydrogenase deficiency (MCADD) is a disorder of mitochondrial fatty acid oxidation and is one of the most common inborn errors of metabolism. (biomedcentral.com)
  • Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is the most common inherited disorder of the mitochondrial fatty acid oxidation, caused by mutations in the ACADM gene. (biomedcentral.com)
  • In the current study, the regression analysis was performed to identify short chain acyl-CoA dehydrogenase (SCAD) deficiency, medium chain acyl-CoA dehydrogenase (MCAD) deficiency, and very long chain acyl-CoA dehydrogenase (VLCAD) deficiency. (figshare.com)
  • Deficiency of very long-chain acyl-CoA dehydrogenase (VLCAD) is the most common disorder of mitochondrial β-oxidation of long-chain fatty acids. (springeropen.com)
  • Multiple acyl-CoA dehydrogenase deficiency (MADD), previously called glutaric aciduria type II, is a rare congenital metabolic disorder of fatty acids and amino acids oxidation, with recessive autosomal transmission. (biomedcentral.com)
  • Medium-chain acyl-CoA dehydrogenase deficiency , often known as MCAD deficiency or MCADD , is a disorder of fatty acid oxidation that impairs the body's ability to break down medium-chain fatty acids into acetyl-CoA . (wikipedia.org)
  • Acyl-CoA dehydrogenases (ACADs) are a class of enzymes that function to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells. (wikipedia.org)
  • The following reaction is the oxidation of the fatty acid by FAD to afford an α,β-unsaturated fatty acid thioester of Coenzyme A: ACADs can be categorized into three distinct groups based on their specificity for short-, medium-, or long-chain fatty acid acyl-CoA substrates. (wikipedia.org)
  • While different dehydrogenases target fatty acids of varying chain length, all types of ACADs are mechanistically similar. (wikipedia.org)
  • The medium chain acyl-CoA dehydrogenase (MCAD) is the best known structure of all ACADs, and is the most commonly deficient enzyme within the class that leads to metabolic disorders in animals. (wikipedia.org)
  • Thus, we hypothesized that the fatty acid intermediate, butyryl-CoA, is the substrate for histone butyrylation and its abundance is regulated by acyl-CoA dehydrogenase short chain (ACADS). (nih.gov)
  • 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. (biomedcentral.com)
  • Acads encodes short-chain acyl-CoA dehydrogenase (SCAD), a member of the family of four enzymes that catalyzes the first of four sequential steps in the mitochondrial fatty acid oxidation spiral which produces acetyl-CoA for the tricarboxylic acid cycle. (biomedcentral.com)
  • Previously we reported that mice with a global, genetic inactivation of the gene encoding short-chain acyl-CoA dehydrogenase ( Acads−/− ) shift consumption away from fat and toward carbohydrate when offered a choice between macronutrient-rich diets [ 1 ]. (biomedcentral.com)
  • The ACADS gene provides instructions for making an enzyme called short-chain acyl-CoA dehydrogenase (SCAD). (nih.gov)
  • ACADS (Acyl-CoA Dehydrogenase Short Chain) is a Protein Coding gene. (genecards.org)
  • MCAD can bind to a rather broad range of chain-lengths in the acyl-CoA substrate, however studies show that its specificity tends to target octanoyl-CoA (C8-CoA). (wikipedia.org)
  • acyl-CoA dehydrogenase (MCAD) protein. (cdc.gov)
  • 2]) upon reduction with its substrate, medium chain acyl-CoA dehydrogenase (MCAD). (thefreedictionary.com)
  • We have determined the frequency of the A985G mutation in the medium-chain acyl-CoA dehydrogenase (MCAD) gene in a cohort of 1142 healthy babies born in two Geneva hospitals. (epfl.ch)
  • Medium chain acyl-CoA dehydrogenase (MCAD) is a tetrameric flavoprotein essential for the beta-oxidation of medium chain fatty acids. (cdc.gov)
  • The ACADM gene provides instructions for making an enzyme called medium-chain acyl-CoA dehydrogenase (MCAD). (nih.gov)
  • To discern whether two related nuclear genes are expressed similarly, the tissue distribution and developmental profile of the rat long- and medium-chain acyl-CoA dehydrogenase (LCAD and MCAD) mRNAs were compared. (elsevier.com)
  • LC-MS/MS was used to measure MCAD- or VLCAD-catalyzed production of enoyl-CoA and hydroxyacyl-CoA, in human lymphocytes. (cdc.gov)
  • 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)
  • Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). (genecards.org)
  • Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:21237683, PubMed:11134486). (genecards.org)
  • The first step of the [beta]-oxidation cycle is catalyzed by acyl-CoA dehydrogenases , whereas the enzymes of MTP catalyze the last 3 steps of [beta]-oxidation. (thefreedictionary.com)
  • Additionally, acyl-CoA dehydrogenase , very long chain, which is involved in a fatty acid [beta]-oxidation pathway, was found in the QTL interval on SSC12 [14]. (thefreedictionary.com)
  • Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the initial rate-limiting step in mitochondrial fatty acid beta-oxidation. (nih.gov)
  • Previous analysis of the riboflavin-deficient rat has shown that the failure of fatty acid oxidation is due to a decrease in the activity of the acyl-CoA dehydrogenases of beta-oxidation. (biochemj.org)
  • Very-long-chain acyl-CoA dehydrogenase (VLCAD) is one of four straight-chain acyl-CoA dehydrogenase (ACD) enzymes, which are all nuclear encoded mitochondrial flavoproteins catalyzing the initial step in fatty acid beta-oxidation. (semanticscholar.org)
  • Without acyl CoA dehydrogenase to initiate the first step of mitochondrial beta-oxidation, your ability to metabolize fats is inhibited (1). (blogspot.com)
  • Because the body relies on the production of acetyl CoA from its storage of fat for energy, the lack of acetyl CoA dehydrogenase and in its capacity to produce beta-oxidation causes the body to end up in a hypoglycemic (no glucose) and hypoketotic state (no ketones from oxidation of fatty acids) (1p159;2-3). (blogspot.com)
  • The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). (genecards.org)
  • In isolated muscle mitochondria, cytochromes aa3, b and c were partially decreased, butyryl-CoA dehydrogenase and palmitoyl-CoA dehydrogenase activities were 10 and 54% of the normal, respectively. (elsevier.com)
  • The optimum substrate for SCAD is butyryl-CoA, a fatty acid with four carbon units. (biomedcentral.com)
  • ACADM, a member of the acyl-CoA dehydrogenase (ACAD) family that comprises 9 known proteins, is involved in the oxidation of medium-chain fatty acids and amino acids (Kim Miura, 2004). (thefreedictionary.com)
  • Recommended when Medium Chain Acyl-CoA Dehydrogenase (ACADM) 2 Mutations ( 0051205 ) does not identify two causative variants. (aruplab.com)
  • [email protected]#To investigate the effect of medium-chain acyl-CoA dehydrogenase (ACADM) on invasion and metastasis of breast cancer cells and explore the underlying mechanism. (bvsalud.org)
  • This gene provides instructions for making an enzyme called medium-chain acyl-CoA dehydrogenase, which is required to break down (metabolize) a group of fats called medium-chain fatty acids. (medlineplus.gov)
  • is an enzyme with systematic name very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. (wikipedia.org)
  • This enzyme catalyses the following chemical reaction a very-long-chain acyl-CoA + electron-transfer flavoprotein ⇌ {\displaystyle \rightleftharpoons } a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein This enzyme contains FAD as prosthetic group. (wikipedia.org)
  • This gives a total of four FAD molecules and four acyl-CoA substrate binding sites per enzyme. (wikipedia.org)
  • The acyl-CoA substrate is bound completely within each monomer of the enzyme. (wikipedia.org)
  • Acyl CoA dehydrogenase is the enzyme used to catalyze the first step of β-oxidation in Fatty acid metabolism . (wikidoc.org)
  • Deficiencies have been identified in each of these FAO enzyme forms with the exception of long-chain acyl-CoA dehydrogenase (5). (thefreedictionary.com)
  • The activity of this enzyme is increased such that the ratio of short-chain acyl-CoA dehydrogenase apoenzyme to holoenzyme does not change. (biochemj.org)
  • The increased mitochondrial specific activity of short-chain acyl-CoA dehydrogenase during starvation may result from an increased availability of flavin coenzyme or an increase in enzyme catalytic efficiency. (biochemj.org)
  • The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds. (creative-enzymes.com)
  • VLCAD occurs when the body either does not make enough or makes non-working enzyme called very long-chain acyl-CoA dehydrogenase. (diseaseinfosearch.org)
  • That is, the enzyme-one of four depending on fatty acid chain lengths-catalyzes the formation of the double bond between alpha- and beta-carbons, which then are degraded to two-carbon acetyl CoA units (1p159). (blogspot.com)
  • This led us to study the pyruvate dehydrogenase complex (PDC), the key enzyme in the glycolysis releasing acetyl-CoA to the TCA cycle. (regionh.dk)
  • It occurs due to the defects present in the enzyme complex to break the certain group of fatty acids and is known as the short chain acyl co enzyme A dehydrogenase which is referred as the SCADD. (alldiseases.org)
  • These lead to the lower levels of enzyme known as the short chain acyl co enzyme A dehydrogenase which is referred as the SCADD. (alldiseases.org)
  • Electron-transferring-flavoprotein dehydrogenase (ETF dehydrogenase or electron transfer flavoprotein-ubiquinone oxidoreductase, EC 1.5.5.1) is an enzyme that transfers electrons from electron-transferring flavoprotein in the mitochondrial matrix, to the ubiquinone pool in the inner mitochondrial membrane. (wikipedia.org)
  • Co enzyme A (CoA) is a ubiquitous cofactor present in every known organism. (mdpi.com)
  • exceptions are AtuC/AtuF, which constitute the two subunits of geranyl-CoA carboxylase, the key enzyme of the Atu pathway. (microbiologyresearch.org)
  • Enzyme analyses were performed in leukocytes with: hexanoyl-CoA (C6-CoA) +/− butyryl-CoA (C4-CoA), and phenylpropionyl-CoA (PP-CoA). (biomedcentral.com)
  • Very-long-chain acyl-CoA dehydrogenase (EC 1.3.8.9, ACADVL (gene). (wikipedia.org)
  • Recombinant adeno-associated virus-mediated gene delivery of long chain acyl coenzyme A dehydrogenase (LCAD) into LCAD-deficient mice. (umassmed.edu)
  • Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene. (semanticscholar.org)
  • Nagan N, Kruckeberg KE, Tauscher AL, Bailey KS, Rinaldo P, Matern D. The frequency of short-chain acyl-CoA dehydrogenase gene variants in the US population and correlation with the C(4)-acylcarnitine concentration in newborn blood spots. (nih.gov)
  • This gene encodes a tetrameric mitochondrial flavoprotein, which is a member of the acyl-CoA dehydrogenase family. (genecards.org)
  • Gene Ontology (GO) annotations related to this gene include flavin adenine dinucleotide binding and fatty-acyl-CoA binding . (genecards.org)
  • Purified PA1535 gene product revealed high citronellyl-CoA dehydrogenase activity ( V max 2450 mU mg −1 ) but had significantly lower affinity than AtuD to citronellyl-CoA ( K m 18 μM). (microbiologyresearch.org)
  • The extent of the LCADH-flavin cofactor reduction observed with most substrates and the rate of the subsequent reoxidation with oxygen are markedly different from those found with human medium chain acyl-CoA dehydrogenase. (uni-konstanz.de)
  • This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. (nih.gov)
  • ac·yl-CoA de·hy·dro·gen·ase/ ( de-hi´dro-jen-ās ) any of several enzymes that catalyze the oxidation of acyl coenzyme A thioesters as a step in the degradation of fatty acids. (thefreedictionary.com)
  • Long-chain 3-hydroxy acyl-coenzyme A dehydrogenase (LCHAD) is 1 of 3 enzymatic activities that comprise the trifunctional protein of the inner mitochondrial membrane. (medigest.uk)
  • The other 2 activities of the protein are long-chain 3-ketoacyl CoA thiolase (LCKT) and 2-enoyl coenzyme A (CoA) hydratase (LCEH). (medigest.uk)
  • The mitochondrial isovaleryl-coenzyme A dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism. (microbiologyresearch.org)
  • Medium-chain acyl-CoAs generated by long-chain specific enzymes at the inner mitochondrial membrane undergo a series of enzymatic steps in the matrix to generate acetyl-CoA and a chain-shortened acyl-CoA. (dovepress.com)
  • In vitro studies were performed using isovaleryl-CoA dehydrogenase (IVD), isobutyryl-CoA dehydrogenase (IBD) and short branched-chain acyl-CoA dehydrogenase (SBCAD), enzymes involved in the degradation pathway of leucine, valine and isoleucine. (aspetjournals.org)
  • The enzymatic activities of the three purified human enzymes were measured using optimized HPLC procedures and the respective kinetic parameters were determined in the absence and presence of VPA and the corresponding CoA and dephosphoCoA conjugates. (aspetjournals.org)
  • In the present work, we sought to compare the dehydrogenase activities and H2O2-producing capacities of VLCAD and LCAD using isolated liver mitochondria, recombinant enzymes, and the human hepatic cell line HepG2. (informnetwork.org)
  • Synthesis of CoA-thioesters is vital for the study of CoA-dependent enzymes and pathways, but also as standards for metabolomics studies. (mdpi.com)
  • MADD can be primary, caused by a genetic defect in the electron transfer flavoproteins (ETF) or in ETF dehydrogenase (ETFDH), or secondary, resulting from genetic defects of riboflavin transport (RFVT) or flavin adenine dinucleotide (FAD) synthesis (i.e. (nature.com)
  • Changes in blood carnitine and acylcarnitine profiles of very long-chain acyl-CoA dehydrogenase-deficient mice subjected to stress. (labome.org)
  • Tissue carnitine homeostasis in very-long-chain acyl-CoA dehydrogenase-deficient mice. (labome.org)
  • This reduces malonyl-CoA content and promotes mitochondrial fatty acid oxidation by diminishing the inhibitory effect of malonyl CoA on carnitine palmitoyltransferase-1. (diabetesjournals.org)
  • Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. (biochemj.org)
  • cDNA clone for general acyl CoA dehydrogenase (GAD) was isolated from a rat liver cDNA expression library in λgtll using anti-pig kidney GAD antibody. (uni-konstanz.de)
  • Normally, electrons generated by fatty acids oxidation in the mitochondrial matrix are first transferred to ETF and then electron transfer flavoprotein dehydrogenase (ETFDH = ETF-Ubiquinone-oxidoreductase = ETF-QO). (biomedcentral.com)
  • In my own specialist area of lipid metabolism, deficiencies of the fatty acid metabolizing acyl-CoA dehydrogenases are defined as a group of diseases that may be potentially treatable with a combination of dietary manipulation and prevention of fasting, because these are essentially diseases of fasting intolerance. (thefreedictionary.com)
  • Gregersen N, Andresen BS, Corydon MJ, Corydon TJ, Olsen RK, Bolund L, Bross P. Mutation analysis in mitochondrial fatty acid oxidation defects: Exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship. (nih.gov)
  • Some success in identifying acyl-CoA dehydrogenase (ACAD) deficiencies before they are symptomatic has been achieved through tandem mass spectrometry. (figshare.com)
  • Rodents are also known to highly express long-chain acyl-CoA dehydrogenase (LCAD), another flavoprotein that functionally overlaps with VLCAD. (informnetwork.org)
  • One of these genes, lipB , encodes an acyl-CoA dehydrogenase homologue. (microbiologyresearch.org)
  • We measured the oxidation rate of palmitoyl-CoA (C16-CoA) as well as the expression of genes involved in lipogenesis and renal failure. (springeropen.com)
  • This probably allowed for the substrate binding site to open up considerably to accommodate much larger polycyclic-CoA substrates, rather than fatty acids of varying chain lengths. (wikipedia.org)
  • Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons. (nih.gov)
  • The starvation-associated increase in fatty acid oxidation is mediated by an increase in the mitochondrial short-chain acyl-CoA dehydrogenase activity. (biochemj.org)
  • We conclude that short-chain acyl-CoA dehydrogenase activity is limiting for fatty acid oxidation when its activity falls below a critical point. (biochemj.org)
  • EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. (creative-enzymes.com)
  • Pig kidney LCADH was purified using an optimized method which also produces apparently pure short-chain-acyl-CoA dehydrogenase (SCADH) and medium-chain-acyl-CoA dehydrogenase (MCADH) in good yields. (uni-konstanz.de)
  • Schmidt SP, Corydon TJ, Pedersen CB, Bross P, Gregersen N. Misfolding of short-chain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress. (nih.gov)
  • 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)
  • This is the first study demonstrating that acylcarnitines and acyl-CoA directly correlate and concomitantly increase after exercise in VLCAD-deficient muscle. (labome.org)
  • Recently, very long-chain acyl-CoA dehydrogenase (VLCAD) was shown to have partial oxidase activity and to produce H2O2 in the livers of mice maintained on a high-fat diet. (informnetwork.org)
  • In vitro, recombinant mouse LCAD (mLCAD) exhibited stronger dehydrogenase activity than mouse VLCAD (mVLCAD) with palmitoyl-CoA as substrate, and produced H2O2 at a significantly higher rate. (informnetwork.org)
  • To address this question, we measured the palmitoyl-CoA (C16-CoA) oxidation rate in the kidney of wild-type (WT) and VLCAD −/− mice in situations of normal and increased energy demand as well as the expression of other dehydrogenases with overlapping substrate specificity. (springeropen.com)
  • Their action results in the introduction of a trans double-bond between C2 (α) and C3 (β) of the acyl-CoA thioester substrate. (wikipedia.org)
  • Based on our results we provide a general guideline to the optimal synthesis method of a given CoA-thioester in respect to its functional group(s) and the commercial availability of the precursor molecule. (mdpi.com)
  • To our knowledge AtuD is the first acyl-CoA dehydrogenase with a documented substrate specificity for terpenoid molecule structure and is essential for a functional Atu pathway. (microbiologyresearch.org)
  • This class of ACAD was demonstrated to form α2β2 heterotetramers, rather than the usual α4 homotetramer, a protein architecture that evolved in order to accommodate a much larger steroid-CoA substrate. (wikipedia.org)
  • Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. (biochemj.org)
  • C6-C10-dicarboxylic aciduria: investigations of a patient with riboflavin responsive multiple acyl-CoA dehydrogenation defects. (medscape.com)
  • 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)
  • On binding to its receptor, gAcrp30 activates AMPK, leading to subsequent inhibition of acetyl-CoA carboxylase ( 1 , 10 ). (diabetesjournals.org)
  • The thioesters of CoA are core intermediates in many metabolic processes, such as the citric acid cycle, fatty acid biosynthesis and secondary metabolism, including polyketide biosynthesis. (mdpi.com)
  • Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. (nih.gov)
  • Thus, the clinical features may arise from either toxicity due to long-chain acyl-CoA esters that cause cardiomyopathy and cardiac arrhythmias or from a block in long-chain fatty acid oxidation that leads to an inability to synthesize ketone bodies and/or adenosine triphosphate from long-chain fatty acids. (medigest.uk)
  • The CoA esters produced range from short- to long-chain, include branched and α,β-unsaturated representatives as well as other functional groups. (mdpi.com)
  • The overall reaction catalyzed by ETF-QO is as follows: ETF-QO(red) + ubiquinone ↔ ETF-QO(ox) + ubiquinol Enzymatic activity is usually assayed spectrophotometrically by reaction with octanoyl-CoA as the electron donor and ubiquinone-1 as the electron acceptor. (wikipedia.org)
  • Friulimicin consists of a cyclic peptide core of ten amino acids and an acyl residue linked to an exocyclic amino acid. (microbiologyresearch.org)
  • Our results demonstrate that LCADH is as important as the other acyl-CoA dehydrogenases in fatty acid oxidation at physiological, mitochondrial pH with optimal substrates of chain length C10 C14. (uni-konstanz.de)