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)

The condition is inherited in an X-linked recessive pattern, meaning that the gene for G6PD deficiency is located on the X chromosome and affects males more frequently than females. Females may also be affected but typically have milder symptoms or may be carriers of the condition without experiencing any symptoms themselves.

G6PD deficiency can be caused by mutations in the G6PD gene, which can lead to a reduction in the amount of functional enzyme produced. The severity of the condition depends on the specific nature of the mutation and the degree to which it reduces the activity of the enzyme.

Symptoms of G6PD deficiency may include jaundice (yellowing of the skin and eyes), fatigue, weakness, and shortness of breath. In severe cases, the condition can lead to hemolytic anemia, which is characterized by the premature destruction of red blood cells. This can be triggered by certain drugs, infections, or foods that contain high levels of oxalic acid or other oxidizing agents.

Diagnosis of G6PD deficiency typically involves a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment is focused on managing symptoms and preventing complications through dietary modifications, medications, and avoidance of triggers such as certain drugs or infections.

Overall, G6PD deficiency is a relatively common genetic disorder that can have significant health implications if left untreated. Understanding the causes, symptoms, and treatment options for this condition is important for ensuring appropriate care and management for individuals affected by it.

... (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) Portal: Biology ( ... 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 ...
In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction acyl-CoA + ... crotonyl-CoA reductase, and acyl-CoA dehydrogenase (NADP+). As of late 2007, only one structure has been solved for this class ... Other names in common use include 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide, ... the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+. This ...
Acyl-CoA dehydrogenase Medium-chain acyl-CoA dehydrogenase Butyryl-CoA (also known as butanoyl-CoA) Mahler HR (January 1954). " ... Short-chain acyl-CoA dehydrogenase (EC 1.3.8.1, butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase, butyryl dehydrogenase, ... short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:( ... Short-chain+acyl-CoA+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ...
... (EC 1.3.8.8, palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, long-chain acyl ... long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase, ACADL (gene).) is an enzyme with systematic name long-chain acyl-CoA: ... Long-chain+acyl-CoA+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the ...
... acyl dehydrogenase (ambiguous), fatty-acyl-CoA dehydrogenase (ambiguous), acyl CoA dehydrogenase (ambiguous), general acyl CoA ... Medium-chain acyl-CoA dehydrogenase (EC 1.3.8.7, fatty acyl coenzyme A dehydrogenase (ambiguous), acyl coenzyme A dehydrogenase ... dehydrogenase (ambiguous), medium-chain acyl-coenzyme A dehydrogenase, acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous), ... Medium-chain+acyl-CoA+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ...
The entire sequence of transfer reactions is as follows: Acyl-CoAAcyl-CoA dehydrogenase → ETF → ETF-QO → UQ → Complex III. ... Deficiency in ETF dehydrogenase causes the human genetic disease multiple acyl-CoA dehydrogenase deficiency. ETQ-QO links the ... Singla M, Guzman G, Griffin AJ, Bharati S (Mar 2008). "Cardiomyopathy in multiple Acyl-CoA dehydrogenase deficiency: a clinico- ... also known as MADD for multiple acyl-CoA dehydrogenase deficiency), in which there is an improper buildup of fats and proteins ...
Medium-chain acyl-CoA dehydrogenase deficiency (MCAD deficiency or MCADD) is a disorder of fatty acid oxidation that impairs ... "Orphanet: Medium chain acyl CoA dehydrogenase deficiency". www.orpha.net. Retrieved 14 April 2019. Morris, Andrew A.M.; ... Rinaldo, P.; O'Shea, J. J.; Coates, P. M.; Hale, D. E.; Stanley, C. A.; Tanaka, K. (1988). "Medium-Chain Acyl-CoA Dehydrogenase ... "Maternal medium-chain acyl-CoA dehydrogenase deficiency identified by newborn screening". Molecular Genetics and Metabolism. ...
"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 ...
Due to this mutation, effective levels of very long-chain-acyl-CoA-dehydrogenase are low or absent in the body, giving rise to ... A change of the gene that codes for very long-chain-acyl-CoA-dehydrogenase (VLCAD) results in a deficiency or malfunction of ... "Very Long Chain Acyl CoA Dehydrogenase Deficiency (LCAD)". "VLCAD deficiency , Genetic and Rare Diseases Information Center ( ... Mutations in the ACADVL gene lead to inadequate levels of an enzyme called very long-chain acyl-coenzyme A (CoA) dehydrogenase ...
"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-transferring-flavoprotein dehydrogenase. When one of these enzymes is ...
"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 ...
"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 ...
Multiple acyl-CoA dehydrogenase deficiency - similar in biochemical features; responsive to riboflavin in the majority of late- ...
"Long-Chain Acyl CoA Dehydrogenase Deficiency: Background, Pathophysiology, Epidemiology". eMedicine. 24 March 2016. Retrieved ... "HADHA hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit [Homo ... "OMIM Entry - * 600890 - HYDROXYACYL-CoA DEHYDROGENASE/3-KETOACYL-CoA THIOLASE/ENOYL-CoA HYDRATASE, ALPHA SUBUNIT; HADHA". omim. ... Avoiding factors that might precipitate condition Glucose Low fat/high carbohydrate nutrition Long-chain acyl-CoA dehydrogenase ...
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 ...
Two prominent examples are coumaroyl-coenzyme A and crotonyl-coenzyme A. They arise by the action of acyl-CoA dehydrogenases. ... Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718-25 ... it is the acyl group derived from acrylic acid. The preferred IUPAC name for the group is prop-2-enoyl, and it is also known as ...
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 ... "ACADM - Medium-chain specific acyl-CoA dehydrogenase, mitochondrial precursor - Homo sapiens (Human) - ACADM gene & protein". ... "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 ...
... (GCDH) is an enzyme encoded by the GCDH gene on chromosome 19. The protein belongs to the acyl-CoA ... "GCDH glutaryl-CoA dehydrogenase [ Homo sapiens (human) ]". NCBI. Retrieved 6 August 2015. Fu Z, Wang M, Paschke R, Rao KS, ... Rao KS, Albro M, Dwyer TM, Frerman FE (December 2006). "Kinetic mechanism of glutaryl-CoA dehydrogenase". Biochemistry. 45 (51 ... Chemistry portal Biology portal Technology portal Glutaryl-CoA+dehydrogenase at the US National Library of Medicine Medical ...
"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. ...
Other names in common use include branched-chain acyl-CoA dehydrogenase, 2-methyl branched chain acyl-CoA dehydrogenase, and 2- ... Ikeda Y, Dabrowski C, Tanaka K (1983). "Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver ... Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". J. Biol. Chem. 258 (2): 1066-76. PMID 6401712. Portal ... a 2-methylacyl-CoA dehydrogenase (EC 1.3.99.12) is an enzyme that catalyzes the chemical reaction 2-methylbutanoyl-CoA + ...
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 ...
Beta oxidation of acyl-CoA occurs in four steps. 1. Acyl-CoA dehydrogenase catalyzes dehydrogenation of the acyl-CoA, creating ... The latter conversion is mediated by acyl-CoA synthase" acyl-P + HS-CoAacyl-S-CoA + Pi + H+ Three types of acyl-CoA ... A rare disease called multiple acyl-CoA dehydrogenase deficiency (MADD) is a fatty acid metabolism disorder. Acyl-CoA is ... catalyzed by acyl-CoA synthetase. Fatty acids are converted to their acyl phosphate, the precursor to acyl-CoA. ...
"Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ... "Orphanet: Short chain acyl CoA dehydrogenase deficiency". www.orpha.net. Retrieved 2016-10-30. Online Mendelian Inheritance in ... Mutations in the ACADS gene lead to inadequate levels of short-chain acyl-CoA dehydrogenase, which is important for breaking ... The symptoms of short-chain acyl-CoA dehydrogenase deficiency may be triggered during illnesses such as viral infections. In ...
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 (Articles with short ...
... 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 ...
Fatty acids are made by fatty acid synthases that polymerize and then reduce acetyl-CoA units. The acyl chains in the fatty ... Hundreds of separate types of dehydrogenases remove electrons from their substrates and reduce NAD+ into NADH. This reduced ... and this breakdown process involves the release of significant amounts of acetyl-CoA, propionyl-CoA, and pyruvate, which can ... The glycerol enters glycolysis and the fatty acids are broken down by beta oxidation to release acetyl-CoA, which then is fed ...
3-Hydroxyisovaleryl CoA accumulation can inhibit cellular respiration either directly or via effects on the ratios of acyl CoA: ... The concentration of β-hydroxybutyrate in blood plasma is measured through a test that uses β-hydroxybutyrate dehydrogenase, ... This metabolic pathway is as follows: butyrate→butyryl-CoA→crotonyl-CoA→β-hydroxybutyryl-CoA→poly-β-hydroxybutyrate→D-β-(D-β- ... Metabolic impairment diverts methylcrotonyl CoA to 3-hydroxyisovaleryl CoA in a reaction catalyzed by enoyl-CoA hydratase (22, ...
Medium chain acyl dehydrogenase deficiency Reference, Genetics Home. "LCHAD deficiency". Genetics Home Reference. Retrieved ... "Long-Chain 3-Hydroxyacyl-CoA Dehydrogenase Deficiency: Clinical Presentation and Follow-Up of 50 Patients". Pediatrics. 109 (1 ... Mutations in the HADHA gene lead to inadequate levels of an enzyme called long-chain 3-hydroxyacyl-coenzyme A (CoA) ... Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency is a rare autosomal recessive fatty acid oxidation disorder that ...
ACSF3: encoding enzyme Acyl-CoA synthetase family member 3 ACSM2B: encoding enzyme Acyl-coenzyme A synthetase ACSM2B, ... encoding protein Pyruvate dehydrogenase phosphatase regulatory subunit PKDTS: Polycystic kidney disease, infantile severe, with ... mitochondrial ACSM3: encoding enzyme Acyl-coenzyme A synthetase ACSM3, mitochondrial 2 ADHD1: Attention deficit-hyperactivity ...
Middleton B (1994). "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase ... which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. The encoded protein can also bind ... Trifunctional protein deficiency is characterized by decreased activity of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), ... Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, ...
... a gene Medium-chain acyl-CoA dehydrogenase, an enzyme used in lipid metabolism Medium-chain acyl-coenzyme A dehydrogenase ...
By disrupting an acyl-coenzyme A (CoA) thioesterase gene, Sabirova and colleagues were able to mutate the organism to hyper- ... This sequential pathway first produces alcohols, then alcohol and aldehyde dehydrogenases, and ultimately aldehydes and fatty ...
Examples of this type of disorder are albinism, medium-chain acyl-CoA dehydrogenase deficiency, cystic fibrosis, sickle cell ...
The catechol is then metabolized to acetyl CoA and succinyl CoA, used by organisms mainly in the citric acid cycle for energy ... The reaction involves the acylation of benzene (or many other aromatic rings) with an acyl chloride using a strong Lewis acid ... These include cytochrome P450 2E1 (CYP2E1), quinine oxidoreductase (NQ01 or DT-diaphorase or NAD(P)H dehydrogenase (quinone 1 ...
A molecule of coenzyme A carrying an acyl group is also referred to as acyl-CoA. When it is not attached to an acyl group, it ... Acetyl-CoA is utilised in the post-translational regulation and allosteric regulation of pyruvate dehydrogenase and carboxylase ... Propionyl-CoA Butyryl-CoA Myristoyl-CoA Crotonyl-CoA Acetoacetyl-CoA Coumaroyl-CoA (used in flavonoid and stilbenoid ... The major route of CoA activity loss is likely the air oxidation of CoA to CoA disulfides. CoA mixed disulfides, such as CoA-S- ...
Deficiency of LCHAD (3-hydroxyacyl-CoA dehydrogenase) leads to an accumulation of medium and long chain fatty acids. When this ... "Disorders of mitochondrial fatty acyl-CoA beta-oxidation" (PDF). Journal of Inherited Metabolic Disease. 22 (4): 442-487. doi: ... IJlst L, Oostheim W, Ruiter JP, Wanders RJ (1997). "Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: ... caused by long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency. This leads to decreased metabolism of long chain fatty ...
SCARB2 Acyl-CoA dehydrogenase, long chain, deficiency of; 201460; ACADL Acyl-CoA dehydrogenase, medium chain, deficiency of; ... ACADM Acyl-CoA dehydrogenase, short chain, deficiency of; 201470; ACADS Adenocarcinoma of lung, response to tyrosine kinase ... ACADSB 3-hydroxyacyl-coa dehydrogenase deficiency; 231530; HADHSC 3-hydroxyisobutryl-CoA hydrolase deficiency; 250620; HIBCH 3- ... DCX Succinic semialdehyde dehydrogenase deficiency; 271980; ALDH5A1 Succinyl-CoA:3-oxoacid CoA transferase deficiency; 245050; ...
It has been found in certain Candida yeast, where it participates in omega oxidation of fatty acids to produce acyl-CoA for ... Yeast have low levels of fatty alcohol dehydrogenase.) The long-chain alcohol is then oxidized by long-chain fatty aldehyde ... This is different from the pathway found in mammalian tissues, which employs long-chain fatty alcohol dehydrogenase or fatty ... dehydrogenase to a carboxylic acid, also producing NADH from NAD+. Fatty acids can be oxidized again to make dicarboxylic ...
An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA ... "Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different ... THC-CoA oxidase, THCA-CoA oxidase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, 3alpha,7alpha,12alpha- ... Schepers L, Van Veldhoven PP, Casteels M, Eyssen HJ, Mannaerts GP (1990). "Presence of three acyl-CoA oxidases in rat liver ...
... 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 ...
β-Oxidation uses pyruvate carboxylase, acyl-CoA dehydrogenase, and β-ketothiolase. Amino acid production is facilitated by ... The citric acid cycle involves acyl-CoA, pyruvate, acetyl-CoA, citrate, isocitrate, α-ketoglutarate, succinyl-CoA, fumarate, ... isocitrate dehydrogenase, α-ketoglutarate dehydrogenase, succinyl-CoA synthetase, fumarase, and malate dehydrogenase. The urea ... in the matrix activates pyruvate dehydrogenase, isocitrate dehydrogenase, and α-ketoglutarate dehydrogenase which increases the ...
... acyl-CoA oxidase (see, e.g., ACOX1, MIM 609751); the 'D-bifunctional enzyme,' with enoyl-CoA hydratase and D-3-hydroxyacyl-CoA ... 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities". The Journal of Biological Chemistry. 265 ... "D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified ... D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein: its expression in the developing human ...
STEP 3: Acyl group transfer to CoA. The proper arrow-pushing mechanism is shown in Figure 5. *NOTE: The reduced lipoyl arm now ... and converting them to α-Methylbutyryl-CoA, Isobutyryl-CoA and Isovaleryl-CoA respectively. In bacteria, this enzyme ... BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and alpha- ... Other mitochondrial autoantigens include pyruvate dehydrogenase and branched-chain oxoglutarate dehydrogenase, which are ...
... and acyl CoA dehydrogenase. FADH and FADH2 are reduced forms of FAD. FADH2 is produced as a prosthetic group in succinate ... Flavin mononucleotide is a prosthetic group found in, among other proteins, NADH dehydrogenase, E.coli nitroreductase and old ... dehydrogenase, an enzyme involved in the citric acid cycle. In oxidative phosphorylation, two molecules of FADH2 typically ...
Implications for the treatment of multiple acyl-CoA dehydrogenase deficiency". Journal of Inherited Metabolic Disease. 44 (4): ... Crotonyl-coenzyme A Acetoacetyl CoA Beta-hydroxybutyryl-CoA dehydrogenase Numa, S.; Ishimura, Y.; Nishizuka, Y.; Hayaishi, O. ( ... The L-3-hydroxybutyl-CoA (or (S)-3-hydroxybutanoyl-CoA) enantiomer is also the second to last intermediate in beta oxidation of ... β-Hydroxybutyryl-CoA (or 3-hydroxybutyryl-coenzyme A) is an intermediate in the fermentation of butyric acid, and in the ...
... 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 ...
In the mitochondria, acyl-CoA esters are involved in the acylation of mitochondrial NAD+ dependent dehydrogenases; because ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl ... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ... "Entrez Gene: ACOT4 acyl-CoA thioesterase 4". Mashek DG, Bornfeldt KE, Coleman RA, Berger J, Bernlohr DA, Black P, DiRusso CC, ...
The phenotype of the patients is reminiscent of multiple acyl-CoA dehydrogenase deficiency (MADD). According to a review ...
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 ...
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 ...
Supplementary test information for Very Long-Chain Acyl-CoA Dehydrogenase (ACADVL) Deficiency such as test interpretation, ... Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is an inherited disorder of mitochondrial long-chain fatty acid ... Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency. Am J Hum Genet. 1999 ... Rhabdomyolysis in the military: recognizing late-onset very long-chain acyl Co-A dehydrogenase deficiency. Mil Med. 2006;171(7 ...
"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 ... Acyl-CoA Dehydrogenase, Long-Chain*Acyl-CoA Dehydrogenase, Long-Chain. *Acyl CoA Dehydrogenase, Long Chain ... Below are the most recent publications written about "Acyl-CoA Dehydrogenase, Long-Chain" by people in Profiles. ...
Medium-chain Acyl-CoA dehydrogenase deficiency (MCADD) is the most common inherited disorder of fatty acid beta-oxidation. ... Medium-chain Acyl-CoA dehydrogenase deficiency presenting with neonatal pulmonary haemorrhage.. Staels, Willem; DHaese, James ...
Short/Branched Chain Acyl-CoA Dehydrogenase (SBCAD) Deficiency Short-Chain Acyl-CoA Dehydrogenase Deficiency (SCADD) Sickle ... Short-Chain Acyl-CoA Dehydrogenase Deficiency - Information for Parents (STAR-G). A fact sheet, written by a genetic counselor ... Because short-chain acyl-CoA dehydrogenase deficiency (SCADD) (the result of an intramitochondrial defect in the beta-oxidation ... Short-Chain Acyl-CoA Dehydrogenase Deficiency (OMIM). Information about clinical features, diagnosis, management, and molecular ...
... a secondary marker for medium chain acyl-CoA dehydrogenase deficiency), immunoreactive trypsinogen (a primary marker for cystic ... Medium-chain acyl-CoA dehydrogenase deficiency. Very long-chain acyl-CoA dehydrogenase deficiency ... Short-chain acyl-CoA dehydrogenase deficiency. Medium/short-chain L-3-hydroxyacyl-CoA ...
Very-long-chain acyl-coenzyme A (CoA) dehydrogenase deficiency (VLCADD) is an autosomal recessive disorder of fatty acid ... Genotype-phenotype correlations: sudden death in an infant with very-long-chain acyl-CoA dehydrogenase deficiency. Coughlin CR ...
Mediumchain acyl-CoA dehydrogenase deficiency: human genome epidemiology review. Genet Med. 1999;1(7):332-9. ...
Keywords : acyl-CoA dehydrogenase deficiency; fatty acids; beta oxidation disorder; Duchenne muscular dystrophy; dystrophin. ... Clinical presentation of a pediatric patient diagnosed with Duchenne muscular dystrophy and medium chain acyl-CoA dehydrogenase ...
acyl-CoA dehydrogenase medium chain. IEA. KEGG. rno:00410. NCBI chr 2:242,858,865...242,883,036 Ensembl chr 2:242,858,865... ... enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase. IEA. KEGG. rno:00410. NCBI chr11:79,241,927...79,275,173 Ensembl chr11 ... hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha. IEA. KEGG. rno:00410. NCBI chr 6:26,187,969... ... malonyl-CoA decarboxylase. IEA. KEGG. rno:00410. NCBI chr19:47,447,931...47,463,794 Ensembl chr19:47,447,970...47,463,793 ...
The first steps in the processing of fats are facilitated by acyl-CoA dehydrogenases. Three distinct acyl-CoA dehydrogenases ... Miller ME, Brooks JG, Forbes N, Insel R. Frequency of medium-chain acyl-CoA dehydrogenase deficiency G-985 mutation in sudden ... Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation ... The most common disorder of fatty acid beta-oxidation is medium-chain acyl-CoA dehydrogenase deficiency (MCADD). MCADD is an ...
medium-chain acyl-CoA dehydrogenase deficiency(Genetics Home Reference). *ACYL-CoA DEHYDROGENASE, MEDIUM-CHAIN, DEFICIENCY OF. ... Medium-chain acyl-CoA dehydrogenase deficiency is caused by mutations in the ACADM gene; it has an autosomal recessive pattern ... Medium-chain acyl-CoA dehydrogenase deficiency is an inherited condition characterized by inadequate levels of an enzyme ...
Medium-chain acyl-CoA dehydrogenase deficiency (MCAD). *Very long-chain acyl-CoA dehydrogenase deficiency (VLCAD) ...
Very long-chain acyl-CoA dehydrogenase deficiency. VLCAD. Core. 237997005. 277.85. E71.310 ...
A deficiency in the activity of medium chain acyl-CoA dehydrogenase, an enzyme in the pathway for beta-oxidation of fatty acids ... Both HMG-CoA reductase and the LDLR are synthesized in response to high levels of intracellular cholesterol ... HMG-CoA reductase is activated when the LDLR is down-regulated and the cell requires cholesterol ... HMG-CoA red uctase is activated due to low levels of thyroid hormones ...
Short-chain Acyl-CoA dehydrogenase deficiency: studies in a large family adding to the complexity of the disorder. Pediatrics. ... primary carnitine deficiency or medium-chain acyl-CoA dehydrogenase [MCAD] deficiency), molecular analysis can be performed. ... Long-Chain 3-Hydroxyacyl-CoA Dehydrogenase (LCHAD) Deficiency * Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency (MCADD) ...
Condition Long-chain L-3-Hydroxy acyl-CoA dehydrogenase deficiency (LCHAD): revised SNOMED CT code, UMLS CUI, ICD-10-CM code ... Condition Short-chain L-3-hydroxy acyl-CoA dehydrogenase deficiency (SCHAD): added ICD-10-CM code; revised ICD-9-CM code ... Condition Medium-chain acyl-CoA dehydrogenase deficiency (MCAD): revised OMIM number. *Condition Methylene tetrahydrofolate ... Condition Short-chain L-3-hydroxy acyl-CoA dehydrogenase deficiency (SCHAD): revised OMIM number ...
Fold e.6: Acyl-CoA dehydrogenase NM domain-like [56644] (1 superfamily). 2 domains: (1) all-alpha: 5 helices; (2) contains an ... Superfamily e.6.1: Acyl-CoA dehydrogenase NM domain-like [56645] (3 families) flavoprotein: binds FAD; constituent families ... Family e.6.1.1: Medium chain acyl-CoA dehydrogenase, NM (N-terminal and middle) domains [56646] (10 proteins). ...
Pompe disease, metachromatic leukodystrophy, glycogen storage disease, isovaleric acidemia, short-chain acyl-coA dehydrogenase ...
People with medium chain acyl-CoA dehydrogenase deficiency (MCADD) cannot burn fat for energy. Our bodies rely on fat for ...
Fischer T, Och U, Marquardt T. Long-term ketone body therapy of severe multiple acyl-CoA dehydrogenase deficiency: a case ... In children with fatty acid oxidation defects such as multiple acyl-CoA dehydrogenase deficiency, D+L-BHB improved heart ... 3-oxoacid-CoA transferase (SCOT) required to convert AcAc back to acetyl-CoA (3). However, the liver contributes to the ... The acute production of excess acetyl-CoA drives the production of AcAc and then D-BHB which are both secreted into the ...
E71311 Medium chain acyl CoA dehydrogenase deficiency E71312 Short chain acyl CoA dehydrogenase deficiency E71313 Glutaric ... E71310 Long chain/very long chain acyl CoA dehydrogenase deficiency ...
Acyl-CoA dehydrogenase (tetradecanoyl-CoA). Model: iSbBS512_1146. Reaction:. nad_c + tdcoa_c → h_c + nadh_c + td2coa_c ...
Very long-chain Acyl-CoA dehydrogenase deficiency (VLCAD), Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHAD) or ...
Similar problems have arisen in connection with proposals for pilot trials on screening for medium chain acyl CoA dehydrogenase ...
... medium-chain acyl CoA dehydrogenase deficiency, Pompe disease, Adrenoleukodystrophy, Mucopolysaccharidosis type I, and ...
... medium chain acyl-CoA dehydrogenase deficiency (MCAD), and cystic fibrosis (CF). The authors point out that making inferences ...
... butyryl-CoA (C4:0) or isovaleryl-CoA (5:0). This gene encodes a member of the acyl-CoA dehydrogenase family. Members of this ... Mutations in this gene cause acyl-CoA dehydrogenase family member type 9 deficiency. Alternate splicing results in multiple ... and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA than on stearoyl-CoA. However, it does not play a ... family of proteins localize to the mitochondria and catalyze the rate-limiting step in the beta-oxidation of fatty acyl-CoA. ...
Acyl-CoA dehydrogenase Synonymes. Acyl déshydrogénase Acyl-CoA déshydrogénase Acyl-CoA déshydrogénase des acides gras à chaine ... Acyl déshydrogénase. Acyl-CoA déshydrogénase. Acyl-CoA déshydrogénase des acides gras à chaine moyenne. Acyl-CoA déshydrogénase ... ACYL-COA DEHYDROGENASES and ACYL-COA DEHYDROGENASE, LONG-CHAIN are also available. ... Acyl-CoA déshydrogénase des acides gras à chaîne moyenne Acyl-coenzyme A déshydrogénase Octanoyl-CoA déshydrogénase Octanoyl- ...
  • 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)
  • Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is an inherited disorder of mitochondrial long-chain fatty acid oxidation, resulting in an inability to properly break down very long-chain fatty acids into energy. (arupconsult.com)
  • Medium-chain Acyl-CoA dehydrogenase deficiency presenting with neonatal pulmonary haemorrhage. (bvsalud.org)
  • Medium-chain Acyl-CoA dehydrogenase deficiency (MCADD) is the most common inherited disorder of fatty acid beta- oxidation . (bvsalud.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)
  • 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)
  • Very-long-chain acyl-coenzyme A (CoA) dehydrogenase deficiency (VLCADD) is an autosomal recessive disorder of fatty acid oxidation. (coughlinlab.org)
  • Mediumchain acyl-CoA dehydrogenase deficiency: human genome epidemiology review. (cdc.gov)
  • Clinical presentation of a pediatric patient diagnosed with Duchenne muscular dystrophy and medium chain acyl-CoA dehydrogenase deficiency. (scielo.sa.cr)
  • 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)
  • A deficiency in the activity of medium chain acyl-CoA dehydrogenase, an enzyme in the pathway for beta-oxidation of fatty acids, is corrected by large doses of its vitamin component in some patients. (proprofs.com)
  • Background People with medium chain acyl-CoA dehydrogenase deficiency (MCADD) cannot burn fat for energy. (cdc.gov)
  • This is a Phase 1b, open-label, multiple-dose study of the safety and tolerability of 2 dose levels of REN001 in subjects with fatty acid oxidation disorders (FAODs) with confirmed mutations in the Carnitine palmitoyltransferase II deficiency (CPT2), Very long-chain Acyl-CoA dehydrogenase deficiency (VLCAD), Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHAD) or Trifunctional Protein Deficiency (TFP). (clinicaltrials.gov)
  • The Newborn Screening Molecular Laboratory performs second-tier molecular testing of newborns for cystic fibrosis, galactosemia, medium-chain acyl CoA dehydrogenase deficiency, Pompe disease, Adrenoleukodystrophy, Mucopolysaccharidosis type I, and guanidinoacetate methyltransferase in order to "rule-in" a positive diagnosis. (wadsworth.org)
  • Mutations in this gene cause acyl-CoA dehydrogenase family member type 9 deficiency. (nih.gov)
  • Very long chain acyl-CoA dehydrogenase deficiency is an autosomal recessive genetic disorder in which the first step in the mitochondrial beta-oxidation of fatty acids for 14-20 carbons is defective. (medipol.edu.tr)
  • Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase (PubMed:27499296, PubMed:15159392, PubMed:15975918, PubMed:9334218, PubMed:10356313). (nih.gov)
  • It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:9334218). (nih.gov)
  • Abstract: DESCRIPTION (provided by applicant): Carnitine acetyltransferase (CrAT) is a freely reversible mitochondrial matrix enzyme that catalyzes the exchange of short-chain acyl groups between CoA and carnitine. (nih.gov)
  • By doing so, this reaction is thought to play a key role in regenerating free CoA, modulating mitochondrial acetyl-CoA/CoA balance and relieving acetyl-CoA-mediated inhibition of pyruvate dehydrogenase (PDH), the committed step in glucose oxidation. (nih.gov)
  • Acyl-CoA Dehydrogenase, Long-Chain" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (musc.edu)
  • This graph shows the total number of publications written about "Acyl-CoA Dehydrogenase, Long-Chain" by people in this website by year, and whether "Acyl-CoA Dehydrogenase, Long-Chain" was a major or minor topic of these publications. (musc.edu)
  • Below are the most recent publications written about "Acyl-CoA Dehydrogenase, Long-Chain" by people in Profiles. (musc.edu)
  • The encoded protein is specifically active toward palmitoyl-CoA and long-chain unsaturated substrates. (nih.gov)
  • 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)
  • Members of this family of proteins localize to the mitochondria and catalyze the rate-limiting step in the beta-oxidation of fatty acyl-CoA. (nih.gov)
  • It shuttles electrons between primary flavoprotein dehydrogenases and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. (nih.gov)
  • This gene encodes a member of the acyl-CoA dehydrogenase family. (nih.gov)
  • CrAT purportedly acts to export excess carbon fuels from the mitochondria during conditions wherein the production of short-chain acyl-CoAs exceeds TCA cycle flux. (nih.gov)
  • The primary substrate of CrAT, acetyl-CoA, holds a prominent position in intermediary metabolism as the two-carbon universal end product of fatty acid, glucose and amino acid oxidation. (nih.gov)
  • Treatment of hypercholesterolemia requires knowledge of the control of HMG-CoA reductase activity and LDL receptor (LDLR) levels. (proprofs.com)
  • Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). (nih.gov)
  • Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0). (nih.gov)
  • As its major metabolic fate, acetyl-CoA typically enters the tricarboxylic acid (TCA) cycle where it drives production of reducing equivalents that in turn fuel the electron transport chain. (nih.gov)
  • The acute production of excess acetyl-CoA drives the production of AcAc and then D-BHB which are both secreted into the systemic circulation ( 8 ). (frontiersin.org)
  • AcylCoA formation to DAG, TAG, and lipid vacuole formation (Nathan Barr) (in process) f. (nih.gov)
  • Mutations in nuclear genes encoding for mitochondrial proteins very long-chain acyl-CoA dehydrogenase (VLCAD) and trifunctional protein (TFP) cause rare autosomal recessive disorders. (nih.gov)
  • 4. Tissue-specific strategies of the very-long chain acyl-CoA dehydrogenase-deficient (VLCAD-/-) mouse to compensate a defective fatty acid β-oxidation. (nih.gov)
  • 15. Development and pathomechanisms of cardiomyopathy in very long-chain acyl-CoA dehydrogenase deficient (VLCAD(-/-)) mice. (nih.gov)
  • acyl-CoA dehydrogenase (MCAD) protein. (cdc.gov)
  • Carnitine binds acyl residues and helps in their elimination, decreasing the number of acyl residues conjugated with coenzyme A (CoA) and increasing the ratio between free and acylated CoA. (medscape.com)
  • C6-C10-dicarboxylic aciduria: investigations of a patient with riboflavin responsive multiple acyl-CoA dehydrogenation defects. (medscape.com)
  • and CHOLINE catabolism, that is due to defects in either subunit of ELECTRON TRANSFER FLAVOPROTEIN or its dehydrogenase, electron transfer flavoprotein-ubiquinone oxidoreductase (EC 1.5.5.1). (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)
  • 16. De novo fatty acid biosynthesis and elongation in very long-chain acyl-CoA dehydrogenase-deficient mice supplemented with odd or even medium-chain fatty acids. (nih.gov)
  • The recent incorporation of medium chain acyl-CoA dehy death and intellectual disability. (cdc.gov)
  • 5. Cardiac tissue citric acid cycle intermediates in exercised very long-chain acyl-CoA dehydrogenase-deficient mice fed triheptanoin or medium-chain triglyceride. (nih.gov)