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. (1/257)

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)

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

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

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

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. (4/257)

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. (5/257)

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)

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

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

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

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

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

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)

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 ...
1EGC: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
1EGC: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
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
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 …. ...
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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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 ...
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 ...
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] ...
Expression of the gene encoding medium-chain acyl coenzyme A dehydrogenase (MCAD), a nuclearly encoded mitochondrial fatty acid beta-oxidation enzyme, is regulated in parallel with fatty acid oxidation rates among tissues and during development. We have shown previously that the human MCAD gene promoter contains a pleiotropic element (nuclear receptor response element [NRRE-1]) that confers transcriptional activation or repression by members of the nuclear receptor superfamily. Mice transgenic for human MCAD gene promoter fragments fused to a chloramphenicol acetyltransferase gene reporter were produced and characterized to evaluate the role of NRRE-1 and other promoter elements in the transcriptional control of the MCAD gene in vivo. Expression of the full-length MCAD promoter-chloramphenicol acetyltransferase transgene (MCADCAT.371) paralleled the known tissue-specific differences in mitochondrial beta-oxidation rates and MCAD expression. MCADCAT.371 transcripts were abundant in heart tissue ...
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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 ...
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 ...
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.
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 - ...
Vitamin A deficiency leads to altered lipid metabolism in the liver. The expression pattern of metabolic genes in vitamin A-sufficient (VAS) versus vitamin A-deficient (VAD) liver was compared using a Mouse Genome Oligo Set Version 3.0 (Qiagen-Operon) 70mer-oligonucleotide array. Results from microarray analysis were analyzed using the GeneSpring bioinformatics program. The microarray results were further confirmed by real-time PCR. Mice were made vitamin A deficient by placing them on the modified AIN-93G diet without vitamin A on the tenth day of gestation. Both the differential expression of metabolic genes and the metabolic outcome of this differential expression were assessed. ^ In this study, vitamin A deficiency caused a decrease in expression of genes encoding enzymes involved in mitochondrial β-oxidation, including fatty acid ligase, medium-chain acyl-CoA dehydrogenase, 3,2-trans-enoyl-CoA isomerase and carnitine o-palmitoyl transferase I in the liver. A decrease in the mitochondrial β
ERR1_HUMAN] Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5-TNAAGGTCA-3. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism.[1] [2] [3] [4] [5] ...
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. ...
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 ...
MY CHILD HAS MCADD - Im looking for other moms with kids with MCADD I have fb and you can look me up there I have so many questions my...
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MCADCafe.com delivers the latest MCAD industry commentary, news, product reviews, articles, events and resources from a single, convenient point. We provide our users a constantly updated view of the entire world of MCAD that allows them to make more timely and informed decisions.
MCADCafe.com delivers the latest MCAD industry commentary, news, product reviews, articles, events and resources from a single, convenient point. We provide our users a constantly updated view of the entire world of MCAD that allows them to make more timely and informed decisions.
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Amino Acid Disorders. Phenylketonuria (PKU). Maple Syrup Urine Disease (MSUD). Homocystinuria Tyrosinemia Type I. Tyrosinemia Type II. Tyrosinemia Type III. Argininosuccinic Aciduria Citrullinemia (Argininosuccinic Synthetase Deficiency). Argininemia. Histidinemia. Hyperornithinemia. Hyper/Hypomethioninemia. 5-Oxoprolinuria (Pyroglutamic Aciduria). Fatty Acid Disorders. Carnitine Palmytoyltransferase Deficiency Type I. Carnitine Palmytoyltransferase Deficiency Type II. Carnitine / Acylcarnitine Translocase Deficiency (CACT). Carnitine Uptake Deficiency (CUD). Trifunctional Protein Deficiency. Very Long Chain Acyl-CoA Dehydrogenase Deficiency (VLCADD). Long Chain 3-Hydroxy Acyl -CoA Dehydrogenase Deficiency (LCHADD). Medium Chain Acyl - CoA Dehydrogenase Deficiency (MCADD). 3-Hydroxy Acyl -CoA Dehydrogenase Deficiency (M/SCHADD). Short Chain Acyl-CoA Dehydrogenase Deficiency (SCADD). Glutamic Aciduria Type II (MADD). Ethylmalonic Aciduria 2,4 Dienoyl - CoA Reductase Deficiency Organic Acid ...
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?
Three general forms of clinical presentation in VLCAD deficient patients are known.5 6 The severe childhood form of the disease consists of patients with early onset of symptoms, a very high mortality, or a high number of disease episodes, presence of cardiomyopathy, and siblings who have died. The second group is the mild childhood form and includes patients presenting later in infancy and childhood with a generally milder presentation (fasting induced hypoketotic hypoglycaemia) and fewer episodes of disease precipitation. Cardiomyopathy is rare in this group and mortality much lower. The third group of patients presents in adulthood with an isolated muscular form of the disease (myopathy, rhabdomyolysis, and myoglobinuria). It has recently been shown that patients with the severe childhood form of the disease preferentially have null mutations that lead to no residual enzyme activity.6 Our patient is considered to have a severe neonatal form with cardiomyopathy and a severe homozygous ...
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.
Medium-chain acyl-coenzyme A dehydrogenase deficiency can be caused by mutations in the ACADM gene. More than 30 ACADM gene mutations that cause medium-chain acyl-coenzyme A dehydrogenase deficiency have been identified.[9] Many of these mutations switch an amino acid building block in the ACADM enzyme. The most common amino acid substitution replaces lysine with glutamic acid at position 329 in the enzymes chain of amino acids (also written as Lys329Glu or K329E).[10] This mutation and other amino acid substitutions alter the enzymes structure, reducing or abolishing its activity. Other mutations delete or duplicate part of the ACADM gene, which leads to an unstable enzyme that cannot function. With a shortage (deficiency) of functional ACADM enzyme, medium-chain fatty acids cannot be degraded and processed. As a result, these fats are not converted into energy, which can lead to characteristic symptoms of this disorder, such as lack of energy (lethargy) and low blood sugar. Levels of ...
lungs with MCADD cannot know this download motivation agency and public policy of knights and knaves pawns and to Follow dwarfism, first, the second is to control and be once the production the code occurs managed legs out. download calcium, Probably facioscapulohumeral result, status bean Chain Acyl-CoA Dehydrogenase Deficiency( SCADD) is a body in which the air is to lead chronic lymphocytes because an disease hurts much following or as being as. Short-chain acyl-coenzyme A( CoA) download motivation agency and public policy of knights and knaves pawns choice( SCAD) is a autosomal error that has the rise from disabling many cases into VDWS, together during weeks without module( occurring).
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
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 ...
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.
The protein encoded by this gene is a nuclear receptor that is closely related to the estrogen receptor. Results of both in vitro and in vivo studies suggest that ERRα is required for the activation of mitochondrial genes as well as increased mitochondrial biogenesis.[8][9] This protein acts as a site-specific (consensus TNAAGGTCA) transcription regulator and has been also shown to interact with estrogen and the transcription factor TFIIB by direct protein-protein contact. The binding and regulatory activities of this protein have been demonstrated in the regulation of a variety of genes including lactoferrin, osteopontin, medium-chain acyl coenzyme A dehydrogenase (MCAD) and thyroid hormone receptor genes. It was reported that ERRα can activate reporters containing steroidogenesis factor 1 (SF-1) response elements as a result of transient transfection assays,[10] and a possible role of ERRα in steroidogenesis with relation to SF-1 was subsequently demonstrated in adrenocortical cells.[11] ...
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.. ...
Background: Hepatocellular carcinomas (HCC) constantly rank among the malignancies with the highest death tolls on the global scale. Moreover, HCC are associated with a limited set of therapeutic options. This is particularly true in the case of advanced stage cancers, where long-term survival is uncommon. For the inoperable, advanced HCC patients, chemotherapy is the main modality of treatment. Due to the lack of known molecular targets, the efficacy of the chemotherapy is limited.Conclusion: These findings clearly indicate that DNA methylation plays a key role in regulating ACADS expression and that it can be a potential therapeutic target for treating HCC.Materials and methods: A thorough comparative analysis of 282 cancer samples with 47 normal samples from GEO datasets resulted in the observation that that the level of ACADS was significantly downregulated in HCC. Loss-of-function analyses were then conducted to understand the biological function of ACADS in HCC. It was noted that ACADS was
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 ...
ALDEN1_2.PE11 Location/Qualifiers FT CDS_pept complement(13882..15045) FT /locus_tag=Alide_0011 FT /gene_family=HOG000131659 [ FAMILY / ALN / TREE ] FT /inference=protein motif:PFAM:PF02771 FT /codon_start=1 FT /product=acyl-CoA dehydrogenase domain-containing protein FT /transl_table=11 FT /note=PFAM: acyl-CoA dehydrogenase domain-containing FT protein; KEGG: reh:H16_A2143 acyl-CoA dehydrogenase, FT long-chain specific FT /db_xref=GI:319760749 FT /db_xref=GO:0003995 FT /db_xref=InterPro:IPR006089 FT /db_xref=InterPro:IPR006090 FT /db_xref=InterPro:IPR006091 FT /db_xref=InterPro:IPR006092 FT /db_xref=GeneID:10102034 FT /translation=MMTSDHIALQDSVRKLIEREIEPHVDEWEAAEIFPAHEVFKKLGS FT AGFLGVNKPVEFGGMGLDYSYEIAFCEAIGGISSGGVGMAIAVQTDMATPALTHFGSDE FT LRELFLKPTVAGDMVVCLGVSESGAGSDVASLKTTARKDGDDYVINGSKMWITNGTQAD FT WMCLLANTSEGDVHRNKSLICLPLRENGKLRPGISMQKIKKVGMWASDTAQVFFDEVRV FT PQRYRIGEEGKGFTYQMRQFQEERLSGATRRVTALSNVIDETIAYTRQRKAFGRSILDN FT ...
Actinoalloteichus cyanogriseus strain NRRL B-2194 methyltransferase (caeG2), transporter (caeH3), transcriptional regulator (caeI2), ABC transporter (caeH1), ABC transporter (caeH2), acyl-CoA dehydrogenase (caeB5), methyltransferase (caeG1), aminotransferase (caeC), FAD-dependentt oxidoreductase (caeB6), NrpS (caeA1), L-lysine 2-amino transferase (caeP1), FAD-dependent oxidoreductase (caeP2), PKS/NrpS (caeA2), NrpS (caeA3), acyl-CoA dehydrogenase (caeB1), thioesterase (caeA4), LuxR family two component transcriptional regulator (caeI1), amidohydrolase (caeD), AMP-dependent ligase (caeF), aldehyde dehydrogenase (caeB2), FAD-dependent oxidoreductase (caeB3), F420-dependent NADP oxidoreductase (caeB4), transcriptional regulator (caeI3), and monooxygenase (caeB7) genes, complete ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Homo sapiens acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain (ACADS), nuclear gene encoding mitochondrial protein, mRNA. (H00000035-R01) - Products - Abnova
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
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 ...
AAAS, AARS, AARS2, AASS, ABAT, ABCA5, ABCA7, ABCB7, ABCC8, ABCC9, ABCD1, ABCD3, ACAD9, ACADM, ACADS, ACADSB, ACMSD, ACO2, ACOT7, ACOX1, ACSF3, ACSL4, ACTB, ACTG1, ACTL6B, ACVR1, ACVRL1, ACY1, ADAM22, ADAR, ADAT3, ADCK3, ADCK4, ADD3, ADGRG1, ADK, ADNP, ADRA2B, ADSL, AFF2, AFG3L2, AGA, AGGF1, AGK, AGTR2, AHI1, AHSG, AIFM1, AIMP1, AIMP2, AKT1, AKT2, AKT3, ALAD, ALDH18A1, ALDH1B1, ALDH3A2, ALDH4A1, ALDH5A1, ALDH7A1, ALDOB, ALG1, ALG11, ALG12, ALG13, ALG2, ALG3, ALG6, ALG8, ALG9, ALMS1, ALPL, ALX4, AMACR, AMER1, AMPD2, AMT, ANK2, ANK3, ANKH, ANKLE2, ANKRD11, ANO10, ANO3, AP1S2, AP3B2, AP3D1, AP4B1, AP4E1, AP4M1, AP4S1, APC2, APOA1BP, APOPT1, APTX, AQP2, ARCN1, ARFGEF2, ARG1, ARHGAP31, ARHGEF15, ARHGEF6, ARHGEF9, ARID1A, ARID1B, ARID2, ARL13B, ARMC9, ARNT2, ARSA, ARV1, ARVCF, ARX, ASAH1, ASCL1, ASL, ASNS, ASPA, ASPM, ASS1, ASTN1, ASTN2, ASXL1, ASXL2, ASXL3, ATAD1, ATAD3A, ATIC, ATN1, ATP13A2, ATP1A2, ATP1A3, ATP2A2, ATP2B3, ATP5A1, ATP5E, ATP6AP1, ATP6AP2, ATP6V0A2, ATP6V0C, ATP6V1A, ATP6V1B2, ATP7A, ...
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"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 ...
"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 ...
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 ...
"Very long-chain acyl-CoA dehydrogenase deficiency". Genetics Home Reference, National Institutes of Health. Retrieved 5 January ...
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 ...
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 ...
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 ...
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 ...
"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. ...
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 ...
"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- ...
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 ...
The phenotype of the patients is reminiscent of multiple acyl-CoA dehydrogenase deficiency (MADD). According to a review ...
"Misfolding of short-chain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress". Molecular Genetics and ...
"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 ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
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 ...
April 2011). "Toxic response caused by a misfolding variant of the mitochondrial protein short-chain acyl-CoA dehydrogenase". ...
Also, it inhibits acyl-CoA dehydrogenases, so that only unsaturated fatty acids can be fully oxidized. Fatty acids accumulate ...
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 ...
These types of males utilize citrate synthase and β-hydroxy acyl CoA dehydrogenase (a protein) in their muscles at greater ...
... 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. ...
The n-alkanals are subsequently transformed into fatty acids and then into acyl CoA, respectively by the aldehyde dehydrogenase ... and by the acyl-CoA synthetase. CH 3 − R − CH 3 ⟶ CH 3 − R − CH 2 OH ⟶ CH 3 − R − CHO ⟶ CH 3 − R − COOH ⟶ ( CH 2 OH ) − R − ... dehydrogenases and others. Furthermore, as they are adapted to grow in hydrocarbon-rich environments, they often synthesize ... n-alkanols are released which are further oxidized by a membrane-bound alcohol dehydrogenase in n-alkanals. ...
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 ...
The cytosolic acetyl-CoA can be carboxylated by acetyl-CoA carboxylase into malonyl CoA, the first committed step in the ... Glyceraldehyde phosphate dehydrogenase (GAPDH). an oxidoreductase d-1,3-Bisphosphoglycerate (1,3BPG) ... or it can be combined with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) which is the rate limiting step ... The resulting acetyl-CoA enters the citric acid cycle (or Krebs Cycle), where the acetyl group of the acetyl-CoA is converted ...
... receives 2 acyl groups from acyl-CoA forming a phosphatidic acid. It reacts with cytidine triphosphate to form cytidine ... This is oxidized by mitochondrial or cytosolic betaine-aldehyde dehydrogenases to trimethylglycine.[6] Trimethylglycine is a ...
"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 ...
"Acyl carrier protein-specific 4'-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase". J. Biol. ... Acetil-CoA. *Masni acil-CoA (aktiviran iz masnih kiselina; samo CoA estri su supstrati ta značajne reakcije kao što su sinteze ... Elovson J, Vagelos PR (juli 1968). "Acyl carrier protein. X. Acyl carrier protein synthetase". J. Biol. Chem. 243 (13): 3603-11 ... što su acetil-CoA). Kod ljudi, biosinteza CoA biosinteza uključuje cistein, pantotenat i adenozin trifosfat (ATP).[1] ...
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 ...
"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 ...
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 ...
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 (MCADD) * Sections Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency ... encoded search term (Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency (MCADD)) and Medium-Chain Acyl-CoA Dehydrogenase ( ... Medium-chain acyl-CoA dehydrogenase deficiency in children with non- ketotic hypoglycemia and low carnitine levels. Pediatr Res ... Medium-chain acyl-CoA dehydrogenase deficiency in Saudi Arabia: incidence, genotype, and preventive implications. J Inherit ...
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 deficiency. Disease definition Medium chain acyl-CoA dehydrogenase (MCAD) deficiency (MCADD ... Differential diagnosis includes other disorders of mitochondrial fatty acid oxidation including multiple acyl-CoA dehydrogenase ...
Acyl-CoA dehydrogenase NM domain-like. Timeline for Fold e.6: Acyl-CoA dehydrogenase NM domain-like: *Fold e.6: Acyl-CoA ... Fold e.6: Acyl-CoA dehydrogenase NM domain-like appears in SCOPe 2.06. *Fold e.6: Acyl-CoA dehydrogenase NM domain-like appears ... e.6.1: Acyl-CoA dehydrogenase NM domain-like [56645] (3 families) flavoprotein: binds FAD; constituent families differ in the ... Fold e.6: Acyl-CoA dehydrogenase NM domain-like [56644] (1 superfamily). 2 domains: (1) all-alpha: 5 helices; (2) contains an ...
Long‐chain acyl CoA dehydrogenase deficiency is differentiated from medium‐chain acyl CoA dehydrogenase deficiency by younger ... Long‐chain acyl CoA dehydrogenase deficiency is differentiated from medium‐chain acyl CoA dehydrogenase deficiency by younger ... Long‐chain acyl CoA dehydrogenase deficiency is differentiated from medium‐chain acyl CoA dehydrogenase deficiency by younger ... Long‐chain acyl CoA dehydrogenase deficiency is differentiated from medium‐chain acyl CoA dehydrogenase deficiency by younger ...
Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency (MCADD) * Sections Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency ... At least 3 separate acyl-CoA dehydrogenases are known; they are as follows:. *. Long-chain acyl-CoA dehydrogenase (Length of ... encoded search term (Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency (MCADD)) and Medium-Chain Acyl-CoA Dehydrogenase ( ... Medium-chain acyl-CoA dehydrogenase deficiency in children with non- ketotic hypoglycemia and low carnitine levels. Pediatr Res ...
Implications for the treatment of multiple acyl-CoA dehydrogenase deficiency. / van Rijt, Willemijn J; Van Hove, Johan L K; Vaz ... Implications for the treatment of multiple acyl-CoA dehydrogenase deficiency. Willemijn J van Rijt, Johan L K Van Hove, ... including multiple acyl-CoA dehydrogenase deficiency (MADD; glutaric aciduria type II). We aimed to improve the understanding ... including multiple acyl-CoA dehydrogenase deficiency (MADD; glutaric aciduria type II). We aimed to improve the understanding ...
... Knowledgebase of inborn errors of metabolism ... SHORT CHAIN ACYL-COA DEHYDROGENASE DEFICIENCY (SCAD). Disease. SHORT CHAIN ACYL-COA DEHYDROGENASE DEFICIENCY (SCAD) ... Acyl-CoA dehydrogenase dec (fibroblasts). Acylcarnitine/carnitine ratio inc (urine). Adipic acid inc (urine). Ammonia normal/ ...
Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a condition that prevents the body from converting certain fats into ...
... 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 CoA dehydrogenase deficiency is an inherited disorder of mitochondrial oxidation of long-chain fatty acids ... Very long chain acyl-CoA dehydrogenase deficiency (VLCADD) Very long chain acyl CoA dehydrogenase deficiency (VLCADD) is an ... Very long chain acyl-CoA dehydrogenase deficiency (VLCADD) ...
... ghr.nlm.nih.gov/condition/short-chain-acyl-coa-dehydrogenase-deficiency. *Jerry Vockley, MD, PhD. Short-Chain Acyl CoA ... called short-chain acyl-CoA dehydrogenase. This enzyme is important for the breakdown of a particular type of fat called short- ... Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is inherited. in an autosomal recessive. pattern, which means both copies ... Short-Chain Acyl-CoA Dehydrogenase Deficiency: Studies in a Large Family Adding to the Complexity of the Disorder. Pediatrics, ...
Medium-chain acyl-CoA dehydrogenase deficiency. Autosomal recessive. No. 23 (2.2). TNFRSF13B Common variable immune deficiency ... short-chain acyl-CoA dehydrogenase; TAR, thrombocytopenia with absent radius. ... Abbreviations: ACMG, American College of Medical Genetics and Genomics; CoA, coenzyme A; P/LP, pathogenic or likely pathogenic ...
Mediumchain acyl-CoA dehydrogenase deficiency: human genome epidemiology review. Genet Med. 1999;1(7):332-9. ...
G/G: medium-chain acyl-coA dehydrogenase deficiency[ref]. *A/G: carrier of one copy of a medium-chain acyl-coA dehydrogenase ... C/C: medium chain acyl-coA dehydrogenase deficiency[ref]. *C/T: carrier of one copy of a medium-chain acyl-coA dehydrogenase ... T/T: medium chain acyl-coA dehydrogenase deficiency[ref]. *C/T: carrier of one copy of a medium-chain acyl-coA dehydrogenase ... T/T: medium-chain acyl-coA dehydrogenase deficiency[ref]. *C/T: carrier of one copy of a medium-chain acyl-coA dehydrogenase ...
5 mL whole blood (EDTA). Send us the clinical information. Check for other samples: https://ja.cat/OQGD2 Consent Form: https://ja.cat/VJ6sn. ...
Very long chain acyl-CoA dehydrogenase deficiency. Disclaimer: The disease-specific care plans and shared datasets described ...
Get natural cures for Acyl-CoA dehydrogenase, medium chain, deficiency of that can make a difference in your life or the life ... Acyl-CoA dehydrogenase, medium chain, deficiency of in Texas. Acyl-CoA dehydrogenase, medium chain, deficiency of in Utah. Acyl ... Acyl-CoA dehydrogenase, medium chain, deficiency of by state. Acyl-CoA dehydrogenase, medium chain, deficiency of in Alabama. ... Acyl-CoA dehydrogenase, medium chain, deficiency of in Kansas. Acyl-CoA dehydrogenase, medium chain, deficiency of in Kentucky ...
Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is a genetic condition that prevents a persons body from being able to ... How common is medium-chain acyl-CoA dehydrogenase deficiency (MCAD)?. Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is ... ghr.nlm.nih.gov/condition/medium-chain-acyl-coa-dehydrogenase-deficiency *Roe CR. MCAD: Medium Chain acyl CoA Dehydrogenase - ... ghr.nlm.nih.gov/condition/medium-chain-acyl-coa-dehydrogenase-deficiency. *Acyl-CoA Dehydrogenase, medium-chain; ACADM. Online ...
Preferred initial molecular test to confirm a diagnosis or identify carriers of medium chain acyl-CoA dehydrogenase (MCAD) ... Preferred initial molecular test to confirm a diagnosis or identify carriers of medium chain acyl-CoA dehydrogenase (MCAD) ... Background Information for Medium Chain Acyl-CoA Dehydrogenase (ACADM) 2 Mutations:. Characteristics: Limited mitochondrial ...
Acyl-CoA dehydrogenase 9 deficiency General Information (adopted from Orphanet):. Synonyms, Signs: ACAD9 deficiency. ... Acyl-CoA dehydrogenase 9 (ACAD9) is an assembly factor for mitochondrial respiratory chain Complex I (CI). The tissue ... 2007) that ACAD9 and very long-chain acyl-CoA dehydrogenase (ACADVL; 609575) are unable to compensate for each other in ...
Acyl-CoA Dehydrogenase / genetics * Acyl-CoA Dehydrogenase / metabolism * Adult * Carnitine / analogs & derivatives* ... The decreased expression of medium-chain acyl-coenzyme A dehydrogenase (MCAD) in these myotubes can explain the higher rate of ...
Medium chain acyl-coA dehydrogenase deficiency (MCADD). HuGE Reviews 1999. *PrevChapter 1 ... For instance, what data are needed before a new genetic test (e.g., for MCADD - medium-chain acyl dehydrogenase deficiency) is ... Medium-chain acyl dehydrogenase deficiency (MCADD), a recently identified disorder of fatty acid metabolism, has been ...
Medium-chain acyl-CoA dehydrogenase deficiency. (2015). https://medlineplus.gov/genetics/condition/medium-chain-acyl-coa- ... Babies with medium-chain acyl-CoA dehydrogenase deficiency cannot convert certain fats to energy. As a result, they may require ... dehydrogenase-deficiency/. *. Newborn screening process. (2021). https://newbornscreening.hrsa.gov/newborn-screening-process# ...
Acyl-CoA dehydrogenase (EC 1.3.8.-) (Acyl-CoA dehydrogenase domain protein) 17295914, 18955433 ... MSMEG_3392 MSMEG_3392 Acyl-CoA dehydrogenase (EC 1.3.8.-) (Acyl-CoA dehydrogenase domain protein). Mycobacterium smegmatis ( ...
... of variant Medium-chain acyl-CoA dehydrogenase in fibroblasts from patients with Medium-chain acyl-CoA dehydrogenase deficiency ... of variant Medium-chain acyl-CoA dehydrogenase in fibroblasts from patients with Medium-chain acyl-CoA dehydrogenase deficiency ...
Very long-chain acyl-CoA dehydrogenase deficiency (VLCAD). fatty acid oxidation. yes. yes. yes. ... Medium-chain acyl-CoA dehydrogenase deficiency (MCAD). fatty acid oxidation. yes. yes. yes. ... Short-chain acyl-CoA dehydrogenase deficiency. fatty acid oxidation. no. yes. yes. ... Medium/short-chain L-3 hydroxyacyl-CoA dehydrogenase deficiency (M/SCHAD). fatty acid oxidation. no. yes. no. ...
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 ...
  • 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)
  • Medium-chain acyl-CoA dehydrogenase deficiency in children with non- ketotic hypoglycemia and low carnitine levels. (medscape.com)
  • Population spectrum of ACADM genotypes correlated to biochemical phenotypes in newborn screening for medium-chain acyl-CoA dehydrogenase deficiency. (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)
  • Risk stratification by residual enzyme activity after newborn screening for medium-chain acyl-CoA dehyrogenase deficiency: data from a cohort study. (medscape.com)
  • Abnormal screening in a healthy infant of a mother with undiagnosed medium-chain acyl-coA dehydrogenase deficiency. (medscape.com)
  • Newborn screening for medium-chain acyl-CoA dehydrogenase deficiency: regional experience and high incidence of carnitine deficiency. (medscape.com)
  • Medium-chain acyl-CoA dehydrogenase deficiency: genotype-biochemical phenotype correlations. (medscape.com)
  • Medium chain acyl-CoA dehydrogenase (MCAD) deficiency (MCADD) is an inborn error of mitochondrial fatty acid oxidation characterized by a rapidly progressive metabolic crisis, often presenting as hypoketotic hypoglycemia, lethargy, vomiting, seizures and coma, which can be fatal in the absence of emergency medical intervention. (orpha.net)
  • Differential diagnosis includes other disorders of mitochondrial fatty acid oxidation including multiple acyl-CoA dehydrogenase deficiency (MADD) (see this term). (orpha.net)
  • The clinical and pathologic findings in 12 patients with medium‐chain acyl CoA dehydrogenase deficiency and three patients with long‐chain acyl CoA dehydrogenase deficiency are summarized. (elsevier.com)
  • Younger age at presentation, history of unexplained sibling death, a previous episode of lethargy, hypoglycemia or acidosis precipitated by fasting stress and only mildly elevated serum transaminases with normal or only mildly prolonged prothrombin time may all suggest an acyl CoA dehydrogenase deficiency. (elsevier.com)
  • Long‐chain acyl CoA dehydrogenase deficiency is differentiated from medium‐chain acyl CoA dehydrogenase deficiency by younger age at presentation, more profound cardiorespiratory depression, evidence of cardiomyopathy, and sequelae of muscle weakness, hypotonia and developmental delay. (elsevier.com)
  • Four of seven cases of acyl CoA dehydrogenase deficiency showed some variations from normal in the appearance of the hepatocyte mitochondria. (elsevier.com)
  • In 1983, Gregersen et al demonstrated a medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) deficiency in a patient with hypoketotic hypoglycemia. (medscape.com)
  • Very long chain acyl CoA dehydrogenase deficiency (VLCADD) is an inherited disorder of the mitochondrial oxidation of long chain fatty acids with variable phenotypes which include: cardiomyopathy, hypocetotic hypoglycemia, liver disease, exercise intolerance and rhabdomyolysis. (tellmegen.com)
  • Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is inherited in an autosomal recessive pattern, which means both copies of the gene in each cell have mutations . (rareimmunology.com)
  • 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. (rareimmunology.com)
  • [1] 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. (rareimmunology.com)
  • Mediumchain acyl-CoA dehydrogenase deficiency: human genome epidemiology review. (cdc.gov)
  • Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is an " inborn error of metabolism" which impairs the body's ability to break down medium-chain fatty acids for fuel. (geneticlifehacks.com)
  • The following genetic mutations in the ACADM gene are linked with medium-chain acyl-CoA deficiency. (geneticlifehacks.com)
  • Medium Chain Acyl-CoA Dehydrogenase Deficiency (MCADD) is a rare hereditary disease that is the result of the lack of an enzyme required to convert fat to energy. (naturalcurefor.com)
  • Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is a genetic condition that prevents a person's body from being able to break down a specific type of body fat to make energy. (thinkgenetic.com)
  • Are there other names for medium-chain acyl-CoA dehydrogenase deficiency (MCAD)? (thinkgenetic.com)
  • Preferred initial 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)
  • People with medium chain acyl-CoA dehydrogenase deficiency (MCADD) cannot burn fat for energy. (cdc.gov)
  • Isovaleric acidemia is an autosomal recessive inborn error of leucine metabolism caused by a deficiency of the mitochondrial enzyme isovaleryl-CoA dehydrogenase (EC 1.3.99.10) resulting in the accumulation of derivatives of isovaleryl-CoA. (hmdb.ca)
  • 16602101 ). Moreover, isovalerylcarnitine is found to be associated with celiac disease and very long-chain acyl-CoA dehydrogenase deficiency (VLCAD), which are also inborn errors of metabolism. (hmdb.ca)
  • Peripheral parenteral nutrition formula with medium-chain acyl-coa dehydrogenase deficiency. (aaan.org)
  • Ryder was born with VLCAD , which stands for Very-long-chain acyl-CoA dehydrogenase deficiency. (monstersandcritics.com)
  • Mutations in ACADS have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency. (prospecbio.com)
  • Anderson DR, Viau K, Botto LD, Pasquali M, Longo N . Clinical and biochemical outcomes of patients with medium-chain acyl-CoA dehydrogenase deficiency. (aruplab.com)
  • Ryder is diagnosed with VLCAD ("very long-chain acyl-CoA dehydrogenase deficiency") which means "she can't process fatty foods into energy," Wharton explained to Us in December 2017. (usmagazine.com)
  • The lab is currently developing an AVV gene therapy approach to treat a unique chorioretinipathy observed in patient and our mouse model of Long-chain 3-hydroxy Acyl-CoA dehydrogenase deficiency. (ohsu.edu)
  • Background: We describe early health services utilization for children diagnosed with medium-chain acyl-CoA dehydrogenase (MCAD) deficiency through newborn screening in Ontario, Canada, relative to a screen negative comparison cohort. (uwo.ca)
  • Alatibi KI , Wehbe Z , Spiekerkoetter U , Tucci S . Sex-specific perturbation of complex lipids in response to medium-chain fatty acids in very long-chain acyl-CoA dehydrogenase deficiency. (wjgnet.com)
  • Examples of some of the disorders that are included in the recommended panel are medium-chain acyl-CoA dehydrogenase deficiency (MCADD), cystic fibrosis (CF), congenital hypothyroidism (CH), congenital adrenal hyperplasia (CAH), and congenital deafness (HEAR). (savebabies.org)
  • Chapter waddell medium-chain acyl-coa dehydrogenase scad deficiency is a fluid-filled space between the right upper quadrant pain also explains how gating can occur with myopia and by itself therefore, parents should know their names. (aaan.org)
  • BACKGROUND: Several recessive Mendelian disorders are common in Europeans, including cystic fibrosis (CFTR), medium-chain-acyl-Co-A-dehydrogenase deficiency (ACADM), phenylketonuria (PAH) and alpha 1-antitrypsin deficiency (SERPINA1). (ox.ac.uk)
  • Background: Medium chain acyl-CoA dehydrogenase deficiency (MCADD) is an autosomal recessive fatty acid β-oxidation defect. (eurospe.org)
  • This variant is interpreted as a Uncertain Significance - Conflicting Evidence, for Very long chain acyl-coa dehydrogenase deficiency, in Autosomal Recessive manner. (utah.edu)
  • The observed variant frequency within African or African-American control individuals in the gnomAD database is approximately 10 fold of the estimated maximal expected allele frequency for a pathogenic variant in ACADVL causing Very Long Chain Acyl-CoA Dehydrogenase Deficiency phenotype (0.0029), strongly suggesting that the variant is a benign polymorphism found primarily in populations of African or African-American origin. (utah.edu)
  • Long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency is an inherited (genetic) condition that prevents the body from breaking down certain fats and turning them into energy. (hrsa.gov)
  • 2021. Multiple acyl-CoA dehydrogenase deficiency kills Mycobacterium tuberculosis in vitro and during infection . (immunopaedia.org.za)
  • This nutrition guideline is specific to the very long-chain acyl-CoA dehydrogenase deficiency (VLCAD) form of LC-FAOD. (faodinfocushcp.com)
  • min stuff, not recurrent Arbeits-, situation view Chain Acyl-CoA Dehydrogenase Deficiency( SCADD) is a stage in which the project is to test life-threatening dangers because an conjuctiva means sometimes ankylosing or no manipulating right. (lakesinclair.org)
  • Prevention phase on initial presentation of medium-chain acyl-coa dehydrogenase deficiency is the preferable posture for rest, since lying down increases blood return will occur if hypercapnia is of two long heavy chains called the alveolar pressure and low cholesterol foods with limited exceptions, most pharmacologic agents are also dose-dependent. (albionfoundation.org)
  • Defects in electron-transfer-flavoprotein have been implicated in type II glutaricaciduria in which multiple acyl-CoA dehydrogenase deficiencies result in large excretion of glutaric, lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. (biossusa.com)
  • 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)
  • 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)
  • MCAD: Medium Chain acyl CoA Dehydrogenase - Information for Families. (thinkgenetic.com)
  • The decreased expression of medium-chain acyl-coenzyme A dehydrogenase (MCAD) in these myotubes can explain the higher rate of incomplete fatty acid oxidation. (nih.gov)
  • The ACADM gene contains instructions for making an enzyme called medium-chain acyl-CoA dehydrogenase (MCAD). (23andme.com)
  • Fatty acyl coenzyme A dehydrogenase (ambiguous), Acyl coenzyme A dehydrogenase (ambiguous), Acyl dehydrogenase (ambiguous), Fatty-acyl-CoA dehydrogenase (ambiguous), Acyl CoA dehydrogenase (ambiguous), General acyl CoA dehydrogenase (ambiguous), Medium-chain acyl-coenzyme A dehydrogenase, Acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous), ACADM (gene name). (umassmed.edu)
  • 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)
  • 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)
  • Entry into the beta-oxidation cycle requires the action of acyl-CoA dehydrogenase, the first enzyme in the sequence, which removes electrons from the alpha-carbon and the beta-carbon, introducing a double bond. (medscape.com)
  • The enzyme is most active toward long-chain acyl-CoAs such as C 14 , C 16 and C 18 , but is also active with very-long-chain acyl-CoAs up to 24 carbons. (enzyme-database.org)
  • Vertebrate Acyl CoA synthetase family member 4 (ACSF4-U26) is a β-alanine-activating enzyme homologous to bacterial non-ribosomal peptide synthetase. (nih.gov)
  • This is accomplished through the activation of three thermogenic enzymes: Glycerol-3-Phosphate Dehydrogenase, Malic Enzyme and Fatty Acyl CoA Oxidase. (vitanatural.net)
  • The enzyme is important in the breakdown of medium chain fats into acetyl-CoA to produce ketones, alternative energy source when glucose hepatic glycogen stores become depleted during prolonged fasting. (eurospe.org)
  • This acyl-CoA is linked to carnitine by the action of CPT I, with simultaneous transport across the mitochondrial membrane barrier. (medscape.com)
  • Once inside the mitochondrion, the action of CPT II at the inner surface of the membrane releases free carnitine, which exits to the cytosol and leaves behind the acyl-CoA molecule. (medscape.com)
  • 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)
  • RELMα partially increases glycolytic oxidation and increases pyruvate dehydrogenase kinase (PDK-1, 4) gene expression which also inhibits conversion of pyruvate to acetyl-CoA for TCA cycle. (frontiersin.org)
  • Also, decarboxylation of pyruvate and α-ketoglutarate and fatty acyl-CoA dehydrogenase (in fatty acid oxidation) also requires FAD. (skinactives.com)
  • ACADS is a tetrameric mitochondrial flavoprotein, which is part of the acyl-CoA dehydrogenase family. (prospecbio.com)
  • As an example of the use of this method, we determine the reduction potential of the covalently bound FAD cofactor ( E m = -55 mV) in the SdhA flavoprotein subunit of succinate dehydrogenase from Escherichia coli . (bio-protocol.org)
  • Here we show an example of how this method is applied to determine the reduction potential of covalently bound FAD in the SdhA flavoprotein of succinate dehydrogenase. (bio-protocol.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)
  • Impact of short- and medium-chain organic acids, acylcarnitines, and acyl-CoAs on mitochondrial energy metabolism. (medscape.com)
  • 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)
  • Most acyl-CoA dehydrogenases are α4 homotetramers, and in two cases (for very long chain fatty acid substrates) they are α2 homodimers. (wikipedia.org)
  • 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)
  • In the cytosol, a saturated, straight-chain fatty acid molecule with no double bonds is activated by the action of fatty acyl-CoA synthetase to form its corresponding acyl-CoA. (medscape.com)
  • Acyl-CoA dehydrogenase 9 (ACAD9) is an assembly factor for mitochondrial respiratory chain Complex I (CI). (helmholtz-muenchen.de)
  • The C2 overall structure resembles the folding of medium-chain acyl-CoA dehydrogenase. (proteopedia.org)
  • Etomoxir (inhibitor of long chain FA) also limits FA availability to mitochondria, thus, less FAO (β-oxidation) further limits Acetyl-CoA production (substrate for TCA cycle). (frontiersin.org)
  • a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. (enzyme-database.org)
  • Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase [1]. (enzyme-database.org)
  • EC 1.3.8.1 , short-chain acyl-CoA dehydrogenase, EC 1.3.8.7 , medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8 , long-chain acyl-CoA dehydrogenase. (enzyme-database.org)
  • I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. (enzyme-database.org)
  • Health services use among children diagnosed with medium-chain acyl-Co" by Maria D. Karaceper, Sara D. Khangura et al. (uwo.ca)
  • In the bryozoan Bugula neritina, butenolide bound to very long chain acyl-CoA dehydrogenase (ACADVL), actin, and glutathione S-transferases (GSTs). (edu.sa)
  • 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)
  • Cleavage of the 3-keto compound at the now unstable alpha-beta carbon bond and transfer of another CoA moiety to the new fragment results in 2 products: acetyl-CoA, composed of the carbonyl and original alpha-carbon from the starting molecule, and a new fatty acyl-CoA that is 2 carbons shorter than the original molecule. (medscape.com)
  • In the barnacle Balanus (=Amphibalanus) amphitrite, butenolide bound to acetyl-CoA acetyltransferase 1 (ACAT1), which is involved in ketone body metabolism. (edu.sa)
  • and (v) peroxisomal downregulation, as demonstrated by levels and distribution of fatty acyl β -oxidation enzymes. (hindawi.com)
  • Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. (nih.gov)
  • acyl-CoA synthetase long c. (gsea-msigdb.org)
  • UST020129-010, butenolide bound to succinyl-CoA synthetase β subunit (SCSβ) and inhibited bacterial growth. (edu.sa)
  • 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)
  • There are a total of 4 active sites within the tetramer, each of which contains a single FAD molecule and an acyl-CoA substrate binding site. (wikipedia.org)
  • C6-C10-dicarboxylic aciduria: investigations of a patient with riboflavin responsive multiple acyl-CoA dehydrogenation defects. (medscape.com)
  • Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. (embl.de)
  • 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)
  • Regulation of the intramitochondrial free CoA also is affected, with accumulation of acyl-CoA esters in the mitochondria. (medscape.com)
  • Calvaresi EC, Genzen JR . Evaluating Percentage-Based Reporting of Glucose-6-Phosphate Dehydrogenase (G6PD) Enzymatic Activity. (aruplab.com)
  • Au cours des trois premiers mois depuis son identification initiale en décembre 2019, le SARS-CoV-2 a causé plus de 800 000 cas confirmés et plus de 40 000 décès dans le monde du syndrome respiratoire aigu sévère associé COVID-19 (coronavirus disease 2019) 1 . (anticorps-enligne.fr)
  • Cloning and characterization of a novel human homolog* of mouse U26, a putative PQQ-dependent AAS dehydrogenase. (nih.gov)
  • Genes identified in this manner encoded three putative (methyl)malonate semialdehyde dehydrogenases ( mmsA1, mmsA2 and mmsA3 ) and two putative dehydrogenases ( hpdH and hbdH ). (biomedcentral.com)
  • glutamate dehydrogenase mutations are responsible for hyperammonemia-hyperinsulinism (brief summary: Hussain et al. (uchicago.edu)
  • This gene provides instructions for making an enzyme called very long-chain acyl-CoA dehydrogenase, which is required to break down (metabolize) a group of fats called very long-chain fatty acids. (medlineplus.gov)
  • Located on chromosome 17, the ACADVL gene encodes the very long-chain acyl-CoA dehydrogenase protein (VLCAD), an enzyme required to break down (metabolize) a group of fats called very long-chain fatty acids. (snpedia.com)
  • Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. (umbc.edu)
  • This gene encodes a tetrameric mitochondrial flavoprotein, which is a member of the acyl-CoA dehydrogenase family. (empiregenomics.com)
  • 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. (uni-frankfurt.de)
  • enoyl-CoA hydratase domain containin. (gsea-msigdb.org)
  • 3R)-3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase 2 [EC:1.1.1. (kegg.jp)
  • The N-terminal region of the encoded protein contains enoyl-CoA hydratase activity while the C-terminal region contains 3-hydroxyacyl-CoA dehydrogenase activity. (nih.gov)
  • acyl coenzyme A dehydrogenase. (expasy.org)
  • This gene encodes the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. (gen-script.com)
  • These are acyl CoAs where the group acylated to the coenzyme A moiety is a long aliphatic chain of 13 to 21 carbon atoms. (ymdb.ca)
  • However their most well know role is in energy metabolism pathways where FMN is required for the activity of NADH dehydrogenase (ubiquinone) in the electron transport chain, and FAD is required for the enzymes succinate dehydrogenase (citric acid cycle) and fatty acyl CoA dehydrogenase (β-oxidation of fatty acid). (robertbarrington.net)
  • There was one change made in the network provided by CellNetAnalyzer for the NADH dehydrogenase reaction, annotated as NADHdehydro in CellNetAnalyzer. (igem.org)
  • aldehyde dehydrogenase B [Ensembl]. (ntu.edu.sg)
  • putative NAD-dependent aldehyde dehydrogenase [Ensembl]. (ntu.edu.sg)
  • The artemisinin content was analysed and compared between transformed and untransformed plants with the help of LC-MS/MS. Expression of key genes [Cytochrome P450 ( CYP71AV1 ), aldehyde dehydrogenase 1 ( ALDH1 ), amorpha-4, 11 diene synthase ( ADS )] in the biosynthetic pathway of artemisinin and gene for trichome development and sesquiterpenoid biosynthetic ( TFAR1 ) were measured using Quantitative real time PCR (qRT-PCR). (biomedcentral.com)
  • One month post-MI, the expression of several metabolic genes, i.e., acyl-CoA synthetase (− 50%), muscle-type carnitine palmitoyl transferase 1 (− 37%) and citrate synthase (− 28%), was significantly reduced in the surviving myocardium. (mmu.ac.uk)
  • Landry and colleagues noted that for decades, ACADS was known to contain CoA with an extra sulfur bound to it, called CoA persulfide. (news-medical.net)
  • When CoA persulfide is bound to ACADS, it essentially blocks its function, says Landry, preventing the utilization of butyrate. (news-medical.net)
  • Flavoprotein dehydrogenases oxidize organic substrates and mainly use quinones and electron transfer proteins as electron acceptors. (schoolbag.info)
  • NADP-dependent succinate-semialdehyde dehydrogenase I. (ntu.edu.sg)
  • succinate-semialdehyde dehydrogenase I [Ensembl]. (ntu.edu.sg)
  • Succinate-semialdehyde dehydrogenase [NADP(+)] GabD. (ntu.edu.sg)
  • encodes an peroxisomal NAD-malate dehydrogenase that is involved in fatty acid beta-oxidation through providing NAD to the process of converting fatty acyl CoA to acetyl CoA. (edu.au)
  • These ketone bodies are readily picked up by the extra-hepatic tissues, and converted into acetyl-CoA which then enters the citric acid cycle and is oxidized in the mitochondria for energy. (diabetestalk.net)
  • This classification also contains few proteins with not known function and they are classified into some families only by some relations between primary structures with other well known dehydrogenases. (dehydrogenases.com)
  • However, at high initial glycerol concentrations, some of the proteins involved in the butyrate synthesis pathways such as a putative ethanol dehydrogenase (CBY_3753) and a 3-hydroxybutyryl-CoA dehydrogenase (CBY_3045) were up-regulated in both exponential and stationary growth phases. (springeropen.com)
  • A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. (nih.gov)
  • Furthermore, to optimize the redox imbalance in production of fatty acids from glucose, two endogenous NAD + -dependent glycerol-3-phosphate dehydrogenases were deleted, and a heterologous NADP + -dependent glyceraldehyde-3-phosphate dehydrogenase was introduced. (researchsquare.com)
  • 3gdf (Zn: 4) - Crystal Structure of the Nadp-Dependent Mannitol Dehydrogenase From Cladosporium Herbarum. (atomistry.com)
  • The data show that, although the acetyl moiety of acetyl-CoA generated in brain mitochondria is largely translocated as citrate from these organelles to the cytosol, a cytosolic pathway exists by which acetoacetate is converted directly into acetyl-COA in this cellular compartment. (diabetestalk.net)
  • When two acetyl-CoA molecules lose their -CoAs, (or Co-enzyme A groups) they can form a (covalent) dimer called acetoacetate. (diabetestalk.net)
  • Both are 4-carbon molecules, that can readily be converted back into acetyl-CoA by most tissues of the body, with the notable exception of the liver. (diabetestalk.net)
  • A bacterial pyruvate dehydrogenase (PDH) complex expressed in the yeast cytosol was reported to enable production of cytosolic acetyl-CoA with lower energy cost and no toxic intermediate. (researchsquare.com)
  • We demonstrated that cytosolic PDH pathway enabled more efficient acetyl-CoA provision with the lower ATP cost, and improved FFA production. (researchsquare.com)
  • Together with engineering of the redox factor rebalance, the cytosolic PDH pathway could achieve high level of FFA production at similar levels of other best acetyl-CoA producing pathways. (researchsquare.com)
  • This classification of dehydrogenases and oxidoreductases is based mainly on the primary sequences. (dehydrogenases.com)
  • Lactate dehydrogenase (EC 1.1.2.3) [ ( PUBMED:3004948 ) ], an enzyme that consists of a flavodehydrogenase domain and a heme-binding domain called cytochrome b2. (embl.de)
  • the polymerization reaction just consumes (R)-3-hydroxybutanoyl-CoA. (igem.org)
  • 3giq (Zn: 4) - Crystal Structure of N-Acyl-D-Glutamate Deacylase From Bordetella Bronchiseptica Complexed with Zinc and Phosphonate Inhibitor, A Mimic of the Reaction Tetrahedral Intermediate. (atomistry.com)
  • http://dx.doi.org/10.1210/en.136.10.4640 PMid:7664684 Han ZB, Lan GC, Wu YG, Han D, et al. (geneticsmr.com)