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.
Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.
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.
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)

Identity of heart and liver L-3-hydroxyacyl coenzyme A dehydrogenase. (1/341)

Rat heart and liver cDNAs for precursor of L-3-hydroxyacyl-CoA dehydrogenase have been cloned and sequenced. The results indicate that these different rat organs express identical dehydrogenases. Furthermore, pig heart mRNA for L-3-hydroxyacyl-CoA dehydrogenase precursor was amplified by reverse transcription-polymerase chain reaction, and all the cDNA clones were found to encode a precursor of liver L-3-hydroxyacyl-CoA dehydrogenase (X.-Y. He, S.-Y. Yang, Biochim. Biophys. Acta 1392 (1998) 119-126) but not the well-documented heart form of the dehydrogenase (K.G. Bitar et al., FEBS Lett. 116 (1980) 196-198). Sequencing data and other evidence establish that the pig, like the rat, has the same dehydrogenase in heart and liver. Since the size and structure of pig heart L-3-hydroxyacyl-CoA dehydrogenase are identical to the pig liver dehydrogenase, reports that relied on the published sequence of the pig heart dehydrogenase need to be re-evaluated. For example, the signature pattern of the L-3-hydroxyacyl-CoA dehydrogenase family is HXFXPX3MXLXE. Furthermore, the published crystal structure of the pig heart dehydrogenase that substantiated each subunit comprising 307 residues with a mercury-binding residue at position 204 (J.J. Birktoft et al., Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 8262-8266) must be re-examined in accordance with this revelation.  (+info)

High aerobic capacities in the skeletal muscles of pinnipeds: adaptations to diving hypoxia. (2/341)

The objective was to assess the aerobic capacity of skeletal muscles in pinnipeds. Samples of swimming and nonswimming muscles were collected from Steller sea lions (Eumetopias jubatus, n = 27), Northern fur seals (Callorhinus ursinus, n = 5), and harbor seals (Phoca vitulina, n = 37) by using a needle biopsy technique. Samples were either immediately fixed in 2% glutaraldehyde or frozen in liquid nitrogen. The volume density of mitochondria, myoglobin concentration, citrate synthase activity, and beta-hydroxyacyl-CoA dehydrogenase was determined for all samples. The swimming muscles of seals had an average total mitochondrial volume density per volume of fiber of 9.7%. The swimming muscles of sea lions and fur seals had average mitochondrial volume densities of 6.2 and 8.8%, respectively. These values were 1.7- to 2.0-fold greater than in the nonswimming muscles. Myoglobin concentration, citrate synthase activity, and beta-hydroxyacyl-CoA dehydrogenase were 1.1- to 2. 3-fold greater in the swimming vs. nonswimming muscles. The swimming muscles of pinnipeds appear to be adapted for aerobic lipid metabolism under the hypoxic conditions that occur during diving.  (+info)

Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC. (3/341)

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)

Dietary management of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD). A case report and survey. (4/341)

Current dietary management of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD; long-chain-(S)-3-hydroxyacyl-CoA:NAD+ oxido-reductase, EC 1.1.1.211) deficiency (LCHADD) is based on avoiding fasting, and minimizing energy production from long-chain fatty acids. We report the effects of various dietary manipulations on plasma and urinary laboratory values in a child with LCHADD. In our patient, a diet restricted to 9% of total energy from long-chain fatty acids and administration of 1.5 g medium-chain triglyceride oil per kg body weight normalized plasma acylcarnitine and lactate levels, but dicarboxylic acid excretion remained approximately ten times normal. Plasma docosahexaenoic acid (DHA, 22:6n-3) was consistently low over a 2-year period; DHA deficiency may be related to the development of pigmentary retinopathy seen in this patient population. We also conducted a survey of metabolic physicians who treat children with LCHADD to determine current dietary interventions employed and the effects of these interventions on symptoms of this disease. Survey results indicate that a diet low in long-chain fatty acids, supplemented with medium-chain triclyceride oil, decreased the incidence of hypoketotic hypoglycaemia, and improved hypotonia, hepatomegaly, cardiomyopathy, and lactic acidosis. However, dietary treatment did not appear to effect peripheral neuropathy, pigmentary retinopathy or myoglobinuria.  (+info)

Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase. (5/341)

Human brain short chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) was found to catalyze the oxidation of 17beta-estradiol and dihydroandrosterone as well as alcohols. Mitochondria have been demonstrated to be the proper location of this NAD+-dependent dehydrogenase in cells, although its primary structure is identical to an amyloid beta-peptide binding protein reportedly associated with the endoplasmic reticulum (ERAB). This fatty acid beta-oxidation enzyme was identified as a novel 17beta-hydroxysteroid dehydrogenase responsible for the inactivation of sex steroid hormones. The catalytic rate constant of the purified enzyme was estimated to be 0.66 min-1 with apparent Km values of 43 and 50 microM for 17beta-estradiol and NAD+, respectively. The catalytic efficiency of this enzyme for the oxidation of 17beta-estradiol was comparable with that of peroxisomal 17beta-hydroxysteroid dehydrogenase type 4. As a result, the human SCHAD gene product, a single-domain multifunctional enzyme, appears to function in two different pathways of lipid metabolism. Because the catalytic functions of human brain short chain L-3-hydroxyacyl-CoA dehydrogenase could weaken the protective effects of estrogen and generate aldehydes in neurons, it is proposed that a high concentration of this enzyme in brain is a potential risk factor for Alzheimer's disease.  (+info)

Absence of spontaneous peroxisome proliferation in enoyl-CoA Hydratase/L-3-hydroxyacyl-CoA dehydrogenase-deficient mouse liver. Further support for the role of fatty acyl CoA oxidase in PPARalpha ligand metabolism. (6/341)

Peroxisomes contain a classical L-hydroxy-specific peroxisome proliferator-inducible beta-oxidation system and also a second noninducible D-hydroxy-specific beta-oxidation system. We previously generated mice lacking fatty acyl-CoA oxidase (AOX), the first enzyme of the L-hydroxy-specific classical beta-oxidation system; these AOX-/- mice exhibited sustained activation of peroxisome proliferator-activated receptor alpha (PPARalpha), resulting in profound spontaneous peroxisome proliferation in liver cells. These observations implied that AOX is responsible for the metabolic degradation of PPARalpha ligands. In this study, the function of enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase (L-PBE), the second enzyme of this peroxisomal beta-oxidation system, was investigated by disrupting its gene. Mutant mice (L-PBE-/-) were viable and fertile and exhibited no detectable gross phenotypic defects. L-PBE-/- mice showed no hepatic steatosis and manifested no spontaneous peroxisome proliferation, unlike that encountered in livers of mice deficient in AOX. These results indicate that disruption of classical peroxisomal fatty acid beta-oxidation system distal to AOX step does not interfere with the inactivation of endogenous ligands of PPARalpha, further confirming that the AOX gene is indispensable for the physiological regulation of this receptor. The absence of appreciable changes in lipid metabolism also indicates that enoyl-CoAs, generated in the classical system in L-PBE-/- mice are diverted to D-hydroxy-specific system for metabolism by D-PBE. When challenged with a peroxisome proliferator, L-PBE-/- mice showed increases in the levels of hepatic mRNAs and proteins that are regulated by PPARalpha except for appreciable blunting of peroxisome proliferative response as compared with that observed in hepatocytes of wild type mice similarly treated. This blunting of peroxisome proliferative response is attributed to the absence of L-PBE protein in L-PBE-/- mouse liver, because all other proteins are induced essentially to the same extent in both wild type and L-PBE-/- mice.  (+info)

Unique multifunctional HSD17B4 gene product: 17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase/hydratase involved in Zellweger syndrome. (7/341)

Six types of human 17beta-hydroxysteroid dehydrogenases catalyzing the conversion of estrogens and androgens at position C17 have been identified so far. The peroxisomal 17beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD 4, gene name HSD17B4) catalyzes the oxidation of estradiol with high preference over the reduction of estrone. The highest levels of 17beta-HSD 4 mRNA transcription and specific activity are found in liver and kidney followed by ovary and testes. A 3 kb mRNA codes for an 80 kDa (737 amino acids) protein featuring domains which are not present in the other 17beta-HSDs. The N-terminal domain of 17beta-HSD 4 reveals only 25% amino acid similarity with the other types of 17beta-HSDs. The 80 kDa protein is N-terminally cleaved to a 32 kDa enzymatically active fragment. Both the 80 kDa and the N-terminal 32 kDa (amino acids 1-323) protein are able to perform the dehydrogenase reaction not only with steroids at the C17 position but also with D-3-hydroxyacyl-coenzyme A (CoA). The enzyme is not active with L-stereoisomers. The central part of the 80 kDa protein (amino acids 324-596) catalyzes the 2-enoyl-acyl-CoA hydratase reaction with high efficiency. The C-terminal part of the 80 kDa protein (amino acids 597-737) facilitates the transfer of 7-dehydrocholesterol and phosphatidylcholine between membranes in vitro. The HSD17B4 gene is stimulated by progesterone, and ligands of PPARalpha (peroxisomal proliferator activated receptor alpha) such as clofibrate, and is down-regulated by phorbol esters. Mutations in the HSD17B4 lead to a fatal form of Zellweger syndrome.  (+info)

A fetal fatty-acid oxidation disorder as a cause of liver disease in pregnant women. (8/341)

BACKGROUND: Acute fatty liver of pregnancy and the HELLP syndrome (hemolysis, elevated liver-enzyme levels, and a low platelet count) are serious hepatic disorders that may occur during pregnancy in women whose fetuses are later found to have a deficiency of long-chain 3-hydroxyacyl-coenzyme A (CoA) dehydrogenase. This enzyme resides in the mitochondrial trifunctional protein, which also contains the active site of long-chain 2,3-enoyl-CoA hydratase and long-chain 3-ketoacyl-CoA thiolase. We undertook this study to determine the relation between mutations in the trifunctional protein in infants with defects in fatty-acid oxidation and acute liver disease during pregnancy in their mothers. METHODS: In 24 children with 3-hydroxyacyl-CoA dehydrogenase deficiency, we used DNA amplification and nucleotide-sequence analyses to identify mutations in the alpha subunit of the trifunctional protein. We then correlated the results with the presence of liver disease during pregnancy in the mothers. RESULTS: Nineteen children had a deficiency only of long-chain 3-hydroxyacyl-CoA dehydrogenase and presented with hypoketotic hypoglycemia and fatty liver. In eight children, we identified a homozygous mutation in which glutamic acid at residue 474 was changed to glutamine. Eleven other children were compound heterozygotes, with this mutation in one allele of the alpha-subunit gene and a different mutation in the other allele. While carrying fetuses with the Glu474Gln mutation, 79 percent of the heterozygous mothers had fatty liver of pregnancy or the HELLP syndrome. Five other children, who presented with neonatal dilated cardiomyopathy or progressive neuromyopathy, had complete deficiency of the trifunctional protein (loss of activity of all three enzymes). None had the Glu474Gln mutation, and none of their mothers had liver disease during pregnancy. CONCLUSIONS: Women with acute liver disease during pregnancy may have a Glu474Gln mutation in long-chain hydroxyacyl-CoA dehydrogenase. Their infants are at risk for hypoketotic hypoglycemia and fatty liver.  (+info)

3-Hydroxyacyl CoA Dehydrogenases (3-HADs) are a group of enzymes that play a crucial role in the beta-oxidation of fatty acids. These enzymes catalyze the third step of the beta-oxidation process, which involves the oxidation of 3-hydroxyacyl CoA to 3-ketoacyl CoA. This reaction is an essential part of the energy-generating process that occurs in the mitochondria of cells and allows for the breakdown of fatty acids into smaller molecules, which can then be used to produce ATP, the primary source of cellular energy.

There are several different isoforms of 3-HADs, each with specific substrate preferences and tissue distributions. The most well-known isoform is the mitochondrial 3-hydroxyacyl CoA dehydrogenase (M3HD), which is involved in the oxidation of medium and long-chain fatty acids. Other isoforms include the short-chain 3-hydroxyacyl CoA dehydrogenase (SCHAD) and the long-chain 3-hydroxyacyl CoA dehydrogenase (LCHAD), which are involved in the oxidation of shorter and longer chain fatty acids, respectively.

Deficiencies in 3-HADs can lead to serious metabolic disorders, such as 3-hydroxyacyl-CoA dehydrogenase deficiency (3-HAD deficiency), which is characterized by the accumulation of toxic levels of 3-hydroxyacyl CoAs in the body. Symptoms of this disorder can include hypoglycemia, muscle weakness, cardiomyopathy, and developmental delays. Early diagnosis and treatment of 3-HAD deficiency are essential to prevent serious complications and improve outcomes for affected individuals.

Acyl-CoA dehydrogenases are a group of enzymes that play a crucial role in the body's energy production process. They are responsible for catalyzing the oxidation of various fatty acids, which are broken down into smaller molecules called acyl-CoAs in the body.

More specifically, acyl-CoA dehydrogenases facilitate the removal of electrons from the acyl-CoA molecules, which are then transferred to coenzyme Q10 and eventually to the electron transport chain. This process generates energy in the form of ATP, which is used by cells throughout the body for various functions.

There are several different types of acyl-CoA dehydrogenases, each responsible for oxidizing a specific type of acyl-CoA molecule. These include:

* Very long-chain acyl-CoA dehydrogenase (VLCAD), which oxidizes acyl-CoAs with 12 to 20 carbon atoms
* Long-chain acyl-CoA dehydrogenase (LCAD), which oxidizes acyl-CoAs with 14 to 20 carbon atoms
* Medium-chain acyl-CoA dehydrogenase (MCAD), which oxidizes acyl-CoAs with 6 to 12 carbon atoms
* Short-chain acyl-CoA dehydrogenase (SCAD), which oxidizes acyl-CoAs with 4 to 8 carbon atoms
* Isovaleryl-CoA dehydrogenase, which oxidizes isovaleryl-CoA, a specific type of branched-chain acyl-CoA molecule

Deficiencies in these enzymes can lead to various metabolic disorders, such as medium-chain acyl-CoA dehydrogenase deficiency (MCADD) or long-chain acyl-CoA dehydrogenase deficiency (LCADD), which can cause symptoms such as hypoglycemia, muscle weakness, and developmental delays.

Acyl-CoA dehydrogenase is a group of enzymes that play a crucial role in the body's energy production process. Specifically, they are involved in the breakdown of fatty acids within the cells.

More technically, acyl-CoA dehydrogenases catalyze the removal of electrons from the thiol group of acyl-CoAs, forming a trans-double bond and generating FADH2. This reaction is the first step in each cycle of fatty acid beta-oxidation, which occurs in the mitochondria of cells.

There are several different types of acyl-CoA dehydrogenases, each specific to breaking down different lengths of fatty acids. For example, very long-chain acyl-CoA dehydrogenase (VLCAD) is responsible for breaking down longer chain fatty acids, while medium-chain acyl-CoA dehydrogenase (MCAD) breaks down medium-length chains.

Deficiencies in these enzymes can lead to various metabolic disorders, such as MCAD deficiency or LC-FAOD (long-chain fatty acid oxidation disorders), which can cause symptoms like vomiting, lethargy, and muscle weakness, especially during periods of fasting or illness.

Lipid A is the biologically active component of lipopolysaccharides (LPS), which are found in the outer membrane of Gram-negative bacteria. It is responsible for the endotoxic activity of LPS and plays a crucial role in the pathogenesis of gram-negative bacterial infections. Lipid A is a glycophosphatidylinositol (GPI) anchor, consisting of a glucosamine disaccharide backbone with multiple fatty acid chains and phosphate groups attached to it. It can induce the release of proinflammatory cytokines, fever, and other symptoms associated with sepsis when introduced into the bloodstream.

Acyltransferases are a group of enzymes that catalyze the transfer of an acyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydrogen atom) from one molecule to another. This transfer involves the formation of an ester bond between the acyl group donor and the acyl group acceptor.

Acyltransferases play important roles in various biological processes, including the biosynthesis of lipids, fatty acids, and other metabolites. They are also involved in the detoxification of xenobiotics (foreign substances) by catalyzing the addition of an acyl group to these compounds, making them more water-soluble and easier to excrete from the body.

Examples of acyltransferases include serine palmitoyltransferase, which is involved in the biosynthesis of sphingolipids, and cholesteryl ester transfer protein (CETP), which facilitates the transfer of cholesteryl esters between lipoproteins.

Acyltransferases are classified based on the type of acyl group they transfer and the nature of the acyl group donor and acceptor molecules. They can be further categorized into subclasses based on their sequence similarities, three-dimensional structures, and evolutionary relationships.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

L-hydroxyacyl-CoA dehydrogenase 3beta-hydroxyacyl coenzyme A dehydrogenase beta-hydroxy acid dehydrogenase beta-hydroxyacyl CoA ... dehydrogenase beta-hydroxyacyl dehydrogenase beta-hydroxyacyl-coenzyme A synthetase beta-hydroxyacylcoenzyme A dehydrogenase ... beta-Hydroxyacyl coenzyme A dehydrogenase". The Journal of Biological Chemistry. 207 (2): 631-8. doi:10.1016/S0021-9258(18) ... Hydroxyacyl-Coenzyme A dehydrogenase HSD17B10 - 3-Hydroxyacyl-CoA dehydrogenase type-2 EHHADH - Peroxisomal bifunctional enzyme ...
... is a rare condition that prevents the body from converting certain fats to ... People with 3-hydroxyacyl-coenzyme A dehydrogenase deficiency have inadequate levels of an enzyme required for a step that ... Problems related to 3-hydroxyacyl-coenzyme A dehydrogenase deficiency can be triggered by periods of fasting or by illnesses ... Individuals with 3-hydroxyacyl-coenzyme A dehydrogenase deficiency are also at risk for complications such as seizures, life- ...
... such that HIV-1 Vpr regulates mitochondrial respiration and enhances the activity of hydroxyacyl-CoA dehydrogenase (HADH) ... Hydroxyacyl-Coenzyme A dehydrogenase (HADH) is an enzyme which in humans is encoded by the HADH gene. The HADH gene is located ... Craig I, Tolley E, Bobrow M (1976). "A preliminary analysis of the segregation of human hydroxyacyl coenzyme A dehydrogenase in ... "Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Molven A, Matre ...
SCARB2 Acyl-CoA dehydrogenase, long chain, deficiency of; 201460; ACADL Acyl-CoA dehydrogenase, medium chain, deficiency of; ... PC Pyruvate dehydrogenase deficiency; 312170; PDHA1 Pyruvate dehydrogenase E2 deficiency; 245348; DLAT Pyruvate dehydrogenase ... ACADM Acyl-CoA dehydrogenase, short chain, deficiency of; 201470; ACADS Adenocarcinoma of lung, response to tyrosine kinase ... DCX Succinic semialdehyde dehydrogenase deficiency; 271980; ALDH5A1 Succinyl-CoA:3-oxoacid CoA transferase deficiency; 245050; ...
Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri- ... An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA ... 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 ...
HSD17B4 "EHHADH enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase [ Homo sapiens (human) ]". NCBI. 6 September 2017. ... v t e (Protein pages needing a picture, Genes on human chromosome 3, Human gene pages with Wikidata item, All stub articles, ...
CoA) dehydrogenase, which is part of a protein complex known as mitochondrial trifunctional protein. Long-chain fatty acids ... Medium chain acyl dehydrogenase deficiency Reference, Genetics Home. "LCHAD deficiency". Genetics Home Reference. Retrieved ... Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency is a rare autosomal recessive fatty acid oxidation disorder that ... Mutations in the HADHA gene lead to inadequate levels of an enzyme called long-chain 3-hydroxyacyl-coenzyme A ( ...
"Entrez Gene: Hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit ... "hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit". Cardiac ... Trifunctional enzyme subunit alpha, mitochondrial also known as hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA ... The enzyme converts medium- and long-chain 2-enoyl-CoA compounds into the following 3-ketoacyl-CoA when NAD is solely present, ...
Beta oxidation of acyl-CoA occurs in four steps. 1. Acyl-CoA dehydrogenase catalyzes dehydrogenation of the acyl-CoA, creating ... The latter conversion is mediated by acyl-CoA synthase" acyl-P + HS-CoA → acyl-S-CoA + Pi + H+ Three types of acyl-CoA ... Acetyl-CoA Beta oxidation Coenzyme A Acyl CoA dehydrogenase Fatty acid metabolism Talley, Jacob T.; Mohiuddin, Shamim S. (2020 ... A rare disease called multiple acyl-CoA dehydrogenase deficiency (MADD) is a fatty acid metabolism disorder. Acyl-CoA is ...
"Disorders of mitochondrial fatty acyl-CoA beta-oxidation" (PDF). Journal of Inherited Metabolic Disease. 22 (4): 442-487. doi: ... Deficiency of LCHAD (3-hydroxyacyl-CoA dehydrogenase) leads to an accumulation of medium and long chain fatty acids. When this ... It is thought to be caused by a disordered metabolism of fatty acids by mitochondria in the fetus, caused by long-chain 3- ... hydroxyacyl-coenzyme A dehydrogenase deficiency. This leads to decreased metabolism of long chain fatty acids by the feto- ...
108 (3): 457-465. doi:10.1172/jci200111294. PMC 209352. PMID 11489939. Dunne, Mark J.; Kane, Charlotte; Shepherd, Ruth M.; ... Butler, Patrick (3 August 2001). "Call to establish children's commissioner". Guardian News and Media Limited. The Guardian. ... Wardrop, Murray (3 February 2010). "'Britain is one of world's most unfriendly countries towards children'". Telegraph Media ... Retrieved 3 November 2018. The National Service Framework for Children, Young People and Maternity Services - Emerging findings ...
... is not an appropriate substrate for acyl CoA dehydrogenase, or enoyl CoA hydratase: If the acyl CoA contains a cis-Δ3 bond, ... This is catalyzed by acyl CoA dehydrogenase to produce trans-delta 2-enoyl CoA. It uses FAD as an electron acceptor and it is ... The overall reaction for one cycle of beta oxidation is: Cn-acyl-CoA + FAD + NAD+ + H 2O + CoA → Cn-2-acyl-CoA + FADH 2 + NADH ... The final cycle produces two separate acetyl CoAs, instead of one acyl CoA and one acetyl CoA. For every cycle, the Acyl CoA ...
"OMIM Entry - * 600890 - HYDROXYACYL-CoA DEHYDROGENASE/3-KETOACYL-CoA THIOLASE/ENOYL-CoA HYDRATASE, ALPHA SUBUNIT; HADHA". omim. ... "HADHA hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit [Homo ... "Long-Chain Acyl CoA Dehydrogenase Deficiency: Background, Pathophysiology, Epidemiology". eMedicine. 24 March 2016. Retrieved ... Avoiding factors that might precipitate condition Glucose Low fat/high carbohydrate nutrition Long-chain acyl-CoA dehydrogenase ...
... protein is predicted to interact highly with enoyl-CoA hydratase and hydroxyacyl-CoA dehydrogenase, based on textmining ... Other predicted interacting proteins are acetyl-CoA carboxylases A and B, glycine dehydrogenase, 3-oxoacid CoA transferase 2. ... Three common missense mutations occur in the 3' UTR and in the coding sequence which change serine to leucine in the protein. ... O-linked glycosylation is predicted to occur at 3 sites toward the C-terminus. These sites are well-conserved in all homologs. ...
"Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity ... 17beta-hydroxysteroid dehydrogenase 10 is a member of the short-chain dehydrogenase/reductase superfamily. This homotetrameric ... He XY, Yang YZ, Schulz H, Yang SY (Jan 2000). "Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of ... "Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl- ...
The dehydrogenase activity of enoyl-CoA occurs in the carboxyl-terminal. Upon further investigation of the CoA binding site on ... delta2-Enoyl-CoA Isomerase and Peroxisomal Multifunctional delta3,delta2- Enoyl-CoA Isomerase, 2-Enoyl-CoA Hydratase, 3- ... Hydroxyacyl-CoA Dehydrogenase Enzyme in Rat Liver" (PDF). Journal of Biological Chemistry. 266 (17): 10750-10753. doi:10.1016/ ... Enoyl-CoA-(∆) isomerase (EC 5.3.3.8, also known as dodecenoyl-CoA-(∆) isomerase, 3,2-trans-enoyl-CoA isomerase, ∆3(cis),∆2( ...
"Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional ... acyl-CoA oxidase (see, e.g., ACOX1, MIM 609751); the 'D-bifunctional enzyme,' with enoyl-CoA hydratase and D-3-hydroxyacyl-CoA ... van Grunsven EG, Mooijer PA, Aubourg P, Wanders RJ (August 1999). "Enoyl-CoA hydratase deficiency: identification of a new type ... It was first identified as a 17-beta-estradiol dehydrogenase (Leenders et al., 1996; van Grunsven et al., 1998). Peroxisomal ...
Estradiol 17-beta-dehydrogenase 12 is an enzyme that in humans is encoded by the HSD17B12 gene. The enzyme 17-beta ... Luu-The V, Tremblay P, Labrie F (2006). "Characterization of type 12 17beta-hydroxysteroid dehydrogenase, an isoform of type 3 ... "Entrez Gene: HSD17B12 hydroxysteroid (17-beta) dehydrogenase 12". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method ... 2006). "Systemic distribution and tissue localizations of human 17beta-hydroxysteroid dehydrogenase type 12". J. Steroid ...
... hydroxyacyl coenzyme-A dehydrogenase, NADP+-linked acetoacetyl CoA reductase, NADPH:acetoacetyl-CoA reductase, D(−)-beta- ... hydroxybutyryl CoA-NADP+ oxidoreductase, short chain beta-ketoacetyl(acetoacetyl)-CoA reductase, beta-ketoacyl-CoA reductase, D ... In enzymology, an acetoacetyl-CoA reductase (EC 1.1.1.36) is an enzyme that catalyzes the chemical reaction (R)-3-hydroxyacyl- ... CoA + NADP+ ⇌ {\displaystyle \rightleftharpoons } 3-oxoacyl-CoA + NADPH + H+ Thus, the two substrates of this enzyme are (R)-3- ...
... (EC 1.3.8.1, butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase, butyryl dehydrogenase, ... Acyl-CoA dehydrogenase Medium-chain acyl-CoA dehydrogenase Butyryl-CoA (also known as butanoyl-CoA) Mahler HR (January 1954). " ... butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl ... Short-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ...
"Long-Chain Acyl CoA Dehydrogenase Deficiency: eMedicine Pediatrics: Genetics and Metabolic Disease". Retrieved 2009-07-11. Wang ... CoA) hydratase, long-chain 3-hydroxy acyl-coenzyme A dehydrogenase and long-chain 3-ketoacyl CoA thiolase. Fatty acid beta- ...
4 Dienoyl-CoA Reductase Deficiency Electron Transfer Flavoprotein (ETF) Dehydrogenase Deficiency (GAII & MADD) 3-Hydroxy-3- ... methylglutaryl-CoA lyase deficiency (HMG deficiency) Very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCAD deficiency ... Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD deficiency) Short-chain acyl-coenzyme A dehydrogenase deficiency ( ... 3-hydroxyacyl-coenzyme A dehydrogenase deficiency (M/SCHAD deficiency) The term fatty acid oxidation disorder (FAOD) is ...
11 beta hydroxysteroid dehydrogenase type 2 deficiency 17 alpha hydroxylase deficiency 17 beta hydroxysteroide dehydrogenase ... 2-Methylacetoacetyl CoA thiolase deficiency, rare (NIH) 2,8 dihydroxy-adenine urolithiasis 21 hydroxylase deficiency 22q11.2 ... coa hydratase deficiency 3-hydroxy 3-methyl glutaryl-coa lyase deficiency 3-hydroxyacyl-coa dehydrogenase deficiency 3-M ... deficiency 17-beta-hydroxysteroid dehydrogenase deficiency, rare (NIH) 17q21.31 microdeletion syndrome 18-Hydroxylase ...
Dehydrogenation by acyl-CoA dehydrogenase, yielding 1 FADH2 Hydration by enoyl-CoA hydratase Dehydrogenation by 3-hydroxyacyl- ... Acetyl-CoA is formed into malonyl-CoA by acetyl-CoA carboxylase, at which point malonyl-CoA is destined to feed into the fatty ... The propionyl-CoA is later converted into succinyl-CoA through biotin-dependant propionyl-CoA carboxylase (PCC) and Vitamin B12 ... CoA dehydrogenase, yielding 1 NADH + H+ Cleavage by thiolase, yielding 1 acetyl-CoA and a fatty acid that has now been ...
... hypoglycaemia Levomepromazine Liver cancer Liver glycogen synthase deficiency Long-chain hydroxyacyl-CoA dehydrogenase ... Trimethoprim Triple A syndrome Tumors Tyrosinaemia type 1 Urea cycle disorder Uremia Very-long-chain acyl-CoA dehydrogenase ... Reye syndrome Ritonavir Saquinavir Sepsis Septic shock Severe hepatitis Sheehan syndrome Short-chain acyl-CoA dehydrogenase ... deficiency Maple syrup urine disease Mcquarrie type infantile idiopathic hypoglycemia Medium chain acyl-CoA dehydrogenase ...
... glutaryl-CoA dehydrogenase (ETF) EC 1.3.8.7: medium-chain acyl-CoA dehydrogenase EC 1.3.8.8: long-chain acyl-CoA dehydrogenase ... butyryl-CoA dehydrogenase. EC 1.3.99.3: now EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA ... benzylsuccinyl-CoA dehydrogenase EC 1.3.8.4: isovaleryl-CoA dehydrogenase EC 1.3.8.5: 2-methyl-branched-chain-enoyl-CoA ... 4-dicarboxylate dehydrogenase EC 1.3.1.62: pimeloyl-CoA dehydrogenase EC 1.3.1.63: Now EC 1.21.1.2, 2,4-dichlorobenzoyl-CoA ...
... deficiency of subtypes of acyl CoA dehydrogenase (LCAD, SCAD, MCAD, VLCAD, 3-hydroxyacyl-coenzyme A dehydrogenase deficiency), ... Elevated concentrations of the enzyme lactate dehydrogenase (LDH) may be detected. Other markers of muscle damage, such as ... glucose-6-phosphate dehydrogenase deficiency, myoadenylate deaminase deficiency and muscular dystrophies Damage to skeletal ... thiolase deficiency Mitochondrial myopathies: deficiency of succinate dehydrogenase, cytochrome c oxidase and coenzyme Q10 ...
... namely acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and thiolase. The cycle produces a new ... It regulates through the ratio of acetyl-CoA versus CoA. Increased concentration of acetyl-CoA activates PDK. Acetyl-CoA is ... Acetyl-CoA can be carboxylated in the cytosol by acetyl-CoA carboxylase, giving rise to malonyl-CoA, a substrate required for ... "Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios". Biochemical and Biophysical ...
"Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ... which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. The encoded protein can also bind ... Middleton B (1994). "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase ... acetyl-CoA acyltransferase, or beta-ketothiolase is an enzyme that in humans is encoded by the HADHB gene. HADHB is a subunit ...
The process of beta oxidation requires the following enzymes: acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA ... The diagram to the left shows how fatty acids are converted into acetyl-CoA. The overall net reaction, using palmitoyl-CoA (16: ... The resulting acyl-CoA cross the mitochondria membrane and enter the process of beta oxidation. The main products of the beta ... Long chain fatty acids (more than 14 carbon) need to be converted to fatty acyl-CoA in order to pass across the mitochondria ...
L-hydroxyacyl-CoA dehydrogenase 3beta-hydroxyacyl coenzyme A dehydrogenase beta-hydroxy acid dehydrogenase beta-hydroxyacyl CoA ... dehydrogenase beta-hydroxyacyl dehydrogenase beta-hydroxyacyl-coenzyme A synthetase beta-hydroxyacylcoenzyme A dehydrogenase ... beta-Hydroxyacyl coenzyme A dehydrogenase". The Journal of Biological Chemistry. 207 (2): 631-8. doi:10.1016/S0021-9258(18) ... Hydroxyacyl-Coenzyme A dehydrogenase HSD17B10 - 3-Hydroxyacyl-CoA dehydrogenase type-2 EHHADH - Peroxisomal bifunctional enzyme ...
3-hydroxyacyl-CoA dehydrogenase deficiency is an inherited condition that prevents the body from converting certain fats to ... Role of short-chain hydroxyacyl CoA dehydrogenases in SCHAD deficiency. Biochem Biophys Res Commun. 2008 Mar 28;368(1):6-11. ... Short-chain hydroxyacyl-coenzyme A dehydrogenase deficiency presenting as unexpected infant death: A family study. J Pediatr. ... Problems related to 3-hydroxyacyl-CoA dehydrogenase deficiency can be triggered by periods of fasting or by illnesses such as ...
The other 2 activities of the protein are 2-enoyl coenzyme A (CoA) hydratase (LCEH) and long-chain 3-ketoacyl CoA thiolase ( ... Long-chain 3-hydroxy acyl-coenzyme A dehydrogenase (LCHAD) is 1 of 3 enzymatic activities that make up the trifunctional ... Schematic demonstrating mitochondrial fatty acid beta-oxidation and effects of long-chain acyl CoA dehydrogenase deficiency ( ... Schematic demonstrating mitochondrial fatty acid beta-oxidation and effects of long-chain acyl CoA dehydrogenase deficiency ( ...
Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+.. ...
Earlier diagnosis and strict diets improve the survival rate and clinical course of long-chain 3-hydroxyacyl-CoA dehydrogenase ... Earlier diagnosis and strict diets improve the survival rate and clinical course of long-chain 3-hydroxyacyl-CoA dehydrogenase ... title = "Earlier diagnosis and strict diets improve the survival rate and clinical course of long-chain 3-hydroxyacyl-CoA ... Earlier diagnosis and strict diets improve the survival rate and clinical course of long-chain 3-hydroxyacyl-CoA dehydrogenase ...
TFP has three enzymatic activities - long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA dehydrogenase, and long-chain ... Long-chain hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency and trifunctional protein (TFP) deficiency are caused by impairment ... In individuals with LCHAD deficiency, there is isolated deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase, while ... Long-Chain Hydroxyacyl-CoA Dehydrogenase Deficiency / Trifunctional Protein Deficiency. Long-chain hydroxyacyl-CoA ...
... a secondary marker for medium chain acyl-CoA dehydrogenase deficiency), immunoreactive trypsinogen (a primary marker for cystic ... Suppl 3):61-7.. * Clinical and Laboratory Standards Institute. Application of a quality management system model for laboratory ... RR-3).. * National Newborn Screening and Genetics Resource Center. National newborn screening status report. Austin, TX: ... 3, 5,11,15,19,20,30,33,34,41-49). Data also were collected from state programs (50,51), CDC studies (8,52,53), and publicly ...
hydroxyacyl-CoA-like_DH_SDR_c-like; (3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs. PRK05653. Location:6 → 208 ... hydroxyacyl-CoA-like_DH_SDR_c-like; (3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs. pfam02036. Location:628 → ... hydroxyacyl-CoA-like_DH_SDR_c-like; (3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs. cd03448. Location:510 → ... hydroxyacyl-CoA-like_DH_SDR_c-like; (3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs. cd03448. Location:461 → ...
Short-chain acyl-CoA dehydrogenase (SCAD) deficiency: ACADS* , MetaboSeq , Test Requisition. *Very-long-chain acyl-CoA ... Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: ACADM , MetaboSeq , Test Requisition. *Multiple Acyl-CoA Dehydrogenation ... 17-beta-hydroxysteroid dehydrogenase X (HSD10) deficiency: HSD17B10* , MetaboSeq , Test Requisition. *Acyl-CoA Dehydrogenase-9 ... HMG-CoA lyase) deficiency: HMGCL* , MetaboSeq , Test Requisition ... Long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency: ...
Medium-chain acyl-CoA dehydrogenase deficiency Multiple acyl-CoA dehydrogenase deficiency. Partial deficiency of complex IV of ... Table 3. Etiologies for CK elevation; A - group 1 (IMD diagnosis); B - group 2 (without IMD diagnosis).. Group 1 - IMD ... Volume 20, Issue 3 July-September 2023. Pages: 87-89. ARTICLE HISTORY. Received 9 August 2022. Accepted 18 October 2022. CITE ... Table 3 shows detailed information about the different triggers for CK elevation. In the first group, CK was measured in ...
Short chain acyl-CoA dehydrogenase deficiency. ACADS. CNV. Short/branched chain acyl-CoA dehydrogenase deficiency. ACADSB. CNV ... Medium chain acyl-CoA dehydrogenase deficiency. ACADM. CNV. ... Very long chain acyl-CoA dehydrogenase deficiency. ACADVL. CNV ...
gi,77741084,ref,ZP_00809569.1, IMP dehydrogenase/GMP reductase:Enoyl-CoA hydratase/isomerase:NADP oxidoreductase, coe.... ... Enoyl-CoA. Match: gi,67549294,ref,ZP_00427162.1,. score: 412. e-value: 4e-113. Identity: 37.32%. Span: 2100bp (82.3%). Frame: 1 ... Enoyl-CoA. Match: gi,107023812,ref,YP_622139.1,. score: 408. e-value: 8e-112. Identity: 35.67%. Span: 2091bp (81.9%). Frame: 1 ... Enoyl-CoA. Match: gi,47575616,ref,ZP_00245651.1,. score: 399. e-value: 3e-109. Identity: 37.29%. Span: 2079bp (81.5%). Frame: 1 ...
Medium chain acyl-CoA dehydrogenase*. *(TFP) Trifunctional protein deficiency*. *(VLCAD) Very long-chain acyl-CoA dehydrogenase ... LCHAD) Long-chain L-3 hydroxyacyl-CoA dehydrogenase*. *(MCAD) ... SCAD) Short-chain acyl-CoA dehydrogenase**. *(X-ALD) X-linked ...
Sets of 4 enzymes (an acyl dehydrogenase, a hydratase, a hydroxyacyl dehydrogenase, and a lyase) specific for different chain ... Medium-chain acyl-CoA dehydrogenase deficiency (MCADD) This deficiency is the most common defect in the beta-oxidation cycle. ... Very long-chain acyl-CoA dehydrogenase deficiency (VLCADD) This deficiency is similar to LCHADD but is commonly associated with ... multiple acyl-coA dehydrogenase deficiency); oxidation of several amino acids is also affected. ...
The percentage contributions of lactate dehydrogenase 1 and 2 isoenzymes to the total amount of all 5 isoenzymes at 12 and 24 ... Conclusions and Clinical Relevance-Changes in protein contents of MCTs and the lactate dehydrogenase isoenzyme profile in GMM ... Muscle activities of phosphofructokinase and citrate synthase were measured biochemically; lactate dehydrogenase isoenzymes ... o 2max) for 3 min/d for 5 d/wk (canter group); walking for 1 h/d for 5 d/wk (walk group); or stall rest (stall group). ...
Long chain 3 Hydroxy acyl Co A Dehydrogenase Deficiency. *Adams Current Formula: 18 ounces of fat free milk divided into 3 6 ... Peripheral sensory-motor polyneuropathy, pigmentary retinopathy, and fatal cardiomyopathy in long-chain 3-hydroxy-acyl-CoA ... dehydrogenase deficiency; European Journal of Pediatrics; June 14, 1991. *see: Tyni, Kivel5, Lappi, Summanen, Nikoskelainen, ... chain 3-Hydroxyacyl-CoA Dehydrogenase Deficiency Caused by the G 158C Mutation; Ophthamology Volume 105, Number 5, May 1998 ...
short-chain acyl-coenzyme A dehydrogenase. unsaturated acyl coenzyme A reductase. Reaction catalysed. ... This enzyme from Streptomyces collinus is specific for (E)-but-2- enoyl-CoA, and is proposed to provide butanoyl-CoA as a ...
ACYL CoA DEHYDROGENASE: - oxidation of Acyl CoA to produce an alkene between α-β Carbons. - reductant is enzyme-bound FAD. - ... 2 Acetyl Coa -> Acetoacetyl Coa + CoA. 2) Citrate Synthase-like reaction:. Acetoacetyl CoA + Acetyl CoA + H2O -> HMG CoA. 3) ... thiol group of a second CoA cleaves off and Acetyl CoA. - reactant is Coa. - products are Acetyl CoA and Acyl-(less 2-C) CoA. ... succinyl CoA + acetoacetate -> Acetoacetyl CoA + succinate. 2) THIOLASE Cleavage:. Acetoacetyl CoA + CoA -> 2 Acetyl CoA. ...
Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHAD) This story is shared by a family who lost a child to LCHADD. Our ... Family Stories FAOD, LCHAD, LCHADD, Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency ...
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial. General function:. Involved in 3-hydroxyacyl-CoA dehydrogenase activity. ... Long Chain Acyl-CoA Dehydrogenase Deficiency (LCAD) (PathBank: SMP0000539). *Very-Long-Chain Acyl-CoA Dehydrogenase Deficiency ... This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. Gene Name: ... This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase. Gene Name: ...
... acetoacetyl-CoA). ... 3-hydroxyacyl-CoA dehydrogenase (acetoacetyl-CoA). Model: iB21_ ...
Medium chain acyl CoA dehydrogenase deficiency (MCAD) Short chain acyl CoA dehydrogenase deficiency (SCAD) Excludes: primary ... Long chain/very long chain acyl CoA dehydrogenase deficiency (LCAD, VLCAD) ... 3. Endocrine, Nutritional and Metabolic Diseases, and Immunity Disorders (240-279). Excludes: endocrine and metabolic ... Codes in Chapter 3 (i.e., 242.8, 246.0, 251-253, 255-259) may be used to identify such functional activity associated with any ...
Sabrina Malvagia 1 , Christopher A Haynes 2 , Laura Grisotto 3 , Daniela Ombrone 1 , Silvia Funghini 1 , Elisa Moretti 4 , ... Kathleen S McGreevy 5 , Annibale Biggeri 3 , Renzo Guerrini 6 , Raquel Yahyaoui 7 , Uttam Garg 8 , Mary Seeterlin 9 , Donald ... Background: 3-Hydroxypalmitoleoyl-carnitine (C16:1-OH) has recently been reported to be elevated in acylcarnitine profiles of ... 3 Department of Statistics, Computer Science and Applications G. Parenti University of Florence, Florence, Italy. ...
... acetoacetyl-CoA). ... 3-hydroxyacyl-CoA dehydrogenase (acetoacetyl-CoA). Model: iBWG_ ...
Coenzyme A dehydrogenase deficiencies *Very long-chain acyl-coenzyme A dehydrogenase deficiency]] (VLCAD) ... Before the fatty acids can be degraded, they must be converted to acyl CoA (a step called activation) and moved from the ... Short-chain acyl-coenzyme A dehydrogenase deficiency (SCAD). *Short chain L-3-hydroxyacyl-coA dehydrogenase deficiency (SCHAD) ... Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD). * ... Type 3 can begin in childhood or adulthood. For type 1 and most ...
Succinate dehydrogenase, β-hydroxyacyl-CoA dehydrogenase, and malate dehydrogenase declined roughly in parallel with citrate ... 4), with citrate synthase, succinate dehydrogenase, β-hydroxyacyl-CoA dehydrogenase, malate dehydrogenase, and β- ... 32) did not observe any significant change in the activities of succinate dehydrogenase and β-hydroxyacyl-CoA dehydrogenase, ... decline in β-hydroxyacyl-CoA dehydrogenase and a 27.1% decline in oxoglutarate dehydrogenase activities. Only the former ...
... dehydrogenase revisited: sequence analysis and crystal structure determination. Protein Science 8, 2010-2018 (1999). ... Barycki JJ, O’Brien LK, Strauss AW, and Banaszak LJ. Glutamate 170 of the catalytic dyad of human L-3-hydroxyacyl-CoA ... dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme. Journal of ... Barycki JJ, OBrien LK, Strauss AW, and Banaszak LJ. Pig heart short chain L-3-hydroxyacyl-CoA ...
... copy of the HIS3 gene under transcriptional control of a minimal CYC1 promoter and two copies of the rat enoyl-CoA hydratase/3- ... hydroxyacyl-CoA dehydrogenase PPRE was constructed and transformed with a rat liver cDNA yeast expression library [28]. ... Mitotic recombination was initiated by HO endonuclease-induced DSBs at the HO cut site (HOcs) located at his3-delta 3::HOcs, ... Of the putative interacting genes examined, PBP1 promoted the highest level of resistance to 3-aminotriazole (,100 mM) in ...
Forshaw, T. R. J., Subhi, Y., Andréasson, S. & Sørensen, T. L., 2022 juni 1, I: Ophthalmologica. 245, 3, s. 195-203 9 s.. ... Sellman, A., Katzman, P., Andreasson, S. & Lõndahl, M., 2020 juli 1, I: Undersea & Hyperbaric Medicine. 47, 3, s. 423-430 8 s. ... Kamme, C., Mayer, A. K., Strom, T. M., Andréasson, S. & Weisschuh, N., 2017, I: Acta Ophthalmologica. 95, 3, s. e250-e252. ... Kafantari, E., Andréasson, S., Säll, T. & Puschmann, A., 2020 okt., I: Parkinsonism and Related Disorders. 79, s. 138-140 3 s. ...
  • 3-hydroxyacyl-CoA dehydrogenase deficiency is an inherited condition that prevents the body from converting certain fats to energy, particularly during prolonged periods without food (fasting). (medlineplus.gov)
  • Problems related to 3-hydroxyacyl-CoA dehydrogenase deficiency can be triggered by periods of fasting or by illnesses such as viral infections. (medlineplus.gov)
  • Mutations in the HADH gene cause 3-hydroxyacyl-CoA dehydrogenase deficiency. (medlineplus.gov)
  • As a result, these fatty acids are not converted to energy, which can lead to characteristic features of 3-hydroxyacyl-CoA dehydrogenase deficiency, such as lethargy and hypoglycemia. (medlineplus.gov)
  • Conditions that disrupt the metabolism of fatty acids, including 3-hydroxyacyl-CoA dehydrogenase deficiency, are known as fatty acid oxidation disorders. (medlineplus.gov)
  • Some patients who are deficient in all 3 enzymatic activities of the protein have been described, although most have an isolated LCHAD deficiency, which results in the inability to metabolize long-chain fatty acids. (medscape.com)
  • Schematic demonstrating mitochondrial fatty acid beta-oxidation and effects of long-chain acyl CoA dehydrogenase deficiency (LCHAD) deficiency. (medscape.com)
  • Patients with LCHAD deficiency may develop a profound CNS deficiency of docosahexanoic acid ethyl ester (DHA), 22:6n-3. (medscape.com)
  • The etiology of the severe peripheral neuropathy of trifunctional protein deficiency may result from the unique metabolite, 3-keto-acyl-CoA, after conversion to a methylketone via spontaneous decarboxylation. (medscape.com)
  • Long-chain hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency and trifunctional protein (TFP) deficiency are caused by impairment of mitochondrial TFP. (nih.gov)
  • In individuals with LCHAD deficiency, there is isolated deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase, while deficiency of all three enzymes occurs in individuals with TFP deficiency. (nih.gov)
  • Isolated deficiency of long-chain 3-hydroxyl-CoA dehydrogenase (LCHAD) is an autosomal recessive disorder characterized by early-onset cardiomyopathy, hypoglycemia, neuropathy, and pigmentary retinopathy, and sudden death (IJlst et al. (nih.gov)
  • Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHAD) This story is shared by a family who lost a child to LCHADD. (savebabies.org)
  • In humans, acetoacetyl-CoA is involved in the metabolic disorder called the short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (HADH) pathway. (hmdb.ca)
  • High levels of C16:1-OH, combined with other hydroxylated long chain acylcarnitines are related to long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD) and trifunctional protein (TFP) deficiency. (nih.gov)
  • Admit patients with long-chain 3-hydroxy acyl-coenzyme A dehydrogenase (LCHAD) deficiency for medical management of acute hypoketotic hypoglycemic encephalopathy. (medscape.com)
  • If diagnosis of long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficiency is suspected but workup facilities are inadequate and no metabolic specialists are available, transfer of patient to a tertiary care hospital for further workup and management may be necessary. (medscape.com)
  • Advise avoidance of exercise and dehydration with hot temperatures because rhabdomyolysis and myoglobinuria may occur with long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficiency. (medscape.com)
  • Screening for long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficiency should be performed in newborns from mothers with hepatic complications during pregnancy such as acute fatty liver of pregnancy or severe hemolytic anemia, elevated liver enzymes, low platelet count (HELLP) syndrome. (medscape.com)
  • Pregnancy: Pregnancy complications reported in long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficiency carriers (with a long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficient fetus), include HELLP syndrome and acute fatty liver of pregnancy. (medscape.com)
  • [4] Trifunctional protein deficiency is characterized by decreased activity of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), long-chain enoyl-CoA hydratase, and long-chain thiolase. (wikidoc.org)
  • Long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) is 1 of 3 enzymatic activities that make up the trifunctional protein of the inner mitochondrial membrane. (medscape.com)
  • Characterization of SCHAD would provide information about the method of action of analogous proteins, such as long chain (LCHAD) and peroxisomal L-3-hydroxyacyl CoA dehydrogenases. (nebraska.edu)
  • In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction (S)-3-hydroxyacyl-CoA + NAD+ ⇌ {\displaystyle \rightleftharpoons } 3-oxoacyl-CoA + NADH + H+ Thus, the two substrates of this enzyme are (S)-3-hydroxyacyl-CoA and NAD+, whereas its 3 products are 3-oxoacyl-CoA, NADH, and H+. (wikipedia.org)
  • In humans, the following genes encode proteins with 3-hydroxyacyl-CoA dehydrogenase activity: HADH - Hydroxyacyl-Coenzyme A dehydrogenase HSD17B10 - 3-Hydroxyacyl-CoA dehydrogenase type-2 EHHADH - Peroxisomal bifunctional enzyme HSD17B4 - Peroxisomal multifunctional enzyme type 2 3-Hydroxyacyl CoA dehydrogenase is classified as an oxidoreductase. (wikipedia.org)
  • This enzyme participates in 8 metabolic pathways: fatty acid elongation in mitochondria fatty acid metabolism valine, leucine and isoleucine degradation lysine degradation tryptophan metabolism benzoate degradation via coa ligation butanoate metabolism caprolactam degradation The systematic name of this enzyme class is (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase. (wikipedia.org)
  • The HADH gene provides instructions for making an enzyme called 3-hydroxyacyl-CoA dehydrogenase. (medlineplus.gov)
  • The 3-hydroxyacyl-CoA dehydrogenase enzyme is required for a step that metabolizes groups of fats called medium-chain fatty acids and short-chain fatty acids. (medlineplus.gov)
  • This enzyme from Streptomyces collinus is specific for (E)-but-2- enoyl-CoA, and is proposed to provide butanoyl-CoA as a starter unit for straight-chain fatty acid biosynthesis. (expasy.org)
  • It is a substrate for succinyl-CoA:3-ketoacid-coenzyme A transferase, hydroxymethylglutaryl-CoA synthase, short-chain 3-hydroxyacyl-CoA dehydrogenase, peroxisomal bifunctional enzyme, acetyl-CoA acetyltransferase, and 3-ketoacyl-CoA thiolase. (hmdb.ca)
  • Barycki JJ, O’Brien LK, Strauss AW, and Banaszak LJ. Glutamate 170 of the catalytic dyad of human L-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme. Journal of Biological Chemistry 276, 36718-36726 (2001). (slu.edu)
  • Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase , acetyl-CoA acyltransferase , or beta-ketothiolase is an enzyme that in humans is encoded by the HADHB gene . (wikidoc.org)
  • Short chain L-3-hydroxyacyl CoA dehydrogenase (SCHAD) is a mitochondrial enzyme involved in the metabolism of fatty acids. (nebraska.edu)
  • Crystals of human SCHAD suitable for x-ray diffraction studies will then be prepared in order to resolve the three-dimensional structure of the apoenzyme, the NAD+-complexed enzyme, and the acyl-CoA-complexed enzyme. (nebraska.edu)
  • Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. (rhea-db.org)
  • This means that the bifunctional protein of rat liver is in fact a trifunctional enzyme possessing delta 3, delta 2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase (EC 4.2.1.17), and L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) activities in the same polypeptide. (rhea-db.org)
  • The other 2 activities of the protein are 2-enoyl coenzyme A (CoA) hydratase (LCEH) and long-chain 3-ketoacyl CoA thiolase (LCKT). (medscape.com)
  • TFP has three enzymatic activities - long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA dehydrogenase, and long-chain 3-ketoacyl-CoA thiolase. (nih.gov)
  • Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+. (yeastrc.org)
  • It catalyzes the oxidation of the hydroxyl group of L-3-hydroxyacyl CoA to a keto group, concomitant with the reduction of NAD+ to NADH. (nebraska.edu)
  • 3-hydroxyacyl-CoA dehydrogenase/ enoyl-CoA hydratase [Arabidopsis thaliana] >gi6728. (cornell.edu)
  • Peroxisomal delta 3, delta 2-enoyl-CoA isomerase (EC 5.3.3.8) was studied in the liver of rats treated with clofibrate. (rhea-db.org)
  • In control experiments, the peroxisomal bifunctional protein purified according to published methods also catalyzed delta 3, delta 2-enoyl-CoA isomerization. (rhea-db.org)
  • Mutations in the HADH gene lead to a shortage of 3-hydroxyacyl-CoA dehydrogenase. (medlineplus.gov)
  • Acetyl CoA is generated from fatty acids through repeated beta-oxidation cycles. (msdmanuals.com)
  • The HADHB protein catalyzes the final step of beta-oxidation, in which 3-ketoacyl CoA is cleaved by the thiol group of another molecule of Coenzyme A . The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. (wikidoc.org)
  • Reye-like syndrome resulting from novel missense mutations in mitochondrial medium- and short-chain l-3-hydroxy-acyl-CoA dehydrogenase. (medlineplus.gov)
  • Thus, the clinical features may result from either toxicity due to long-chain acyl-CoA esters that cause cardiomyopathy and cardiac arrhythmias or from a block in long-chain fatty acid oxidation that leads to an inability to synthesize ketone bodies and/or adenosine triphosphate from long-chain fatty acids. (medscape.com)
  • Sets of 4 enzymes (an acyl dehydrogenase, a hydratase, a hydroxyacyl dehydrogenase, and a lyase) specific for different chain lengths (very long chain, long chain, medium chain, and short chain) are required to catabolize fatty acids completely. (msdmanuals.com)
  • What happens if you lack the proteins to transport Acyl-Coa into the matrix? (flashcardmachine.com)
  • Bennett MJ, Russell LK , Tokunaga C, Narayan SB, Tan L, Seegmiller A, Boriack RL, and Strauss AW. Reye-like syndrome resulting from novel missense mutations in mitochondrial medium- and short- chain L-3-hydroxy-acyl-CoA dehydrogenase. Molecular Genetics and Metabolism 89:74-79 (2006). (slu.edu)
  • Barycki JJ, O'Brien LK, Strauss AW, and Banaszak LJ. Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: sequence analysis and crystal structure determination. Protein Science 8, 2010-2018 (1999). (slu.edu)
  • [10] Additionally, HADHB has been shown to bind to the distal 3' untranslated region of renin mRNA, thereby regulating renin protein expression. (wikidoc.org)
  • In addition to the isomerization of 3-enoyl-CoA esters, the purified protein also catalyzed hydration of trans-2-enoyl-CoA and oxidation of L-3-hydroxyacyl-CoA. (rhea-db.org)
  • Incubation of the purified protein with trans-3-decenoyl-CoA, NAD+, and Mg2+ resulted in an increase in absorbance at 303 nm, indicating the formation of 3-ketoacyl-CoA. (rhea-db.org)
  • It also acts as a catalyst for the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. (nih.gov)
  • In contrast, others have favored the concept that exaggerated insulin secretion will cause insulin resistance ( 3 , 4 ), possibly via fatty acid-mediated impairment of insulin action ( 5 - 7 ). (diabetesjournals.org)
  • 8,10 IMD are the focus in the present work as a possible aetiology for CK elevation and are classically divided in three main groups: group 1 - disorders of intermediary metabolism affecting small molecules (symptoms by intoxication), group 2 - disorders involving primarily energy metabolism (the main responsible for metabolic myopathies) and group 3 - disorders involving complex molecules. (pediatriconcall.com)
  • Acetoacetyl-CoA is an intermediate in the metabolism of butanoate. (hmdb.ca)
  • The extreme symptom of this metabolic crisis is Myoglobinuria (3) which is the breakdown of muscle tissue to such an extent that it can be measured in the urine. (fodsupport.org)
  • 3) Metabolic acidosis with an increase in the anion gap. (who.int)
  • 3-Hydroxypalmitoleoyl-carnitine (C16:1-OH) has recently been reported to be elevated in acylcarnitine profiles of patients with propionic acidemia (PA) or methylmalonic acidemia (MMA) during expanded newborn screening (NBS). (nih.gov)
  • Proporciona un análisis completo de los genes involucrados en esta enfermedad utilizando secuenciación de próxima generación (NGS) para comprender completamente el espectro de genes relevantes involucrados. (igenomix.com)
  • Similar effects have been observed in semi-professional players during 2 weeks of intensified training with ten sessions of aerobic high-intensity training (8 × 2 min with 1 min recovery) and SET-P (10-12 × 25-to 30-s sprints with 3 min recovery) concomitant with a 30% reduction in weekly training time at the end of the competitive season [124, 126]. (researchgate.net)
  • Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, and Banaszak LJ. Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxycyl-CoA dehydrogenase provide insights into catalytic mechanism. Biochemistry 38, 5786-5798 (1999). (slu.edu)
  • [ 1 , 2 ] Loss of mitochondria occurs in many of these maladies, but defects in the remaining mitochondria are emerging as key players in diabetes [ 3 ] and aging-related dysfunctions. (medscape.com)
  • In a systematic review by Stahl et al 3 with the main goal of finding a definition of rhabdomyolysis, the authors concluded that the most consensual definition is a clinical syndrome of acute muscle weakness, myalgia and swelling combined with a CK cut-off value of >1000 IU/L or >5x the upper limit of normal (ULN). (pediatriconcall.com)
  • Less than 0.1% of children who took aspirin developed Reye syndrome, but more than 80% of patients diagnosed with Reye syndrome had taken aspirin in the past 3 weeks. (medscape.com)
  • Barycki JJ, O’Brien LK, Strauss AW, and Banaszak LJ. Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. Journal of Biological Chemistry 275, 27186-27196 (2000). (slu.edu)
  • Acetoacetyl-CoA belongs to the class of organic compounds known as aminopiperidines. (hmdb.ca)
  • HSD17B10, hydroxysteroid (17-beta) dehydrogenase 10, is a member of the short-chain dehydrogenase/reductase superfamily. (nih.gov)
  • In all cases, Ter from Treponema denticola was the preferred trans-enoyl-CoA reductase. (biomedcentral.com)
  • Comment: This step is described by 1.1.1.35, a broader term for 3-hydroxyacyl-CoA dehydrogenases. (lbl.gov)
  • A competitive ELISA for quantitative measurement of Canine 3 hydroxyacyl CoA dehydrogenase type 2(HSD17B10) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (gentaur.pl)
  • 4. Peroxisome proliferator-activated receptor alpha-responsive genes induced in the newborn but not prenatal liver of peroxisomal fatty acyl-CoA oxidase null mice. (nih.gov)
  • 6. Peroxisomal and mitochondrial fatty acid beta-oxidation in mice nullizygous for both peroxisome proliferator-activated receptor alpha and peroxisomal fatty acyl-CoA oxidase. (nih.gov)
  • 12. Coordinate induction of hepatic fatty acyl-CoA oxidase and P4504A1 in rat after activation of the peroxisome proliferator-activated receptor (PPAR) by sulphur-substituted fatty acid analogues. (nih.gov)
  • 3-hydroxyacyl-CoA dehydrogenase PaaC [Ensembl]. (ntu.edu.sg)
  • 3-hydroxyacyl-CoA dehydrogenase PaaC (EC 1.1.1. (lbl.gov)
  • Unexpectedly, dietary \alpha -18:3 caused great reduction in the activity of 3-hydroxyacyl-CoA dehydrogenase measured with short- and medium-chain substrates but not with long-chain substrate. (iospress.com)
  • 3-phenylpropionate dioxygenase, ferredoxin subunit. (ntu.edu.sg)
  • Cecatto C, Godoy KDS, da Silva JC, Amaral AU, Wajner M. Disturbance of mitochondrial functions provoked by the major long-chain 3-hydroxylated fatty acids accumulating in MTP and LCHAD deficiencies in skeletal muscle. (medscape.com)
  • An overload of free fatty acids, particularly saturated free fatty acids, may induce the endoplasmic reticulum (ER) stress response ( 2 , 3 ). (spandidos-publications.com)
  • HP15_2693 (GFF2749) is involved in phenylalanine degradation via phenylacetyl-CoA and likely has this activity. (lbl.gov)
  • Reye-like syndrome resulting from novel missense mutations in mitochondrial medium- and short-chain l-3-hydroxy-acyl-CoA dehydrogenase. (medlineplus.gov)
  • Dietary fats rich in \alpha -18:3-CoA relative to safflower oil did not affect the hepatic activity of fatty acid synthase and glucose 6-phosphate dehydrogenase. (iospress.com)
  • Cecatto C, Wajner A, Vargas CR, Wajner SM, Amaral AU, Wajner M. High vulnerability of the heart and liver to 3‐hydroxypalmitic acid-induced disruption of mitochondrial functions in intact cell systems. (medscape.com)
  • Role of 3-hydroxy fatty acid-induced hepatic lipotoxicity in acute fatty liver of pregnancy. (medscape.com)
  • 13. Differential induction of genes in liver and brown adipose tissue regulated by peroxisome proliferator-activated receptor-alpha during fasting and cold exposure in acyl-CoA dehydrogenase-deficient mice. (nih.gov)
  • An NAD -dependent 3-hydroxyacyl CoA dehydrogenase that has specificity for acyl chains containing 8 and 10 carbons. (bvsalud.org)
  • Recombinant DECAY exhibited substrate specificity similar to the mammalian caspase-3 subfamily. (deathbase.org)
  • Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3. (ntu.edu.sg)
  • The lack of these enzymes leaves the body short of energy and allows breakdown products, such as acyl-CoA, to accumulate. (msdmanuals.com)
  • Then, we tested different enzymes for the subsequent pathway reactions: the 3-hydroxyacyl-CoA dehydrogenase PaaH1 increased hexanoic acid production to 33 mg/L, and the expression of enoyl-CoA hydratases Crt2 or Ech was critical to producing octanoic acid, reaching titers of 40 mg/L in both cases. (biomedcentral.com)
  • Less than 0.1% of children who took aspirin developed Reye syndrome, but more than 80% of patients diagnosed with Reye syndrome had taken aspirin in the past 3 weeks. (medscape.com)
  • Wolcott-Rallison syndrome with 3-hydroxydicarboxylic aciduria and lethal outcome. (nih.gov)
  • An increase in the level of 3-hydroxydicarboxylic acid in the urine. (nih.gov)