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.
A plant genus of the family ARECACEAE. It is a tropical palm tree that yields a large, edible hard-shelled fruit from which oil and fiber are also obtained.
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.
An aspect of cholinesterase (EC 3.1.1.8).
Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.
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.
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.
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 species of gram-negative, aerobic bacteria first isolated from soil in Vineland, New Jersey. Ammonium and nitrate are used as nitrogen sources by this bacterium. It is distinguished from other members of its genus by the ability to use rhamnose as a carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
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.
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
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)
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.-.
Oxidoreductases that are specific for ALDEHYDES.
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.
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.
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 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.
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.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
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.
A rare autosomal recessive disorder resulting from the absence of CATALASE activity. Though usually asymptomatic, a syndrome of oral ulcerations and gangrene may be present.
The rate dynamics in chemical or physical systems.
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 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.
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.
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)
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 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.
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.
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.
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.
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.
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.
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.
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).
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 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 characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
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).
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.

Purification and properties of 3-hydroxybutyryl-coenzyme A dehydrogenase from Clostridium beijerinckii ("Clostridium butylicum") NRRL B593. (1/29)

The enzyme 3-hydroxybutyryl-coenzyme A (CoA) dehydrogenase has been purified 45-fold to apparent homogeneity from the solvent-producing anaerobe Clostridium beijerinckii NRRL B593. The identities of 34 of the N-terminal 35 amino acid residues have been determined. The enzyme exhibited a native M(r) of 213,000 and a subunit M(r) of 30,800. It is specific for the (S)-enantiomer of 3-hydroxybutyryl-CoA. Michaelis constants for NADH and acetoacetyl-CoA were 8.6 and 14 microM, respectively. The maximum velocity of the enzyme was 540 mumol min-1 mg-1 for the reduction of acetoacetyl-CoA with NADH. The enzyme could use either NAD(H) or NADP(H) as a cosubstrate; however, kcat/Km for the NADH-linked reaction was much higher than the apparent value for the NADPH-linked reaction. Also, NAD(H)-linked activity was less sensitive to changes in pH than NADP(H)-linked activity was. In the presence of 9.5 microM NADH, the enzyme was inhibited by acetoacetyl-CoA at concentrations as low as 20 microM, but the inhibition was relieved as the concentration of NADH was increased, suggesting a possible mechanism for modulating the energy efficiency during growth.  (+info)

Misfolding, degradation, and aggregation of variant proteins. The molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency. (2/29)

Short chain acyl-CoA dehydrogenase (SCAD) deficiency is an inborn error of the mitochondrial fatty acid metabolism caused by rare variations as well as common susceptibility variations in the SCAD gene. Earlier studies have shown that a common variant SCAD protein (R147W) was impaired in folding, and preliminary experiments suggested that the variant protein displayed prolonged association with chaperonins and delayed formation of active enzyme. Accordingly, the molecular pathogenesis of SCAD deficiency may rely on intramitochondrial protein quality control mechanisms, including degradation and aggregation of variant SCAD proteins. In this study we investigated the processing of a set of disease-causing variant SCAD proteins (R22W, G68C, W153R, R359C, and Q341H) and two common variant proteins (R147W and G185S) that lead to reduced SCAD activity. All SCAD proteins, including the wild type, associate with mitochondrial hsp60 chaperonins; however, the variant SCAD proteins remained associated with hsp60 for prolonged periods of time. Biogenesis experiments at two temperatures revealed that some of the variant proteins (R22W, G68C, W153R, and R359C) caused severe misfolding, whereas others (R147W, G185S, and Q341H) exhibited a less severe temperature-sensitive folding defect. Based on the magnitude of in vitro defects, these SCAD proteins are characterized as folding-defective variants and mild folding variants, respectively. Pulse-chase experiments demonstrated that the variant SCAD proteins either triggered proteolytic degradation by mitochondrial proteases or, especially at elevated temperature, aggregation of non-native conformers. The latter finding may indicate that accumulation of aggregated SCAD proteins may play a role in the pathogenesis of SCAD deficiency.  (+info)

Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases. (3/29)

The acyl-CoA dehydrogenases are a family of mitochondrial flavoproteins involved in the catabolism of fatty and amino acids. Isobutyryl-CoA dehydrogenase (IBD) is involved in the catabolism of valine and catalyzes the conversion of isobutyryl-CoA to methacrylyl-CoA. The crystal structure of IBD with and without substrate has been determined to 1.76-A resolution. The asymmetric unit contains a homotetramer with substrate/product bound in two monomers. The overall structure of IBD is similar to those of previously determined acyl-CoA dehydrogenases and consists of an NH2-terminal alpha-helical domain, a medial beta-strand domain and a C-terminal alpha-helical domain. The enzyme-bound ligand has been modeled in as the reaction product, methacrylyl-CoA. The location of Glu-376 with respect to the C-2-C-3 of the bound product and FAD confirms Glu-376 to be the catalytic base. IBD has a shorter and wider substrate-binding cavity relative to short-chain acyl-CoA dehydrogenase, permitting the optimal binding of the isobutyryl-CoA substrate. The dramatic lateral expansion of the binding cavity seen in isovaleryl-CoA dehydrogenase is not observed in IBD. The conserved tyrosine or phenylalanine that defines a side of the binding cavity in other acyl-CoA dehydrogenases is replaced by a leucine (Leu-375) in the current structure. Substrate binding changes the position of some residues lining the binding pocket as well as the position of the loop containing the catalytic glutamate and subsequent helix. Three clinical mutations have been modeled to the structure. The mutations do not affect substrate binding but instead appear to disrupt protein folding and/or stability.  (+info)

2-ethylhydracrylic aciduria in short/branched-chain acyl-CoA dehydrogenase deficiency: application to diagnosis and implications for the R-pathway of isoleucine oxidation. (4/29)

BACKGROUND: Isolated excretion of 2-methylbutyrylglycine (2-MBG) is the hallmark of short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD), a recently identified defect in the proximal pathway of L-isoleucine oxidation. SBCADD might be underdiagnosed because detection and recognition of urine acylglycines is problematic. Excretion of 2-ethylhydracrylic acid (2-EHA), an intermediate formed in the normally minor R-pathway of L-isoleucine oxidation, has not previously been described in SBCADD. METHODS: Samples from four patients with 2-MBG excretion were analyzed by gas chromatography-mass spectrometry for urine organic acids, quantification of 2-MBG, and chiral determination of 2-methylbutyric acid. Blood-spot acylcarnitines were measured by electrospray-tandem mass spectrometry. Mutations in the ACADSB gene encoding SBCAD were identified by direct sequencing. RESULTS: SBCADD was confirmed in each patient by demonstration of different ACADSB gene mutations. In multiple urine samples, organic acid analysis revealed a prominent 2-EHA peak usually exceeding the size of the 2-MBG peak. Approximately 40-46% of total 2-methylbutyric acid conjugates were in the form of the R-isomer, indicating significant metabolism via the R-pathway. CONCLUSIONS: If, as generally believed, SBCAD is responsible for R-2-MBG dehydrogenation in the R-pathway, 2-EHA would not be produced in SBCADD. Our observation of 2-ethylhydracrylic aciduria in SBCADD implies that a different or alternative enzyme serves this function. Increased flux through the R-pathway may act as a safety valve for overflow of accumulating S-pathway metabolites and thereby mitigate the severity of SBCADD. Awareness of 2-ethylhydracrylic aciduria as a diagnostic marker could lead to increased detection of SBCADD and improved definition of its clinical phenotype.  (+info)

ETHE1 mutations are specific to ethylmalonic encephalopathy. (5/29)

Mutations in ETHE1, a gene located at chromosome 19q13, have recently been identified in patients affected by ethylmalonic encephalopathy (EE). EE is a devastating infantile metabolic disorder, characterised by widespread lesions in the brain, hyperlactic acidaemia, petechiae, orthostatic acrocyanosis, and high levels of ethylmalonic acid in body fluids. To investigate to what extent ETHE1 is responsible for EE, we analysed this gene in 29 patients with typical EE and in 11 patients presenting with early onset progressive encephalopathy with ethylmalonic aciduria (non-EE EMA). Frameshift, stop, splice site, and missense mutations of ETHE1 were detected in all the typical EE patients analysed. Western blot analysis of the ETHE1 protein indicated that some of the missense mutations are associated with the presence of the protein, suggesting that the corresponding wild type amino acid residues have a catalytic function. No ETHE1 mutations were identified in non-EE EMA patients. Experiments based on two dimensional blue native electrophoresis indicated that ETHE1 protein works as a supramolecular, presumably homodimeric, complex, and a three dimensional model of the protein suggests that it is likely to be a mitochondrial matrix thioesterase acting on a still unknown substrate. Finally, the 625G-->A single nucleotide polymorphism in the gene encoding the short chain acyl-coenzyme A dehydrogenase (SCAD) was previously proposed as a co-factor in the aetiology of EE and other EMA syndromes. SNP analysis in our patients ruled out a pathogenic role of SCAD variants in EE, but did show a highly significant prevalence of the 625A alleles in non-EE EMA patients.  (+info)

Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids. (6/29)

Retinoic acid biosynthesis in vertebrates occurs in two consecutive steps: the oxidation of retinol to retinaldehyde followed by the oxidation of retinaldehyde to retinoic acid. Enzymes of the MDR (medium-chain dehydrogenase/reductase), SDR (short-chain dehydrogenase/reductase) and AKR (aldo-keto reductase) superfamilies have been reported to catalyse the conversion between retinol and retinaldehyde. Estimation of the relative contribution of enzymes of each type was difficult since kinetics were performed with different methodologies, but SDRs would supposedly play a major role because of their low K(m) values, and because they were found to be active with retinol bound to CRBPI (cellular retinol binding protein type I). In the present study we employed detergent-free assays and HPLC-based methodology to characterize side-by-side the retinoid-converting activities of human MDR [ADH (alcohol dehydrogenase) 1B2 and ADH4), SDR (RoDH (retinol dehydrogenase)-4 and RDH11] and AKR (AKR1B1 and AKR1B10) enzymes. Our results demonstrate that none of the enzymes, including the SDR members, are active with CRBPI-bound retinoids, which questions the previously suggested role of CRBPI as a retinol supplier in the retinoic acid synthesis pathway. The members of all three superfamilies exhibit similar and low K(m) values for retinoids (0.12-1.1 microM), whilst they strongly differ in their kcat values, which range from 0.35 min(-1) for AKR1B1 to 302 min(-1) for ADH4. ADHs appear to be more effective retinol dehydrogenases than SDRs because of their higher kcat values, whereas RDH11 and AKR1B10 are efficient retinaldehyde reductases. Cell culture studies support a role for RoDH-4 as a retinol dehydrogenase and for AKR1B1 as a retinaldehyde reductase in vivo.  (+info)

Gene expression profiles in fathead minnow exposed to 2,4-DNT: correlation with toxicity in mammals. (7/29)

Toxicogenomics, the genome-wide analysis of gene expression to study the effect of toxicants, has great potential for use in environmental toxicology. Applied to standard test organisms, it has possible applications in aquatic toxicology as a sensitive monitoring tool to detect the presence of contaminants while providing information on the mechanisms of action of these pollutants. We describe the use of a complementary DNA (cDNA) microarray of the fathead minnow (Pimephales promelas) a standard sentinel organism in aquatic toxicology, to better understand the mechanisms of toxicity of 2,4-dinitrotoluene (2,4-DNT) which is released in the environment through military and industrial use. We have constructed a fathead minnow microarray containing 5000 randomly picked anonymous cDNAs from a whole fish cDNA library. Expression profiles were analyzed in fish exposed to 2,4-DNT for 10 days at three concentrations (11, 22, and 44 microM, respectively) below the measured median lethal concentration (58 microM). Sequence analysis of cDNAs corresponding to differentially expressed genes affected by exposure revealed that lipid metabolism and oxygen transport genes were prominently affected in a dose-specific manner. We measured liver lipids and demonstrate that lipid metabolism is indeed perturbed following exposure. These observations correlate well with available toxicological data on 2,4-DNT. We present possible modes of action of 2,4-DNT toxicity and suggest that fathead minnow cDNA microarrays can be useful to identify mechanisms of toxicity in fish and as a predictive tool for toxicity in mammals.  (+info)

Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. (8/29)

Two distinct mutant alleles of the precursor (p) short chain acyl-CoA dehydrogenase (SCAD) gene were identified in a SCAD-deficient patient (YH2065) using the polymerase chain reaction to amplify cDNA synthesized from total RNA from her fibroblasts. Cells from this patient had previously been shown to synthesize a labile variant SCAD in contrast to the normal stability of variant SCADs in two other SCAD-deficient cell lines (Naito, E., Y. Indo, and K. Tanaka. 1989. J. Clin. Invest. 84:1671-1674). In the present study, both mutant alleles of YH2065 were found to contain a C----T transition, one at position 136 and the other at position 319 of the coding region of pSCAD cDNA. Clones of cDNA amplified from this region showed only one of the C----T transitions, indicating that each mutation was derived from different pSCAD alleles. Each of these mutations altered a known restriction endonuclease site, and restriction analysis of additional cDNA clones from amplified mutant cDNA and Southern blotting of mutant genomic DNA confirmed the presence of two unique mutant alleles in YH2065, indicating YH2065 is a compound heterozygote. These C----T transitions result in the substitution of Arg-22 and Arg-83 of the mature SCAD with Trp and Cys, respectively.  (+info)

Many biological systems including the oxidative catabolic pathway for branched-chain amino acids (BCAAs) are affected in vivo by valproate therapy. In this study we investigated the potential effect of valproic acid (VPA) and some of its metabolites on the metabolism of BCAAs. In vitro studies were performed using isovaleryl-CoA dehydrogenase (IVD), isobutyryl-CoA dehydrogenase (IBD) and short branched-chain acyl-CoA dehydrogenase (SBCAD), enzymes involved in the degradation pathway of leucine, valine and isoleucine. The enzymatic activities of the three purified human enzymes were measured using optimized HPLC procedures and the respective kinetic parameters were determined in the absence and presence of VPA and the corresponding CoA and dephosphoCoA conjugates. Valproyl-CoA and valproyl-dephosphoCoA inhibited IVD activity significantly by a purely competitive mechanism with Ki values of 74±4 µM and 170±12 µM, respectively. IBD activity was not affected by any of the tested VPA esters. ...
ACADSB Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent. Defects in ACADSB are the cause of short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD); also known as 2-methylbutyryl-CoA dehydrogenase deficiency or 2- methylbutyryl glycinuria. SBCADD is an autosomal recessive disorder and consists of a defect in catabolism of L-isoleucine which is characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine. Affected individuals have seizures and psychomotor delay as the main clinical features. Belongs to the acyl-CoA dehydrogenase family. Note: This description may include information from UniProtKB ...
In addition, as described in the above redox balance analysis, a possible involvement of a ferredoxin-dependent butyryl-CoA dehydrogenase/electron transferring flavoprotein complex (BCdH-ETF) in H2 production was proposed. In the BCdH-ETF catalyzed reaction electron transfer flavoproteins (ETFs) are involved in the reduction of crotonyl-CoA to butyryl-CoA, coupled with ferredoxin(ox) reduction by bifurcating electrons from NADH (Fig. 5) [28, 37]. In this proteomic study, two ETFs, namely ETFs subunit alpha (F502_06282) and subunit alpha/beta-like protein (F502_06287), were identified among the most abundant proteins regardless of the iron availability; however, their abundances were slightly higher (1.5-1.7 folds) in the late phase of the Fe+ culture compared to the Fe− late condition. This might indicate a relative increase in the oxidized ferredoxin pool necessary to carry out the BCdH-ETF reaction and also contributed to the stronger H2 production in the late fermentation phase under Fe+ ...
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
Homo sapiens acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain (ACADS), nuclear gene encoding mitochondrial protein, mRNA. (H00000035-R01) - Products - Abnova
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Looking for the definition of ACADS? What does ACADS stand for? Find out it here! 4 meanings for ACADS abbreviations and acronyms on acronymsandslang.com The Worlds most comprehensive acronyms and slang dictionary!
Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a condition that prevents the body from converting certain fats into energy, especially during periods without food (fasting).. Signs and symptoms of SCAD deficiency may appear during infancy or early childhood and can include vomiting, low blood sugar (hypoglycemia), a lack of energy (lethargy), poor feeding, and failure to gain weight and grow at the expected rate (failure to thrive). Other features of this disorder may include poor muscle tone (hypotonia), seizures, developmental delay, and a small head size (microcephaly).. The symptoms of SCAD deficiency may be triggered by fasting or illnesses such as viral infections. This disorder is sometimes mistaken for Reye syndrome, a severe condition that may develop in children while they appear to be recovering from viral infections such as chicken pox or flu. Most cases of Reye syndrome are associated with the use of aspirin during these viral infections.. In some people with SCAD ...
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
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Patient Preparation: A previous bone marrow transplant from an allogenic donor will interfere with testing. Call Mayo Medical Laboratories for instructions for testing patients who have received a bone marrow transplant.. Submit only 1 of the following specimens:. Preferred:. Specimen Type: Whole blood. Container/Tube:. Preferred: Lavender top (EDTA) or yellow top (ACD). Acceptable: Any anticoagulant. Specimen Volume: 3 mL. Collection Instructions:. 1. Invert several times to mix blood.. 2. Send specimen in original tube.. Specimen Stability Information: Ambient (preferred)/Refrigerated. Specimen Type: Cultured fibroblasts. Container/Tube: T-25 flask. Specimen Volume: 2 Full flasks. Specimen Stability Information: Ambient (preferred)/Refrigerated. Specimen Type: Blood spot. Supplies: Card - Blood Spot Collection (Filter Paper) (T493). Container/Tube:. Preferred: Collection card (Whatman Protein Saver 903 Paper). Acceptable: Ahlstrom 226 filter paper, or Blood Spot Collection Card ...
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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 ...
Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA (By similarity).
Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane- associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty ...
Fav-store specialize in supplying special featured herbal medecines, developed to improve your life and makes better your health. We present a 60 day full money back guarantee. Buy butyryl fentanylKeto acid - Wikipedia, the free encyclopedia.
To you SCAD ID kids: As someone who clawed my way through an ID program carrying an ArtBin full of markers, pens, pencils, rulers, French curves and geometric templates, I officially hate you. Do you realize that if we wanted to do a rendering in, say, orange, we had to run out and buy markers in a half-dozen shades of orange? And that when you or the store ran out of orange, you were screwed? Enjoy your digital color pickers, you little.... ...
Dr Ditoiu Alecse Valerian, gastroenterolog spitalul Fundeni Toti stim ca in organismul omului exista microbi, care uneori pot fi distrusi - in special de antibiotice sau medicamente care scad aciditatea din stomac si sunt mult folosite in zilele noastre. De aceea, nu este neobisnuit ca multe persoane cauta pe net remedii naturiste pentru refacerea florei…
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Rabbit recombinant monoclonal ACADS antibody [EPR10862(B)] validated for WB, IP, IHC and tested in Human, Mouse and Rat. Referenced in 1 publication and 2…
GenDR A curated database of genes associated with dietary restriction in model organisms either from genetic manipulation experiments or gene expression profiling.. ...
A stronghold include ,doblo-factory.scad,; include ,lib/doblo-params.scad,; // SCALE=LUGO; SCALE=DOBLO; stronghold(); module stronghold () { union() { doblo (col=-6, row=-6, up=0, width=12, length=12, height=THIRD, nibbles_on_off=false, diamonds=false, scale=SCALE); nibbles (col=3, row=-6, up=THIRD, width=3, length=3, scale=SCALE, extra=false, filled=false, hscale=1); nibbles (col=1, row=3, up=THIRD, width=5, length=3, scale=SCALE, extra=false, filled=false, hscale=1); nibbles (col=-6, row=3, up=THIRD, width=3, length=3, scale=SCALE, extra=false, filled=false, hscale=1); //back ramp (0, -5, 1, 2, 0, scale=SCALE); block (col=-5, row=-5, up=THIRD, width=1, length=1, height=6*FULL, nibbles_on_off=false, scale=SCALE); color (grey) ramp (-4, -5, 1, 2, 0, scale=SCALE); color (black) ramp (-2.5, -5, 1, 2, 180, scale=SCALE); block (col=-3, row=-5, up=THIRD, width=1, length=1, height=6*FULL, nibbles_on_off=false, scale=SCALE); ramp (-2, -5, 1, 2, 0, scale=SCALE); ramp (-0.5, -5, 1, 2, 180, ...
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.
Riboflavin deficiency in weanling rats causes a metabolic disorder characterized by failure to oxidize fatty acids. The disorder is similar to that seen in several human diseases, some of which are responsive to pharmacological doses of riboflavin. Previous analysis of the riboflavin-deficient rat has shown that the failure of fatty acid oxidation is due to a decrease in the activity of the acyl-CoA dehydrogenases of beta-oxidation. The activity of these flavoenzymes in liver rapidly decreases when a riboflavin-deficient diet is initiated. The objectives of these experiments were to analyse the effects of starvation on liver mitochondria isolated from the riboflavin-deficient rat. Our studies show that the decreased mitochondrial fatty acid oxidation induced by riboflavin deficiency is partially reversed by starvation. The extent of this reversal is proportional to the duration of starvation. The starvation-associated increase in fatty acid oxidation is mediated by an increase in the ...
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 ...
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
Abstract: Metabolomics has become an increasingly important methodology for analyzing perturbations in biological systems along with the more established proteomics and genomics tools currently available today. The study of small molecule metabolites has been described as the metabolic complement of functional genomics (Villas Boas 2005), and can provide a snapshot of the complex phenotypic stat... read morees of cellular systems. Metabolic studies have been mainly split into two major groups, global metabolite profiling or targeted metabolite analysis. This study utilizes targeted metabolite analysis to allow direct quantification of small molecules of interest, which can give a snapshot of dynamic metabolic flux and help characterize genetic modifications. In particular, the short chain acyl-CoA class of metabolites, used as building blocks for the production of polyketides, was studied. The acyl-CoA levels in several engineered Escherichia coli strains constructed for improved heterologous ...
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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 ...
M00777 Avermectin biosynthesis, 2-methylbutanoyl-CoA/isobutyryl-CoA => 6,8a-Seco-6,8a-deoxy-5-oxoavermectin 1a/1b aglycone => avermectin A1a/B1a/A1b/ ...
M00777 Avermectin biosynthesis, 2-methylbutanoyl-CoA/isobutyryl-CoA => 6,8a-Seco-6,8a-deoxy-5-oxoavermectin 1a/1b aglycone => avermectin A1a/B1a/A1b/ ...
Dizenteri Amebik është një formë e rëndë e Amebiazës e shoqëruar me dhimbje në stomak, jashtëqitje të përgjakshme, dhe ethe. Rrallë, E. histolyticainvades dëmton mëlçinë dhe formon një absces. Edhe më pak e zakonshme, ajo përhapet në pjesë të tjera të trupit, të tilla si mushkëritë ose trurit.. Disa njerëz përjetojnë parehati të butë të barkut, me diarre, ndoshta me gjak ose mukus, dhe nganjëherë alternohen me kapsllëk.. Raste të rënda kanë ethe, dridhura dhe diarre të përgjakshme ose mukoide.. Në disa raste, organizmi që shkakton sëmundje (patogjen) mund të pushtojë pjesët e tjera të trupit.. ...
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 …. ...
0468]The following compounds of formula I are especially preferred: [0469]4-{(S)-4-carboxy-2-[(4-chloro-6-phenyl-pyridine-2-carbonyl)-amino]-- butyryl}-piperazine-1-carboxylic acid ethyl ester; [0470]4-{(S)-4-carboxy-2-[(6-chloro-4-phenyl-pyridine-2-carbonyl)-amino]-- butyryl}-piperazine-1-carboxylic acid ethyl ester; [0471]4-{(S)-4-carboxy-2-[(4-cyclopentyloxy-6-phenyl-pyridine-2-carbonyl)- -amino]-butyryl}-piperazine-1-carboxylic acid ethyl ester; [0472]4-((S)-4-carboxy-2-{[4-(1-hydroxy-1-methyl-ethyl)-6-phenyl-pyridine- -2-carbonyl]-amino}-butyryl)-piperazine-1-carboxylic acid ethyl ester; [0473]4-{(S)-4-carboxy-2-[(4,6-diphenyl-pyridine-2-carbonyl)-amino]-butyr- yl}-piperazine-1-carboxylic acid ethyl ester; [0474]4-{(S)-4-carboxy-2-[(6-phenyl-4-pyrazol-1-yl-pyridine-2-carbonyl)-a- mino]-butyryl}-piperazine-1-carboxylic acid ethyl ester; [0475]4-((S)-4-carboxy-2-{[4-(4-methoxy-phenyl)-6-phenyl-pyridine-2-carbo- nyl]-amino}-butyryl)-piperazine-1-carboxylic acid ethyl ester; ...
In stable coronary artery disease (SCAD), prasugrel had a similar safety profile as in acute coronary syndromes (ACS), according to results of the BASKET-PROVE II trial released Aug. 31 as part of ESC Congress 2015 in London. However, more major bleeding was observed in elderly and/or low-weight patients despite a reduced dose of prasugrel, as compared to clopidogrel. The study prescribed 10mg of prasugrel to SCAD patients for one year. Patients at high risk for bleeding (i.e., ,75 years and/or ,60kg) received 5mg. The primary endpoint was major bleeding, with a secondary endpoint of ischemic events at two years. Results were compared between SCAD and ACS and with SCAD patients on clopidogrel in a historical control. Overall results found that major bleedings were not different between SCAD (n=845) and ACS (n=1,446) on prasugrel (2.2 vs. 3.3 percent, aHR 0.66 [0.37,1.19], p=0.167). But study investigators did note a greater occurrence of major bleedings in high risk patients during treatment. ...
CP000667.PE408 Location/Qualifiers FT CDS_pept 469214..469912 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=Strop_0408 FT /product=short-chain dehydrogenase/reductase SDR FT /note=PFAM: short-chain dehydrogenase/reductase SDR FT /db_xref=EnsemblGenomes-Gn:Strop_0408 FT /db_xref=EnsemblGenomes-Tr:ABP52893 FT /db_xref=InterPro:IPR002347 FT /db_xref=InterPro:IPR036291 FT /db_xref=UniProtKB/TrEMBL:A4X1Z3 FT /protein_id=ABP52893.1 FT /translation=MVNLDGLRVAVTGAGRASGRLLATAFAEHGAQVFVSARDEVAARR FT TTDSIRQRGRGRGEAFVCDLTSPDSVRAFAAALTDRTDHLDVLVNNGAGYLHGVDLGDV FT EDDHIIATIGGTATGTVLLTKHLLALLRASTRPDIVNMISACGEVGHHRSEAHPAFYAA FT KHAQAGFAEIMSHRLRVEGIRVISLFPPDFVQHGPRVASNNLTAQSVVDCVLFAVSQPR FT DCFIREFRFE gtggtgaatc tcgacggact acgggttgct gtcaccggcg ccgggcgcgc ctccggacgc 60 ctcctggcga ccgccttcgc cgagcacggc gcgcaggtgt ttgtctccgc ccgtgatgag 120 gtggcagcca gacgcaccac ggattcgatc cggcagcgtg ggcgggggag aggcgaagcc 180 ttcgtctgtg acctgaccag ccccgactcg gtacgcgcgt tcgcggcggc gttgaccgac 240 cgcaccgacc ...
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 ...
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If youre a young, healthy woman, it may seem like your chances of developing heart disease are slim, but in actuality, its an illness that affects everyone.
The first committed step of fatty acid and polyketides biosynthesis, the biotin-dependent carboxylation of an acyl-CoA, is catalyzed by acyl-CoA carboxylases (ACCases) such as acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC). ACC and PCC in Streptomyces coelicolor are homologues multisubunit complexes that can carboxylate different short chain acyl-CoAs. While ACC is able to carboxylate acetyl-, propionyl-, or butyryl-CoA with approximately the same specificity, PCC only recognizes propionyl- and butyryl-CoA as substrates. How ACC and PCC have such different specificities towards these substrates is only partially understood. To further understand the molecular basis of how the active site residues can modulate the substrate recognition, we mutated D422, N80, R456 and R457 of PccB, the catalytic beta subunit of PCC. The crystal structures of six PccB mutants and the wild type crystal structure were compared systematically to establish the sequence-structure-function relationship ...
IVD antibody [1B10] (isovaleryl-CoA dehydrogenase) for FACS, ICC/IF, IHC-P, WB. Anti-IVD mAb (GTX84285) is tested in Human, Dog, Monkey, Rat samples. 100% Ab-Assurance.
Looking for online definition of acyl-CoA dehydrogenase family member 9, mitochondrial in the Medical Dictionary? acyl-CoA dehydrogenase family member 9, mitochondrial explanation free. What is acyl-CoA dehydrogenase family member 9, mitochondrial? Meaning of acyl-CoA dehydrogenase family member 9, mitochondrial medical term. What does acyl-CoA dehydrogenase family member 9, mitochondrial mean?
Acylcarnitines are intermediates of fatty acid and amino acid oxidation found in tissues and body fluids. Acylcarnitines are important diagnostic markers for inherited diseases of peroxisomal and mitochondrial oxidation processes and abnormalities in specific acylcarnitine concentrations are used in the identification of carnitine deficiency and diagnosis of fatty acids oxidation defects and organic acidurias such as carnitine-acylcarnitine translocase deficiency (CACTD) or Isobutyryl-CoA dehydrogenase deficiency. Measuring different acylcarnitines can be used to detect more than 40 different inborn errors of metabolism. If these diseases are not diagnosed, the metabolic disorders can already lead to severe irreversible harm to newborns within their first few days of life. Newborn screening programs aim to detect congenital metabolic disorders early on in infants before they become symptomatic. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) has greatly increased the screening possibilities in
October 12, 2012. Thank you Bob and family for this wonderful website and for supporting SCAD research! My SCAD was in 2003, after the birth of my second son. I was 38 and had a widow maker tear at the fork of the LAD, so had double bypass surgery. Today, it feels as though all that happened to a different person. Although SCAD can recur, I dont dwell on that. My focus is my boys future and other women out there who are being misdiagnosed or ignored in the ER.. With deep appreciation to the Alicos, I look forward to knowing all the the SCAD women who are finding this site and gaining comfort. Were in this together! Best, Katherine. ...
Chronic isoproterenol administration produces a rapid, highly reproducible rodent model of cardiac hypertrophy. Yet, despite widespread use of this model, the effects of isoproterenol on in vivo cardiac function and substrate metabolism are unknown. Isoproterenol (5 mg.kg(-1).day(-1)) was infused for 7 days in male Wistar rats (n = 22). In vivo magnetic resonance imaging (MRI) showed that left ventricular mass increased by 37% and end-diastolic and systolic volumes increased by 33% and 73%, respectively, following isoproterenol infusion. Cardiac function at the base of the left ventricle was normal, but apical ejection fraction decreased from 90% to 31% and apical free wall thickening decreased by 94%, accompanied by increased fibrosis and inflammation. Myocardial palmitate oxidation rates were 25% lower, and citrate synthase and medium chain acyl-coenzyme A dehydrogenase activities were reduced by 25% and 29%, respectively, following isoproterenol infusion. Fatty acid transporter protein levels were 11
Androgen-regulated short-chain dehydrogenase/reductase 1, ARSDR1CGI82, EC 1.1.1.300, HCBP12, HCV core-binding protein HCBP12, MDT1, prostate short-chain dehydrogenase reductase 1, Prostate short-chain dehydrogenase/reductase 1, PSDR1FLJ32633, RALR1, RalR1, Retinal reductase 1, retinol dehydrogenase 11, retinol dehydrogenase 11 (all-trans and 9-cis), retinol dehydrogenase 11 (all-trans/9-cis/11-cis), SCALD, SDR7C1, short chain dehydrogenase/reductase family 7C, member ...
EC 1.1.1, EC 1.1.1.-, FLJ16333, MGC126600, Orphan short-chain dehydrogenase/reductase, RDH-S, RDHSMGC126602, SDR-Oorphan short-chain dehydrogenase / reductase, SDROretinol dehydrogenase similar protein, short-chain dehydrogenase/reductase family 9C member 7, short chain dehydrogenase/reductase family 9C, member ...
Protein target information for Acyl-CoA dehydrogenase, putative (Mycobacterium tuberculosis CDC1551). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
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Complete information for IVD gene (Protein Coding), Isovaleryl-CoA Dehydrogenase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Gene List: ACADM, ACADS, ACADSB, ACADVL, CPT1A, CPT2, ETFA, ETFB, ETFDH, HADH, HADHA, HADHB, HMGCL, HMGCS2, MLYCD, SLC22A5, SLC25A20 References: Houten SM…
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... this is also known as butyryl-CoA dehydrogenase deficiency. Many mutations have been identified in specific populations, and ... 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 ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
"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 ... cease before fully realized, which leads to a decrease in the production of NADH and Acetyl-CoA. The cascading effect continues ...
3-Hydroxy Butyryl-CoA Dehydrogenase, Crotonase, Butyryl-CoA Dehydrogenase, Butyraldehyde Dehydrogenase, and NAD-Dependent ... It is acted upon by butyryl-CoA dehydrogenase. It is an intermediary compound of ABE fermentation Butyryl-CoA is also converted ... From Redox data, Butyryl-COA dehydrogenase shows little to no activity at pH higher than 7.0. This is important as Enzyme ... Butyryl-COA dehydrogenase Oxidation-Reduction reaction consists of 2 electron transfer with 1 proton exchange. Ideally, this ...
... (EC 1.3.1.86, butyryl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase, ethylene ... butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl ... CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, CCR) is an enzyme with systematic name butanoyl-CoA:NADP+ 2,3- ... Crotonyl-CoA+reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ...
... (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 US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ...
CS1 maint: discouraged parameter (link) "Deficiency of butyryl-CoA dehydrogenase - Conditions - GTR - NCBI". www.ncbi.nlm.nih. ... "Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ... 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 ...
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 ...
Butyryl-CoA dehydrogenase. *Acyl CoA dehydrogenase *ACADSB. *ACADS. *5α-reductase *SRD5A1 ...
Butyryl-CoA dehydrogenase. *Acyl CoA dehydrogenase *ACADSB. *ACADS. *5α-reductase *SRD5A1 ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... Succinate dehydrogenase cytochrome b560 subunit, mitochondrial. Pfam PF01127 4. SdhD. DHSD_HUMAN. Succinate dehydrogenase [ ...
Acyl CoA dehydrogenase. *Apoptosis-inducing factor. *Butyryl CoA dehydrogenase. *Cryptochrome. *Cytochrome b5 reductase ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3. Pfam PF14987 39. NDUFA4 / MLRQc. NDUA4_HUMAN. NADH dehydrogenase ... NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1. Pfam PF15879 22. NDUFB3 / B12. NDUB3_HUMAN. NADH dehydrogenase [ ...
Butyryl-CoA dehydrogenase. *Acyl CoA dehydrogenase *ACADSB. *ACADS. *5α-reductase *SRD5A1 ... to acetyl-CoA. *Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate ... "Entrez Gene: succinate dehydrogenase complex".. *^ Kita K, Oya H, Gennis RB, Ackrell BA, Kasahara M (January 1990). "Human ... Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SDHB) also known as iron-sulfur subunit of complex II ...
butyryl-CoA dehydrogenase Ja 1.3.99.3 acyl-CoA dehydrogenase Ja 1.3.99.5 3-oxo-5alpha-steroid 4-dehydrogenase Ja ... oxoglutarate dehydrogenase (succinyl-transferring) Ja 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl- ... L-iditol 2-dehydrogenase Ja 1.1.1.15 D-iditol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-sorbose + NADH + H+ D-iditol 2- ... D-arabitol 4-dehydrogenase 1.1.1.12 L-arabitol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. L-xylulose + NADH + H+ L-arabitol ...
This metabolic pathway is as follows: butyrate→butyryl-CoA→crotonyl-CoA→β-hydroxybutyryl-CoA→poly-β-hydroxybutyrate→D-β-(D-β- ... The concentration of β-hydroxybutyrate in blood plasma is measured through a test that uses β-hydroxybutyrate dehydrogenase, ... Metabolic impairment diverts methylcrotonyl CoA to 3-hydroxyisovaleryl CoA in a reaction catalyzed by enoyl-CoA hydratase (22, ... Because oxaloacetate is crucial for entry of acetyl-CoA into the TCA cycle, the rapid production of acetyl-CoA from fatty acid ...
... acyl-coa dehydrogenase, long-chain MeSH D08.811.682.660.150.200 - acyl-CoA oxidase MeSH D08.811.682.660.150.300 - butyryl-coa ... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 - acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 - ... Glutaryl-CoA dehydrogenase MeSH D08.811.682.660.462 - isovaleryl-coa dehydrogenase MeSH D08.811.682.660.490 - 15- ... aspartokinase homoserine dehydrogenase MeSH D08.811.682.047.385 - 3-hydroxyacyl coa dehydrogenases MeSH D08.811.682.047.385.415 ...
"Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain". Biochemical and ... ACAD-9 has little activity on n-octanoyl-CoA (C8:0), n-butyryl-CoA (C4:0) or isovaleryl-CoA (C5:0). In contrast with ACADVL, ... Acyl-CoA dehydrogenase family member 9, mitochondrial is an enzyme that in humans is encoded by the ACAD9 gene. Mitochondrial ... The specific activity of ACAD9 towards palmitoyl-CoA (C16:0) is three times higher than that towards stearoyl-CoA (C18:0). ...
... were known for reducing crotonyl-coA to butyryl-coA. A report by Alber and coworkers concluded that a specific CCR homolog was ... Crotonic acid Glutaryl-CoA dehydrogenase Metabolism portal v t e. ... "Crotonyl-CoA". Wilson, Micheal C.; Moore, Bradley S. (2012). "Beyond ethylmalonyl-CoA: The functional role of crotonyl- ... "A crotonyl-CoA reductase-carboxylase independent pathway for assembly of unusual alkylmalonyl-CoA polyketide synthase extender ...
... binds to propionyl-CoA and butyryl-CoA. These specifically bind to the catalytic domain of Gen5L2. This conserved ... For example, inhibition of pyruvate dehydrogenase by an accumulation of propionyl-CoA in Rhodobacter sphaeroides can prove ... methylmalonyl-CoA by methylmalonyl-CoA racemase. (R)-Methylmalonyl-CoA is converted to succinyl-CoA, an intermediate in the ... In mammals, propionyl-CoA is converted to (S)-methylmalonyl-CoA by propionyl-CoA carboxylase, a biotin-dependent enzyme also ...
Propionyl-CoA Butyryl-CoA Myristoyl-CoA Crotonyl-CoA Acetoacetyl-CoA Coumaroyl-CoA (used in flavonoid and stilbenoid ... Acetyl-CoA is utilised in the post-translational regulation and allosteric regulation of pyruvate dehydrogenase and carboxylase ... The major route of CoA activity loss is likely the air oxidation of CoA to CoA disulfides. CoA mixed disulfides, such as CoA-S- ... Acetyl-CoA fatty acyl-CoA (activated form of all fatty acids; only the CoA esters are substrates for important reactions such ...
Regulation Acetyl-CoA is formed into malonyl-CoA by acetyl-CoA carboxylase, at which point malonyl-CoA is destined to feed into ... Omega-alicyclic fatty acids typically contain an omega-terminal propyl or butyryl cyclic group and are some of the major ... the cycle as CO2 in the decarboxylation reactions catalyzed by isocitrate dehydrogenase and alpha-ketoglutarate dehydrogenase. ... and isoleucine to form 2-methylpropanyl-CoA, 3-methylbutyryl-CoA, and 2-Methylbutyryl-CoA, respectively. 2-Methylpropanyl-CoA ...
The biosynthesis of fatty acids from acetyl-CoA primarily requires two enzymes. Acetyl-CoA carboxylase creates malonyl-CoA, ... 2 reductions involving the use of NADPH and one dehydration creates butyryl-ACP. Extension of the fatty acid comes from ... RNA tRNA ribosomal RNA tRNA ribosomal protein photosystem I nadh dehydrogenase tRNA ribosomal protein nadh dehydrogenase tRNA ... The carbon used to form the majority of the lipid is from acetyl-CoA, which is the decarboxylation product of pyruvate. ...
The biosynthesis of fatty acids from acetyl-CoA primarily requires two enzymes. Acetyl-CoA carboxylase creates malonyl-CoA, ... 2 reductions involving the use of NADPH and one dehydration creates butyryl-ACP. Extension of the fatty acid comes from ... The carbon used to form the majority of the lipid is from acetyl-CoA, which is the decarboxylation product of pyruvate[162]. ... The initiation of synthesis begins with the condensation of malonyl-ACP with acetyl-CoA to produce ketobutyryl-ACP. ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
The crystal structure of butyryl-CoA dehydrogenase (BCAD) from Megasphaera elsdenii complexed with acetoacetyl-CoA has been ... Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii.. Djordjevic S1, Pace CP, Stankovich MT, Kim ... BCAD is a bacterial analog of short chain acyl-CoA dehydrogenase from mammalian mitochondria. Mammalian acyl-CoA dehydrogenases ... was solved by the molecular replacement method using the atomic coordinates of pig liver medium chain acyl-CoA dehydrogenase ( ...
"Butyryl-CoA Dehydrogenase" by people in this website by year, and whether "Butyryl-CoA Dehydrogenase" was a major or minor ... "Butyryl-CoA Dehydrogenase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Butyryl-CoA Dehydrogenase*Butyryl-CoA Dehydrogenase. *Butyryl CoA Dehydrogenase. *Dehydrogenase, Butyryl-CoA ... Below are the most recent publications written about "Butyryl-CoA Dehydrogenase" by people in Profiles. ...
... butyryl-CoA dehydrogenase; Etf electron transport flavoproteins; Cat, butyryl CoA: acetate CoA transferase; Glt, glutamate ... 2008) Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf ... The last step in E. rectales butyrate production pathway is catalyzed by the butyrylCoA dehydrogenase/electron transfer ... Pts, phosphotransferase systems; Gpd, glycerol 3-phosphate dehydrogenase; Pck, phosphoenolpyruvate carboxykinase; Por, pyruvate ...
Crotonyl-CoA is reduced to butyryl-CoA by butyryl-CoA dehydrogenase (6), which reacts with acetoacetate to form butyrate and ... glutamate dehydrogenase (7); acetoacetyl-CoA thiolase (8); phosphate acetyltransferase (9); acetate kinase (10); butyryl-CoA ... It is further converted into 3-aminobutyryl-CoA and acetoacetate in the presence of acetyl-CoA by 3-keto-5-aminohexanoate ... butyrate CoA transferase (7). The latter compound is converted to acetate via acetyl-CoA and acetyl phosphate by acetoacetyl- ...
The ACADS gene provides instructions for making an enzyme called short-chain acyl-CoA dehydrogenase (SCAD). This enzyme ... Butyryl-CoA dehydrogenase. *SCAD. *Unsaturated acyl-CoA reductase. Additional Information & Resources. Tests Listed in the ... in short-chain acyl-CoA dehydrogenase identified in subjects with short-chain acyl-CoA dehydrogenase deficiency. Hum Genet. ... Short-chain acyl-CoA dehydrogenase deficiency. More than 55 mutations in the ACADS gene have been found to cause short-chain ...
Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a condition that prevents the body from converting certain fats into ... Rare disorders of metabolism with elevated butyryl- and isobutyryl-carnitine detected by tandem mass spectrometry newborn ... medlineplus.gov/genetics/condition/short-chain-acyl-coa-dehydrogenase-deficiency/ Short-chain acyl-CoA dehydrogenase deficiency ... Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ...
... is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and ... Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the ... Butyryl-CoA dehydrogenase (EC:1.3.8.1*Search proteins in UniProtKB for this EC number. ... Isovaleryl-CoA dehydrogenase, mitochondrial (Ivd). *Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (Mccc1), ...
3-Hydroxy Butyryl-CoA Dehydrogenase, Crotonase, Butyryl-CoA Dehydrogenase, Butyraldehyde Dehydrogenase, and NAD-Dependent ... It is acted upon by butyryl-CoA dehydrogenase. It is an intermediary compound of ABE fermentation Butyryl-CoA is also converted ... From Redox data, Butyryl-COA dehydrogenase shows little to no activity at pH higher than 7.0. This is important as Enzyme ... Butyryl-COA dehydrogenase Oxidation-Reduction reaction consists of 2 electron transfer with 1 proton exchange. Ideally, this ...
... this is also known as butyryl-CoA dehydrogenase deficiency. Many mutations have been identified in specific populations, and ... 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 ...
Acyl-CoA Dehydrogenase Short Chain, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - ... Uncertain Significance: Deficiency of butyryl-CoA dehydrogenase. 120,737,872(+). G/A MISSENSE_VARIANT,INTRON_VARIANT. ... Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial ... Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
... acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC. DR GO ... DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313,EMBL:ABL68314.1}; DE EC=1.3.8.1 {ECO:0000313,EMBL:ABL68314.1}; GN ... DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203 ... DR Gene3D; 1.10.540.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR ...
... butyryl-CoA dehydrogenase/electron-transferring flavoprotein (Bcd/Etf) complex; 17, butyrate kinase; 18, butyryl-CoA:acetate ... after phosphorylation of butyryl-CoA) or a butyryl-CoA:acetate CoA transferase (Falony et al., 2009c; Louis and Flint, 2009; ... in which the last step is carried out by a butyryl-CoA dehydrogenase/electron-transferring flavoprotein complex that catalyzes ... The butyryl-CoA:acetate CoA transferase step involves the consumption of external acetate (coming from for instance ...
... butyryl-CoA catalyzed by butyryl CoA dehydrogenase/electron-transfer flavoprotein complex. Butyryl-CoA dehydrogenase. A short- ... 2-acetyl-CoACoA + acetoacetyl-CoA. EC 2.3.1.9. 3-Hydroxybutyryl-CoA dehydrogenase. 3-Acetoacetyl-CoA + NADPH + H+ ↔ 3- ... Butyryl-CoA dehydrogenase/Etf complex. Butanoyl-CoA + 2 NAD+ + 2 reduced Fd ↔ Crotonoyl-CoA + 2 NADH + 2 oxidized Fd. EC 1.3. ... Butyryl-CoA dehydrogenase/Etf complex. EC 1.3.1.109. Acetate CoA-transferase. Acyl-CoA + acetate ↔ a fatty acid anion + acetyl- ...
Butyryl CoA dehydrogenase antibody. *Butyryl-CoA dehydrogenase antibody. *EC 1.3.99.2 antibody ... Effects of short-chain acyl-CoA dehydrogenase on cardiomyocyte apoptosis.. J Cell Mol Med 20:1381-91 (2016). WB ; Rat . Read ... Defects in ACADS are the cause of acyl-CoA dehydrogenase short-chain deficiency (ACADSD) [MIM:201470]. It is an autosomal ... Acyl-CoA dehydrogenase, C2 to C3 short chain antibody. *Acyl-CoA dehydrogenase, short chain antibody ...
1E). The gene marker, butyryl-CoA dehydrogenase from Fn (m1704941; 99.13% identity), showed an occurrence of only 52.7% (39/74 ...
"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...
... acetoacetyl-CoA transferase; [46] 3-hydroxybutyryl-CoA dehydrogenase; [47] 3-hydroxybutyryl-CoA dehydratase; [48] butyryl-CoA ... But-CoA, butyryl-CoA; DEH, 5-dehydro-4-deoxy-glucuronate; DG6S, d-galactose-6-sulfate; DHAP, dihydroxyacetone phosphate; Fdox/ ... acetate-CoA transferase; [52] glycerol dehydrogenase; [53] dihydroxyacetone kinase; [54] glycerol kinase; [55] glycerol-3- ... isocitrate dehydrogenase; [68] Fe-Fe hydrogenase; [69] V-ATPase; [70] F-ATPase; [71] P-PPase; [72] lactate dehydrogenase; [73] ...
Short Chain Acyl-Coa Dehydrogenase Deficiency 12 55 14 Deficiency of Butyryl-Coa Dehydrogenase 24 28 69 ... MalaCards integrated aliases for Acyl-Coa Dehydrogenase, Short-Chain, Deficiency of:. Name: Acyl-Coa Dehydrogenase, Short-Chain ... An important gene associated with Acyl-Coa Dehydrogenase, Short-Chain, Deficiency of is ACADS (Acyl-CoA Dehydrogenase Short ... Acyl-Coa Dehydrogenase, Short-Chain, Deficiency of, also known as scad deficiency, is related to acyl-coa dehydrogenase, very ...
Coupled ferredoxin coenzyme A (CoA) and crotonyl-CoA reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex ... acetyl-CoA and protons are reduced to butyryl-CoA and hydrogen, respectively. From 2 butyryl-CoA and 1 acetyl-CoA, 3 ATP are ... Four of the 5 acetyl-CoA formed are reduced by 4 NADH to 2 butyryl-CoA (see Fig. 2). Three ATP are generated from 2 butyryl-CoA ... 3-hydroxybutyryl-CoA to acetoacetyl-CoA and is used for reduction of crotonyl-CoA to butyryl-CoA (Fig. 4). This leads to 2 ...
... "acyl-CoA dehydrogenase" FT /EC_number="1.3.99.-" FT /note="GO_function: GO:0004085 - butyryl-CoA dehydrogenase FT activity; GO_ ... "possible isovaleryl-CoA dehydrogenase" FT /note="GO_function: GO:0008470 - isovaleryl-CoA FT dehydrogenase activity; GO_process ... "3-hydroxyacyl-CoA dehydrogenase" FT /EC_number="1.1.1.157" FT /note="GO_function: GO:0008691 - 3-hydroxybutyryl-CoA FT ... acyl-CoA dehydrogenase activity; GO_function: FT GO:0005524 - ATP binding; GO_function: GO:0016874 - ligase FT activity; GO_ ...
Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex ... Formate dehydrogenases and hydrogenases in syntrophic propionate-oxidizing communities : gene analysis and transcritional ... identification of an Rnf-type NADH dehydrogenase as a potential coupling site ...
bceo:I35_7369 Butyryl-CoA dehydrogenase 371 100 ( -) 29 0.321 84 -, 1 bpb:bpr_I2510 glucose-1-phosphate cytidylyltransferase ... clv:102083960 acyl-CoA dehydrogenase family member 9, m K15980 513 105 ( -) 30 0.303 122 -, 1 dfd:Desfe_0644 alpha amylase ... coa:DR71_433 trehalose synthase K05343 603 152 ( -) 40 0.285 172 -, 1 cre:CHLREDRAFT_173725 alpha-amylase-like protein K01176 ... bcj:BCAS0711 pyruvate dehydrogenase E1 component 3 K00163 904 105 ( 5) 30 0.306 98 ,-, 2 brd:JL11_09525 50S ribosomal protein ...
sve:SVEN_1021 Butyryl-CoA dehydrogenase 392 100 ( -) 29 0.306 134 -, 1 tbc:A0O31_00890 aminotransferase K14155 356 100 ( -) 29 ... ams:AMIS_21660 putative acyl-CoA thiolase K00626 373 107 ( -) 30 0.309 123 -, 1 ase:ACPL_6850 putative glucarate transporter ... rel:REMIM1_PF00079 L-idonate 5-dehydrogenase 2 K00098 344 100 ( -) 29 0.319 72 -, 1 rpc:RPC_2950 conserved hypothetical protein ... rpha:AMC79_PD00068 L-idonate 5-dehydrogenase 2 K00098 344 103 ( -) 29 0.333 72 -, 1 sfh:SFHH103_03710 Copper homeostasis ...
Quantitative PCR abundance of two gene markers (butyryl-CoA dehydrogenase from F. nucleatum, and RNA polymerase subunit β, rpoB ... The third gene (m1704941, butyryl-CoA dehydrogenase from F. nucleatum) was incidentally among the two genes successfully ... butyryl-CoA dehydrogenase from Fusobacterium nucleatum, m1696299: RNA polymerase subunit β, rpoB, from Parvimonas micra) were ... butyryl-CoA dehydrogenase from F. nucleatum; m482585, RNA-directed DNA polymerase from an unknown microbe) were also ...
Homo sapiens acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain (ACADS), nuclear gene encoding mitochondrial protein, mRNA ... butyryl-CoA dehydrogenase,short chain acyl-CoA dehydrogenase,unsaturated acyl-CoA reductase ... This gene encodes a a tetrameric mitochondrial flavoprotein, which is a member of the acyl-CoA dehydrogenase family. This ... Mutations in this gene have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency. [provided by RefSeq ...
... and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans. J. Biol. Chem. 289, 5145-5157 (2014). doi:10.1074/jbc. ... A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei ... The FlxABCD-HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria ... which is the reductive fixation of CO2 catalyzed by formylmethanofuran dehydrogenase (6, 7). ...
2008) Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyrylCoA dehydrogenase/Etf ... Wang S, Huang H, Kahnt J and Thauer RK (2013c) Clostridium acidurici electron‐bifurcating formate dehydrogenase. Applied and ... 2013b) An NADP‐specific electron‐bifurcating [FeFe]‐hydrogenase in a functional complex with formate dehydrogenase in ...
Interestingly, the abundance of the bcd gene encoding butyryl-CoA dehydrogenase (K00248) was significantly enriched in both E1 ... a Pathway showing the genes involved in final biosynthetic steps from crotonyl-CoA to butyrate, including bcd (butyryl-CoA ... butyryl CoA: acetate CoA transferase, K01034) were all significantly enriched in E1 as compared to E2 and E3, suggesting a ... butyryl CoA:acetate CoA transferase, K01034). b The relative abundance of genes involved in butyrate production within each ...
... butyryl dehydrogenase) which oxidizes C4 and C6 acyl-CoA substrates. The energy yield per cycle is 5 mols of ATP for each round ... The (D)methylmalonyl-CoA is isomerized to succinyl-CoA by methylmalonyl CoA mutase: (D)-methylmalonyl-CoA = succinyl-CoA Note ... of palmitoyl-CoA from acetyl-CoA units is: 8 acetyl-CoA + 7ATP +14NADPH +14H+ Þ palmitoyl-CoA + 7ADP + 7Pi + 7CoA + 14NADP+ + ... The acyl-CoA dehydrogenase is specific for the length of the acyl chain being oxidized. Three types of the dehydrogenase exist ...
  • Biochemical correction of short-chain acyl-coenzyme A dehydrogenase deficiency after portal vein injection of rAAV8-SCAD. (umassmed.edu)
  • Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a condition that prevents the body from converting certain fats into energy, especially during periods without food (fasting). (medlineplus.gov)
  • Mutations in this gene have been associated with short-chain acyl-CoA dehydrogenase (SCAD) deficiency. (genecards.org)
  • 49 Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a rare genetic condition that prevents the body from converting certain fats (called short-chain fatty acids) into energy. (malacards.org)
  • Acyl-Coa Dehydrogenase, Short-Chain, Deficiency of, also known as scad deficiency , is related to acyl-coa dehydrogenase, very long-chain, deficiency of and myopathy , and has symptoms including seizures , lethargy and failure to thrive . (malacards.org)
  • We showed previously that mice with genetically inactivated Acads , encoding short-chain acyl-CoA dehydrogenase (SCAD), shift food consumption away from fat and toward carbohydrate when tested in a macronutrient choice paradigm. (biomedcentral.com)
  • Acads encodes short-chain acyl-CoA dehydrogenase (SCAD), a member of the family of four enzymes that catalyzes the first of four sequential steps in the mitochondrial fatty acid oxidation spiral which produces acetyl-CoA for the tricarboxylic acid cycle. (biomedcentral.com)
  • The optimum substrate for SCAD is butyryl-CoA, a fatty acid with four carbon units. (biomedcentral.com)
  • Based on this proposition, the current study addressed the metabolic consequences of short-chain acyl-coenzyme A (CoA) dehydrogenase (SCAD) deficiency and dietary fat content on liver metabolism, including effects on tissue acylcarnitines, mitochondrial oxidative metabolism, hepatic pAMPK level, and genome-wide transcription. (biomedcentral.com)
  • The W177R missense variant in the ACADS gene has been reported previously in association with short chainacyl-CoA dehydrogenase (SCAD) deficiency using alternative nomenclature (Gregersen et al. (utah.edu)
  • Expression of short-chain acyl-CoA dehydrogenase (SCAD) proteins in the liver of SCAD deficient mice after hydrodynamic gene transfer. (labome.org)
  • The ACADS gene provides instructions for making an enzyme called short-chain acyl-CoA dehydrogenase (SCAD). (nih.gov)
  • More than 55 mutations in the ACADS gene have been found to cause short-chain acyl-CoA dehydrogenase (SCAD) deficiency. (nih.gov)
  • Biochemical, molecular, and clinical characteristics of children with short chain acyl-CoA dehydrogenase deficiency detected by newborn screening in California. (medlineplus.gov)
  • Jethva R, Bennett MJ, Vockley J. Short-chain acyl-coenzyme A dehydrogenase deficiency. (medlineplus.gov)
  • Defects in ACADS are the cause of acyl-CoA dehydrogenase short-chain deficiency (ACADSD) [MIM:201470]. (abcam.com)
  • These mutations lead to a shortage (deficiency) of an enzyme known as short-chain acyl-CoA dehydrogenase, which is involved in the breakdown of short-chain fatty acids. (malacards.org)
  • An important gene associated with Acyl-Coa Dehydrogenase, Short-Chain, Deficiency of is ACADS (Acyl-CoA Dehydrogenase Short Chain), and among its related pathways/superpathways are Fatty acid degradation and Fatty acid metabolism . (malacards.org)
  • 71 Acyl-CoA dehydrogenase short-chain deficiency: An inborn error of mitochondrial fatty acid beta-oxidation resulting in acute acidosis and muscle weakness in infants, and a form of lipid- storage myopathy in adults. (malacards.org)
  • The ACADS gene associated with short-chain acyl-coenzyme A dehydrogenase deficiency. (wikipedia.org)
  • this is also known as butyryl-CoA dehydrogenase deficiency. (wikipedia.org)
  • As short-chain acyl-CoA dehydrogenase is involved in beta-oxidation, a deficiency in this enzyme is marked by an increased amount of fatty acids. (wikipedia.org)
  • Genetic causes of secondary hyperammonemias can include the organic acidemias (primarily methylmalonic acidemia, propionic acidemia, and isovaleric acidemia), lysinuric protein intolerance, pyrroline-5-carboxylate synthetase deficiency, glutamine synthase deficiency, disorders that cause a decrease in the availability of acetyl-CoA (such as fatty acid oxidation defects), and defects in the carnitine cycle (Häberle 2013). (preventiongenetics.com)
  • Clinical and biochemical characterization of short-chain acyl-coenzyme A dehydrogenase deficiency. (wikibooks.org)
  • Genetic deficiency of short-chain acyl-coenzyme A (CoA) dehydrogenase activity was demonstrated in cultured fibroblasts from a 2-yr-old female whose early postnatal life was complicated by poor feeding, emesis, and failure to thrive. (elsevier.com)
  • These data demonstrated that medium-chain acyl-CoA dehydrogenase accounted for 50% of the activity towards the short-chain substrate, butyryl-CoA, under these conditions, but that antibody against that enzyme could be used to unmask the specific and virtually complete deficiency of short-chain acyl-CoA dehydrogenase in this patient. (elsevier.com)
  • ACADS (Acyl-CoA Dehydrogenase Short Chain) is a Protein Coding gene. (genecards.org)
  • Homo sapiens acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain (ACADS), nuclear gene encoding mitochondrial protein, mRNA. (abnova.com)
  • Acyl-CoA dehydrogenase, C-2 to C-3 short chain is an enzyme that in humans is encoded by the ACADS gene. (wikipedia.org)
  • Previously we reported that mice with a global, genetic inactivation of the gene encoding short-chain acyl-CoA dehydrogenase ( Acads−/− ) shift consumption away from fat and toward carbohydrate when offered a choice between macronutrient-rich diets [ 1 ]. (biomedcentral.com)
  • Thus, we hypothesized that the fatty acid intermediate, butyryl-CoA, is the substrate for histone butyrylation and its abundance is regulated by acyl-CoA dehydrogenase short chain (ACADS). (nih.gov)
  • The objective of this study was to determine the genomic distribution of H3K9-butyryl (H3K9Bu) and its regulation by dietary fat, stress, and ACADS and its impact on gene expression. (nih.gov)
  • ACADS is a tetrameric mitochondrial flavoprotein, which is part of the acyl-CoA dehydrogenase family. (assaysolution.com)
  • The structure of BCAD was solved by the molecular replacement method using the atomic coordinates of pig liver medium chain acyl-CoA dehydrogenase (MCAD). (nih.gov)
  • All of this residual activity was inhibited by an antibody against medium-chain acyl-CoA dehydrogenase. (elsevier.com)
  • Crotonyl-CoA is reduced to butyryl-CoA by butyryl-CoA dehydrogenase (6), which reacts with acetoacetate to form butyrate and acetoacetyl-CoA through the action of acetoacetate:butyrate CoA transferase (7). (nih.gov)
  • this was validated by reverse transcription-PCR (RT-PCR) of related genes, protein expression levels, in vitro CoA transferase assay, and fed-batch fermentation. (asm.org)
  • Acetone is produced from acetoacetyl coenzyme A (acetoacetyl-CoA) in a two-step process that involves a CoA transferase and an acetoacetate decarboxylase. (asm.org)
  • The CoA transferase consists of two different subunits encoded by the ctfA and ctfB genes, which are part of the sol operon ( 13 ). (asm.org)
  • Through parameter perturbation analysis, it was found that butyrate kinase has large and positive influence on butanol production while CoA transferase has negative effect on butanol production, suggesting that butyrate kinase has more efficiency in converting butyrate to butanol than CoA transferase. (biomedcentral.com)
  • grey) with ato (encoding butyryl-CoA:acetoacetate CoA transferase). (asm.org)
  • Unlike other food fermentations, yeast and molds are lesser microorganisms participating in vegetable fermentation and In the final step, propionyl-CoA yields propionic acid, and CoA is transferred to succinic acid by an enzyme, CoA-transferase. (fyfo.org)
  • The enzyme crystallizes in the P422 space group with cell dimensions a = b = 107.76 A and c = 153.67 A. BCAD is a bacterial analog of short chain acyl-CoA dehydrogenase from mammalian mitochondria. (nih.gov)
  • It is further converted into 3-aminobutyryl-CoA and acetoacetate in the presence of acetyl-CoA by 3-keto-5-aminohexanoate cleavage enzyme (4). (nih.gov)
  • This gene provides instructions for making an enzyme called short-chain acyl-CoA dehydrogenase, which is required to break down (metabolize) a group of fats called short-chain fatty acids. (medlineplus.gov)
  • an enzyme catalyzing a reversible reaction between an l -3-hydroxyacyl-CoA and a 2,3- (or 3,4-) trans- enoyl-CoA in fatty acid degradation. (thefreedictionary.com)
  • Acyl-CoA dehydrogenases ( EC 1.3.99.3 ) are a family of flavoproteins that catalyse the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with the concomitant reduction of enzyme-bound FAD. (embl.de)
  • We have developed an improved kinetic model featured with the incorporation of butyryl-phosphate, inclusion of net effects of complex metabolic regulations, and quantification of endogenous enzyme activity variations caused by these regulations. (biomedcentral.com)
  • exceptions are AtuC/AtuF, which constitute the two subunits of geranyl-CoA carboxylase, the key enzyme of the Atu pathway. (microbiologyresearch.org)
  • Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA dehydrogenase gene product, is a rate-limiting enzyme in long-chain fatty acid β-oxidation. (microbiologyresearch.org)
  • Acyl CoA dehydrogenase is the enzyme used to catalyze the first step of β-oxidation in Fatty acid metabolism . (wikidoc.org)
  • Next, succinyl-CoA produces methyl malonyl- CoA by the action of a vitamin B12-linked enzyme methyl malonyl mutase which catalyses an intra-molecular rearrangement. (fyfo.org)
  • Four of the 5 acetyl-CoA formed are reduced by 4 NADH to 2 butyryl-CoA (see Fig. 2 ). (asm.org)
  • Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri. (semanticscholar.org)
  • The expression of adhE2 from a plasmid in the DG1 mutant of C. acetobutylicum , a mutant cured of the pSOL1 megaplasmid, restored butanol production and provided elevated activities of NADH-dependent butyraldehyde and butanol dehydrogenases. (asm.org)
  • The recombinant AdhE2 protein expressed in E. coli as a Strep -tag fusion protein and purified to homogeneity also demonstrated NADH-dependent butyraldehyde and butanol dehydrogenase activities. (asm.org)
  • Two NADH-dependent butanol dehydrogenases (BDH) (BDH I and BDH II) have been purified, and their genes ( bdhA and bdhB ) have been cloned ( 43 ). (asm.org)
  • NADH Dehydrogenase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
  • This graph shows the total number of publications written about "NADH Dehydrogenase" by people in this website by year, and whether "NADH Dehydrogenase" was a major or minor topic of these publications. (umassmed.edu)
  • Below are the most recent publications written about "NADH Dehydrogenase" by people in Profiles. (umassmed.edu)
  • Seo BB, Nakamaru-Ogiso E, Cruz P, Flotte TR, Yagi T, Matsuno-Yagi A. Functional expression of the single subunit NADH dehydrogenase in mitochondria in vivo: a potential therapy for complex I deficiencies. (umassmed.edu)
  • The reactions catalyzed by different ferredoxin oxidoreductases and the exergonic NADH-dependent reduction of crotonyl-CoA point to a possible chemiosmotic energy conservation via the Rnf complex. (biomedcentral.com)
  • In clostridia the exergonic reduction of crotonyl-CoA to butyryl-CoA by NADH is coupled to the endergonic reduction of ferredoxin by NADH - a process called flavin-based electron bifurcation, catalyzed by a two-FAD-containing electron transferring flavoptrotein (Etf) and butyryl-CoA dehydrogenase (Bcd). (mpg.de)
  • Here, we report on the crystal structure of the formyl-methanofuran dehydrogenase (Fwd) and heterodisulfide-reductase/hydrogenase complexes (Hdr/Mvh). (mpg.de)
  • Rare disorders of metabolism with elevated butyryl- and isobutyryl-carnitine detected by tandem mass spectrometry newborn screening. (medlineplus.gov)
  • This gene encodes a tetrameric mitochondrial flavoprotein, which is a member of the acyl-CoA dehydrogenase family. (genecards.org)
  • Gene Ontology (GO) annotations related to this gene include flavin adenine dinucleotide binding and fatty-acyl-CoA binding . (genecards.org)
  • The adhE2 gene of Clostridium acetobutylicum ATCC 824, coding for an aldehyde/alcohol dehydrogenase (AADH), was characterized from molecular and biochemical points of view. (asm.org)
  • The aad gene of C. acetobutylicum ATCC 824 (referred to as adhE in strain DSM 792) is part of the sol operon, and it encodes a bifunctional aldehyde/alcohol dehydrogenase (AADH) ( 13 , 29 ). (asm.org)
  • Purified PA1535 gene product revealed high citronellyl-CoA dehydrogenase activity ( V max 2450 mU mg −1 ) but had significantly lower affinity than AtuD to citronellyl-CoA ( K m 18 μM). (microbiologyresearch.org)
  • 13. The recombinant solventogenic organism of claim 10, wherein the gene is an alcohol dehydrogenase. (patentsencyclopedia.com)
  • 17. The recombinant solventogenic organism of claim 14, wherein the gene is a butyryl-CoA dehydrogenase. (patentsencyclopedia.com)
  • Nagan N, Kruckeberg KE, Tauscher AL, Bailey KS, Rinaldo P, Matern D. The frequency of short-chain acyl-CoA dehydrogenase gene variants in the US population and correlation with the C(4)-acylcarnitine concentration in newborn blood spots. (nih.gov)
  • The latter compound is converted to acetate via acetyl-CoA and acetyl phosphate by acetoacetyl-CoA thiolase (8), phosphate acetyltransferase (9), and acetate kinase (10), respectively. (nih.gov)
  • During the conversion of acetyl-CoA into butyryl-CoA thiolase crotonase 3-hydroxybutyryl-CoA dehydrogenase and butyryl-CoA dehydrogenase are played vital roles as key enzymes. (thefreedictionary.com)
  • It should be noted that without hydrogen formation the ATP yield would drop to 2.5 mol ATP (5 mol glutamate) −1 , because in order to maintain the redox balance, acetyl-CoA has to be completely reduced to butyrate. (asm.org)
  • The simulation results of our model are more consistent with published experimental data than the previous model, especially in terms of reflecting the kinetics of butyryl-phosphate and butyrate. (biomedcentral.com)
  • To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA. (uniprot.org)
  • Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). (genecards.org)
  • The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). (genecards.org)
  • Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:21237683, PubMed:11134486). (genecards.org)
  • Biochemical correction of short-chain acyl-coenzyme A dehydrogenase de" by Stuart G. Beattie, Eric Goetzman et al. (umassmed.edu)
  • We have produced AAV5 and AAV8 vectors that express mouse short-chain acyl-CoA dehydrogenase (mSCAD) cDNA under the transcriptional control of the cytomegalovirus-chicken beta-actin hybrid promoter. (umassmed.edu)
  • The activities of the mitochondrial FAD-dependent straight-chain acyl-CoA dehydrogenases (butyryl-CoA, octanoyl-CoA and palmitoyl-CoA) and the branched-chain acyl-CoA dehydrogenases (isovaleryl-CoA and isobutyryl-CoA) involved in the degradation of branched-chain acyl-CoA esters derived from branched-chain amino acids were assayed in liver mitochondrial extracts prepared in the absence and presence of exogenous FAD. (portlandpress.com)
  • Butyryl-CoA dehydrogenase [ ( PUBMED:11812788 ) ] prefers short chain substrates, medium chain- and long-chain acyl-CoA dehydrogenases prefer medium and long chain substrates, respectively, and Isovaleryl-CoA dehydrogenase [ ( PUBMED:9214289 ) ] prefers branched-chain substrates. (embl.de)
  • This entry represents the middle beta-barrel domain found in medium chain acyl-CoA dehydrogenases, as well as in the related peroxisomal acyl-CoA oxidase-II enzymes. (embl.de)
  • Identification of the catalytic base in long chain acyl-CoA dehydrogenase. (microbiologyresearch.org)
  • The cloning, using a PCR approach, of genes from both Streptomyces coelicolor and Streptomyces avermitilis encoding an acyl-CoA dehydrogenase (AcdH), putatively involved in the catabolism of branched-chain amino acids, is reported. (microbiologyresearch.org)
  • The deduced amino acid sequences of both genes have a high similarity to prokaryotic and eukaryotic short-chain acyl-CoA dehydrogenases. (microbiologyresearch.org)
  • Schmidt SP, Corydon TJ, Pedersen CB, Bross P, Gregersen N. Misfolding of short-chain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress. (nih.gov)
  • Black cells in the column " Bcd-αβ " represent the presence of the butyryl-CoA dehydrogenase electron transfer protein complex, i.e., bcd is in synteny with the etf genes. (asm.org)
  • Letters (A to D) represent the four distinct regions of individual trees based on genes of the acetyl-CoA pathway, and "*" marks deviations from the overall trend. (asm.org)
  • In isolated muscle mitochondria, cytochromes aa3, b and c were partially decreased, butyryl-CoA dehydrogenase and palmitoyl-CoA dehydrogenase activities were 10 and 54% of the normal, respectively. (elsevier.com)
  • Mammalian acyl-CoA dehydrogenases are flavin adenine dinucleotide (FAD)-containing enzymes that catalyze the first step in the beta-oxidation of fatty acids. (nih.gov)
  • To our knowledge AtuD is the first acyl-CoA dehydrogenase with a documented substrate specificity for terpenoid molecule structure and is essential for a functional Atu pathway. (microbiologyresearch.org)
  • 3-aminobutyryl-CoA is deaminated to crotonyl-CoA by an ammonia lyase (5). (nih.gov)
  • It is an intermediary compound of ABE fermentation Butyryl-CoA is also converted from Crotonyl-CoA. (wikipedia.org)
  • This occurs when FADH- transfers a hydride to crotonyl-CoA. (wikipedia.org)
  • Fibroblasts from her parents had intermediate levels of activity towards butyryl-CoA, consistent with the autosomal recessive inheritance of this metabolic defect. (elsevier.com)
  • We characterized a novel, unique aminotransferase that acts exclusively on Coenzyme A (CoA) esters, and proposed a variant route for lysine fermentation. (nih.gov)
  • Butyryl-coenzyme A (or butyryl-CoA) is the coenzyme A-activated form of butyric acid. (wikipedia.org)
  • Relative to other family-level groups, salt stress induced a significant enrichment of transcripts related to the CO dehydrogenase/acetyl-coenzyme A synthase complex, methanogenesis, heat shock, ammonium uptake, and thermosomes, but the absolute abundance of methanosarcinal mRNA decreased. (frontiersin.org)
  • The mitochondrial isovaleryl-coenzyme A dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism. (microbiologyresearch.org)
  • Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. (uniprot.org)
  • For instance, 0.12 g/L of butanol was produced from crystalline cellulose after introduction of the CoA-dependent pathway by the recombinant C. cellulolyticum after 20 days. (biomedcentral.com)
  • The hypothetical alternative metabolism of 3-aminobutyryl-CoA. (nih.gov)
  • Butyryl-CoA is an intermediate in the metabolism of Butanoate. (hmdb.ca)
  • File:Steroidogenesis.svg 5α-reductases , also known as 3-oxo-5α-steroid 4-dehydrogenases , are enzymes involved in steroid metabolism. (wikidoc.org)
  • We demonstrate that in rat liver dicarboxylic acids (C5-C16) can be converted into their CoA esters by a dicarboxylyl-CoA synthetase. (portlandpress.com)
  • Investigations about the fate of dicarboxylyl-CoA esters disclosed the existence of an oxidase, which could be measured by monitoring the production of H2O2. (portlandpress.com)
  • SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. (univ-lyon1.fr)
  • Further genomic and proteomic analysis showed that the capabilities of efficient xylan degradation and butanol synthesis were attributed to the efficient expression of xylanase, β-xylosidase and the bifunctional alcohol/aldehyde dehydrogenase (AdhE). (biomedcentral.com)
  • Reduced ferredoxin, a potent electron donor, drives the first step of methanogenesis, which is the reductive fixation of CO 2 catalyzed by formylmethanofuran dehydrogenase ( 6 , 7 ). (sciencemag.org)
  • Butyryl-COA dehydrogenase Oxidation-Reduction reaction consists of 2 electron transfer with 1 proton exchange. (wikipedia.org)
  • Fibroblasts from this patient had 50% of control levels of acyl-CoA dehydrogenase activity towards butyryl-CoA as substrate at a concentration of 50 μM in a fluorometric assay based on the reduction of electron transfer flavoprotein. (elsevier.com)
  • This genus employs pathways and enzymes with unique activities mostly involved in amino acid degradation, such as B12-dependent aminomutases, selenium containing oxidoreductases and extremely oxygen-sensitive 2-hydroxyacyl-CoA dehydratases [ 4 - 6 ]. (biomedcentral.com)
  • Ethanol and butanol are produced from acetyl-CoA and butyryl-CoA, respectively, in two reductive steps catalyzed by aldehyde dehydrogenases and alcohol dehydrogenases (ADHs). (asm.org)
  • Gregersen N, Andresen BS, Corydon MJ, Corydon TJ, Olsen RK, Bolund L, Bross P. Mutation analysis in mitochondrial fatty acid oxidation defects: Exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship. (nih.gov)
  • The final result of beta-oxidation is acetyl-CoA. (wikipedia.org)
  • Berzin V, Kiriukhin M, Tyurin M (2013) Cre- lox 66/ lox 71-based elimination of phosphotransacetylase or acetaldehyde dehydrogenase shifted carbon flux in acetogen rendering selective overproduction of ethanol or acetate. (springer.com)
  • Of particular significance is the finding that H 2 formation in C. pasteurianum is coupled to the ferredoxin-dependent butyryl-CoA dehydrogenase catalyzed reaction, which significantly affects the redox balance and thus the product selectivity. (biomedcentral.com)