3-Hydroxyacyl CoA Dehydrogenases: 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.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Acyl-CoA Dehydrogenase: 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.Cocos: 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.Butyryl-CoA Dehydrogenase: 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.Butyrylcholinesterase: An aspect of cholinesterase (EC 3.1.1.8).Butyrates: Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.L-Lactate Dehydrogenase: 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.Alcohol Dehydrogenase: 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.Glyceraldehyde-3-Phosphate Dehydrogenases: 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.Aldehyde Dehydrogenase: 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.Glutamate Dehydrogenase: 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.Glucosephosphate DehydrogenaseMalate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Isocitrate Dehydrogenase: 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.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Dihydrolipoamide Dehydrogenase: 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.Carbohydrate Dehydrogenases: 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.Succinate Dehydrogenase: 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.L-Iditol 2-Dehydrogenase: 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 1.1.1.14Glycerolphosphate DehydrogenaseNAD: 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)Glucose 1-Dehydrogenase: 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.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Ketoglutarate Dehydrogenase ComplexCoenzyme AGlucose Dehydrogenases: 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 1.1.99.10.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.Phosphogluconate Dehydrogenase: 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.Sugar Alcohol Dehydrogenases: 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.NADH Dehydrogenase: 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.IMP Dehydrogenase: An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.Formate Dehydrogenases: 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 1.2.1.2.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.Xanthine Dehydrogenase: 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.Hydroxybutyrate Dehydrogenase3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide): A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.Kinetics: The rate dynamics in chemical or physical systems.Oxidoreductases: 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)Pyruvate Dehydrogenase (Lipoamide): 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).Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.11-beta-Hydroxysteroid Dehydrogenases: 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.NADP: 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)Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.Glucosephosphate Dehydrogenase Deficiency: 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.Molecular Sequence Data: 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.11-beta-Hydroxysteroid Dehydrogenase Type 1: 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.Alanine Dehydrogenase: 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.3-alpha-Hydroxysteroid Dehydrogenase (B-Specific): 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.Mannitol Dehydrogenases: Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.Acyl Coenzyme A: 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.Amino Acid Sequence: 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.Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Retinal Dehydrogenase: 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.Oxidation-Reduction: 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).Acyl-CoA Dehydrogenase, Long-Chain: 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.20-Hydroxysteroid Dehydrogenases: 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).11-beta-Hydroxysteroid Dehydrogenase Type 2: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Acetyl Coenzyme A: 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.Isovaleryl-CoA Dehydrogenase: 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).Homoserine Dehydrogenase: 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+ ...
Homo sapiens acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain (ACADS), nuclear gene encoding mitochondrial protein, mRNA. (H00000035-R01) - Products - Abnova
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
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 ...
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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.... ...
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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, ...
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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 ...
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 ...
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/ ...
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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 ...
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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?
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 ...
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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
DROUILLARD, J.S.; HENNING, P.H.; MEISSNER, H.H. and LEEUW, K-J.. Megasphaera elsdenii on the performance of steers adapting to a high-concentrate diet, using three or five transition diets. S. Afr. j. anim. sci. [online]. 2012, vol.42, n.2, pp.195-199. ISSN 2221-4062.. Megasphaera elsdenii (M.e.) NCIMB 41125 is a robust lactate utilizing strain of M.e. that is effective in minimizing the risk of ruminal acidosis in feedlot cattle. When dosed orally, cattle adapt smoothly to increasing concentrates in the diet, the incidence of digestive disturbances, morbidity and mortality is reduced, and carcass yield improves. One could therefore expect that the smooth transition should benefit overall performance. Dosing with the organism also provides the opportunity of a reduction in the time necessary for adaptation, rendering a further decrease in the cost of feeding. These two objectives were tested with 80 yearling crossbred steers blocked by weight before allotment to the respective treatments. The ...
This gene encodes the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Defects in this gene cause medium-chain acyl-CoA dehydrogenase deficiency, a disease characterized by hepatic dysfunction, fasting hypoglycemia, and encephalopathy, which can result in infantile death. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] ...
MalaCards based summary : Muscular Lipidosis, also known as lipid storage myopathy, is related to acyl-coa dehydrogenase, short-chain, deficiency of and carnitine deficiency, systemic primary. An important gene associated with Muscular Lipidosis is ACADS (Acyl-CoA Dehydrogenase Short Chain). Affiliated tissues include heart, skeletal muscle and kidney, and related phenotypes are Decreased viability and Decreased viability ...
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1EGC: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
1EGC: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
CP000667.PE429 Location/Qualifiers FT CDS 488729..489889 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Strop_0429" FT /product="acyl-CoA dehydrogenase domain protein" FT /note="PFAM: acyl-CoA dehydrogenase domain protein; FT Acyl-CoA dehydrogenase, type 2, C-terminal domain" FT /db_xref="EnsemblGenomes-Gn:Strop_0429" FT /db_xref="EnsemblGenomes-Tr:ABP52914" FT /db_xref="GOA:A4X214" FT /db_xref="InterPro:IPR006091" FT /db_xref="InterPro:IPR009075" FT /db_xref="InterPro:IPR009100" FT /db_xref="InterPro:IPR013786" FT /db_xref="InterPro:IPR036250" FT /db_xref="InterPro:IPR037069" FT /db_xref="UniProtKB/TrEMBL:A4X214" FT /protein_id="ABP52914.1" FT /translation="MSPLDLLDVDSSLSAEERQIRAVVRQLVDEQVRPHVAGWYEEGRV FT PARELAREFGRLGLLGMHLTGYGCAGSSAVAYGLACLELEAGDSGVRSLVSVQGALAMY FT AIWRYGSTEQKQHWLPAMAAGETIGCFALTEPDHGSDPASMTTRARRDGDDWVLHGTKM FT WITNATIADVAVIWARTDEGVRGFAVPTSTPGVAVREIRRKMSLRASVTGEISLDDVRL FT PAAARLPDAVGLKAPLGCLTEARHGIVWGALGAARDCLETTLEYAGSRTQFGRPLAGFQ FT ...
Incorporates a phase consisting of a 2,6-di-O-pentyl-3-butyryl derivative of gamma-cyclodextrin. Exhibits high selectivity for amino acids, amines, and furans.
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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 ... As short-chain acyl-CoA dehydrogenase is involved in beta-oxidation, a deficiency in this enzyme is marked by an increased ... Mutations of the ACADS gene are associated with a deficiency in the encoded protein short chain acyl-CoA dehydrogenase; ...
"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- ...
... or butyryl-CoA) is the coenzyme A-activated form of butyric acid. It is acted upon by butyryl-CoA dehydrogenase. It is an ...
"Deficiency of butyryl-CoA dehydrogenase - Conditions - GTR - NCBI". www.ncbi.nlm.nih.gov. NIH. Retrieved 30 October 2016. Wolfe ... "Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ... "Short-chain acyl-CoA dehydrogenase deficiency , Genetic and Rare Diseases Information Center(GARD) - an NCATS Program". ... Mutations in the ACADS gene lead to inadequate levels of short-chain acyl-CoA dehydrogenase, which is important for breaking ...
... (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) Molecular and Cellular Biology ...
2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase, and 2-methyl-3-hydroxy-butyryl CoA dehydrogenase. This enzyme participates ... In enzymology, a 3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC 1.1.1.178) is an enzyme that catalyzes the chemical reaction ( ... 2-methylacetoacetyl-CoA + NADH + H+ Thus, the two substrates of this enzyme are (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA and NAD+ ... The systematic name of this enzyme class is (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase. Other names in common ...
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 ...
... (EC 1.3.8.1, butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase, butyryl dehydrogenase, ... 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) Molecular and ... Butyryl coenzyme A dehydrogenase". J. Biol. Chem. 206 (1): 1-12. PMID 13130521. Beinert, H.; Lardy, H.; Myrbäck, K. (1963). " ...
... acyl-coa dehydrogenase, long-chain MeSH D08.811.682.660.150.200 --- acyl-CoA oxidase MeSH D08.811.682.660.150.300 --- butyryl- ... 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- ... 3-hydroxyacyl coa dehydrogenases MeSH D08.811.682.047.385.415 --- hydroxymethylglutaryl coa reductases MeSH D08.811.682.047. ...
... butyryl-CoA dehydrogenase EC 1.3.99.3: acyl-CoA dehydrogenase EC 1.3.99.4: 3-oxosteroid 1-dehydrogenase EC 1.3.99.5: 3-oxo-5a- ... glutaryl-CoA dehydrogenase EC 1.3.8.7: medium-chain acyl-CoA dehydrogenase EC 1.3.8.8: long-chain acyl-CoA dehydrogenase EC 1.3 ... glutaryl-CoA dehydrogenase EC 1.3.99.8: 2-furoyl-CoA dehydrogenase EC 1.3.99.9: now *EC 1.21.99.1 EC 1.3.99.10: isovaleryl-CoA ... benzylsuccinyl-CoA dehydrogenase EC 1.3.8.4: isovaleryl-CoA dehydrogenase EC 1.3.8.5: 2-methyl-branched-chain-enoyl-CoA ...
"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. The ACAD9 gene ... The specific activity of ACAD9 towards palmitoyl-CoA (C16:0) is three times higher than that towards stearoyl-CoA (C18:0). ...
Propionyl-CoA Butyryl-CoA Myristoyl-CoA Crotonyl-CoA Acetoacetyl-CoA Coumaroyl-CoA (used in flavonoid and stilbenoid ... In the citric acid cycle, coenzyme A works as an allosteric regulator in the stimulation of the enzyme pyruvate dehydrogenase. ... The major route of CoA activity loss is likely the air oxidation of CoA to CoA disulfides. CoA mixed disulfides, such as CoA-S- ... Free CoA can be regenerated from CoA disulfide and mixed CoA disulfides with reducing agents such as DTT or BME. Acetyl-CoA ...
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 ... 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. ...
... isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA ... 2-methyl branched chain acyl-CoA dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; 2-methylbutyryl-coenzyme A dehydrogenase; ... Molecular Function: acyl-CoA dehydrogenase activity; FAD binding Biological Process: branched-chain amino acid catabolic ... Defects in ACADSB are the cause of short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD); also known as 2- ...
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; 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- ...
deficiency of butyryl-CoA dehydrogenase. *lipid-storage myopathy secondary to short-chain acyl-coa dehydrogenase deficiency ... Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ... Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a condition that prevents the body from converting certain fats into ... Short-chain acyl-CoA dehydrogenase deficiency. Printable PDF Open All Close All ...
"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 ...
... 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] ...
... or butyryl-CoA) is the coenzyme A-activated form of butyric acid. It is acted upon by butyryl-CoA dehydrogenase. It is an ...
"Deficiency of butyryl-CoA dehydrogenase - Conditions - GTR - NCBI". www.ncbi.nlm.nih.gov. NIH. Retrieved 30 October 2016. Wolfe ... "Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through ... "Short-chain acyl-CoA dehydrogenase deficiency , Genetic and Rare Diseases Information Center(GARD) - an NCATS Program". ... Mutations in the ACADS gene lead to inadequate levels of short-chain acyl-CoA dehydrogenase, which is important for breaking ...
... 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 ... As short-chain acyl-CoA dehydrogenase is involved in beta-oxidation, a deficiency in this enzyme is marked by an increased ... Mutations of the ACADS gene are associated with a deficiency in the encoded protein short chain acyl-CoA dehydrogenase; ...
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- ...
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 ...
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 and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex ... NADP-specific electron-bifurcating [FeFe]-hydrogenase in a functional complex with formate dehydrogenase in Clostridium ... Structural basis of the hydride transfer mechanism in F(420)-dependent methylenetetrahydromethanopterin dehydrogenase. ...
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 ...
... "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_ ...
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 ...
mye:AB431_02000 butyryl-CoA dehydrogenase 611 109 ( -) 31 0.340 100 -, 1 ptm:GSPATT00026592001 hypothetical protein 438 109 ( 1 ... amz:B737_4131 acyl-CoA synthetase 546 100 ( -) 29 0.308 78 -, 1 bmd:BMD_2620 malate dehydrogenase 567 100 ( -) 29 0.313 150 -, ... amd:AMED_4179 acyl-CoA synthetase 546 100 ( -) 29 0.308 78 -, 1 amm:AMES_4131 acyl-CoA synthetase 546 100 ( -) 29 0.308 78 -, 1 ... kvl:KVU_PB0115 L-sorbosone dehydrogenase 609 108 ( -) 30 0.348 89 -, 1 kvu:EIO_3305 L-sorbosone dehydrogenase 609 108 ( -) 30 ...
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 ...
  • 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. (phosphosite.org)
  • 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)
  • 3-aminobutyryl-CoA is deaminated to crotonyl-CoA by an ammonia lyase (5). (nih.gov)
  • Isotopically labeled acetate and bicarbonate were transformed to ethylmalonyl-CoA by cell extracts of acetate-grown, isocitrate lyase-negative Rhodobacter sphaeroides as determined by NMR spectroscopy. (pnas.org)
  • For methylotrophic bacteria such as Methylobacterium extorquens , extension of the serine cycle with reactions of the ethylmalonyl-CoA pathway leads to a simplified scheme for isocitrate lyase-independent C 1 assimilation. (pnas.org)
  • However, the glyoxylate cycle cannot be the sole solution for acetyl-CoA assimilation, because several organisms that require such an anaplerotic reaction sequence lack isocitrate lyase activity ( 4 - 8 ) or show a labeling pattern after growth on acetate inconsistent with the operation of the glyoxylate cycle in acetate assimilation ( 9 , 10 ). (pnas.org)
  • In addition, the diverse group of streptomycetes uses an alternate, isocitrate lyase-independent route for acetyl-CoA assimilation, and there appears to be a direct link to antibiotic biosynthesis ( 8 , 14 ). (pnas.org)
  • 34. The isolated mutant microorganism according to claim 33, wherein the Lumen bacteria have inactive genes encoding lactate dehydrogenase (ldhA) and pyruvate-formate lyase (pfl), and produce succinate in high concentration without substantial production of other organic acids in an anaerobic condition. (patentsencyclopedia.com)
  • There it is cleaved by ATP citrate lyase into acetyl-CoA and oxaloacetate. (wikipedia.org)
  • Rare disorders of metabolism with elevated butyryl- and isobutyryl-carnitine detected by tandem mass spectrometry newborn screening. (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)
  • Moreover, the core methylotrophic pathways in M. extorquens AM1 involve unusual coenzyme A (CoA)-derivative metabolites, such as crotonyl-CoA, which is a precursor for the production of 1-butanol. (biomedcentral.com)
  • To our knowledge AtuD is the first acyl-CoA dehydrogenase with a documented substrate specificity for terpenoid molecule structure and is essential for a functional Atu pathway. (microbiologyresearch.org)
  • 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)
  • 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)
  • Here, a pathway termed the ethylmalonyl-CoA pathway operating in such organisms is described. (pnas.org)
  • In this work, we engineered a modified CoA-dependent pathway in Methylobacterium extorquens AM1 to produce 1-butanol. (biomedcentral.com)
  • In vitro isotopic tracing of metabolic flux and in vivo metabolite analysis showed the accumulation of butyryl-CoA, demonstrating the functionality of the synthetic pathway and identifying targets for future improvement. (biomedcentral.com)
  • We demonstrated the feasibility of using metabolic intermediates of the ethylmalonyl-CoA pathway in M. extorquens AM1 to generate value-added chemicals, with 1-butanol as the test case. (biomedcentral.com)
  • This will not only establish the biotechnological potential of the ethylmalonyl-CoA pathway, but will also introduce M. extorquens AM1 as a potential platform to produce value-added chemicals. (biomedcentral.com)
  • Most of the acetyl-CoA which is converted into fatty acids is derived from carbohydrates via the glycolytic pathway. (wikipedia.org)
  • 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 is an intermediate in the metabolism of Butanoate. (hmdb.ca)
  • This anaplerotic reaction sequence enables an organism to use substrates, which enter the central carbon metabolism on the level of acetyl-CoA, as sole carbon source. (pnas.org)
  • PA is caused by a deficiency of propionyl-CoA carboxylase (encoded by PCCA and PCCB ), and isolated MMA is either caused by a deficiency of methylmalonyl-CoA mutase, methylmalonyl-CoA epimerase or by a defect in the metabolism of the cofactor of methylmalonyl-CoA mutase, 5′-deoxyadenosylcobalamin (encoded by MUT, MCEE, MMAA, MMAB or MMADHC , respectively). (biomedcentral.com)
  • Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I". Cell Metabolism. (wikipedia.org)
  • Note that during fatty synthesis the reducing agent is NADPH, whereas NAD is the oxidizing agent in beta-oxidation (the breakdown of fatty acids to acetyl-CoA). (wikipedia.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)
  • Lastly, these tissues will be utilized to address the process by which distinctive accumulation of Acyl-CoA intermediates serve to locate the site of the defects in fatty acid oxidation. (elsevier.com)
  • However, this acetyl CoA needs to be transported into cytosol where the synthesis of fatty acids and cholesterol occurs. (wikipedia.org)
  • Rat liver 10-formyltetrahydrofolate dehydrogenase, carbamoyl phosphate synthetase 1 and betaine homocysteine S-methytransferase were co-purified on Kunitz-type soybean trypsin inhibitor-coupled sepharose CL-4B. (labome.org)