Butyryl coa dehydrogenase. Medical search

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.

Glucosephosphate Dehydrogenase (G6PD) is an enzyme that plays a crucial role in the pentose phosphate pathway, which generates NADPH for biosynthesis and detoxification processes.

An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.

A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).

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

Glycerolphosphate Dehydrogenase (GPDH) is an enzyme that plays a role in the glycerol phosphate pathway and is involved in the metabolism of glycerol and nucleotide synthesis.

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.

The Ketoglutarate Dehydrogenase Complex is an enzyme complex involved in the citric acid cycle that catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA, CO2, and NADH.

Coenzyme A is a molecule that plays a crucial role in the metabolism of carbohydrates, fats, and proteins in the body.

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.

Hydroxybutyrate Dehydrogenase is an enzyme that plays a role in the metabolism of ketone bodies in the liver.

A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.

The 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)

3-Hydroxyacyl CoA dehydrogenases are a group of enzymes that play a crucial role in the metabolism of fatty acids. These enzymes catalyze the oxidation of 3-hydroxyacyl-CoA molecules to their corresponding trans-enoyl-CoA molecules, which is an essential step in the breakdown of fatty acids for energy production. In the medical field, 3-hydroxyacyl CoA dehydrogenases are often studied in the context of metabolic disorders such as diabetes, obesity, and fatty liver disease. Abnormalities in the activity or expression of these enzymes can lead to the accumulation of toxic intermediates in the fatty acid metabolism pathway, which can cause cellular damage and contribute to the development of these diseases. In addition, 3-hydroxyacyl CoA dehydrogenases are also important in the regulation of energy metabolism in the body. They are involved in the control of the citric acid cycle, which is the primary source of energy for the body's cells. Therefore, understanding the function and regulation of these enzymes is important for developing new treatments for metabolic disorders and improving overall health.

Acyl-CoA dehydrogenases are a group of enzymes that play a crucial role in the metabolism of fatty acids. These enzymes catalyze the first step in the breakdown of fatty acids, which involves the removal of a hydrogen atom from the fatty acid molecule and the formation of a double bond. This process, known as beta-oxidation, generates energy in the form of ATP and reduces NAD+ to NADH. There are several different types of acyl-CoA dehydrogenases, each of which is responsible for catalyzing the oxidation of a specific type of fatty acid. For example, the long-chain acyl-CoA dehydrogenase (LCAD) is responsible for the oxidation of long-chain fatty acids, while the medium-chain acyl-CoA dehydrogenase (MCAD) is responsible for the oxidation of medium-chain fatty acids. Deficiencies in these enzymes can lead to a variety of metabolic disorders, including fatty acid oxidation disorders. These disorders are characterized by the accumulation of fatty acids and their breakdown products in the body, which can cause a range of symptoms, including muscle weakness, neurological problems, and liver damage.

Acyl-CoA dehydrogenase is an enzyme that plays a crucial role in the metabolism of fatty acids. It catalyzes the first step in the breakdown of fatty acids, which is the removal of a hydrogen atom from the fatty acid molecule and the transfer of an electron to an acceptor molecule. This process generates a high-energy molecule called FADH2, which is used to produce ATP through the electron transport chain in the mitochondria. Acyl-CoA dehydrogenase deficiency is a rare genetic disorder that affects the metabolism of fatty acids. It can cause a variety of symptoms, including muscle weakness, low blood sugar, and liver problems. In severe cases, it can be life-threatening.

In the medical field, "Cocos" is not a commonly used term. It is possible that you may be referring to "Coccyx," which is the tailbone or the last bone in the vertebral column. The coccyx is located at the base of the spine and is made up of four small bones called coccygeal vertebrae. It serves as an attachment point for muscles and ligaments that support the pelvic region and provides stability to the spine. Injuries or conditions that affect the coccyx can cause pain and discomfort in the lower back and buttocks.

Butyryl-CoA dehydrogenase (BCKD) is an enzyme that plays a crucial role in the metabolism of certain amino acids, specifically leucine, isoleucine, and valine. It is a member of the mitochondrial dehydrogenase family and is located in the inner mitochondrial membrane. The primary function of BCKD is to catalyze the oxidative decarboxylation of butyryl-CoA, a molecule derived from the metabolism of the branched-chain amino acids. This reaction generates acetyl-CoA, NADH, and CO2. The acetyl-CoA can then enter the citric acid cycle for energy production, while the NADH is used in the electron transport chain to generate ATP. Mutations in the BCKD gene can lead to a group of inherited metabolic disorders known as branched-chain ketoaciduria (BCKAU) or maple syrup urine disease (MSUD). These disorders are characterized by the accumulation of toxic branched-chain ketoacids in the blood and urine, which can lead to neurological damage and other complications if left untreated.

Butyrylcholinesterase (BuChE) is an enzyme that plays a crucial role in the breakdown of acetylcholine, a neurotransmitter that is involved in many important bodily functions. BuChE is primarily found in the blood and in the liver, but it is also present in other tissues throughout the body. In the medical field, BuChE is often measured as a way to assess liver function, as the enzyme is produced by liver cells. Abnormal levels of BuChE can be an indication of liver disease or other conditions that affect liver function. BuChE is also used as a biomarker for exposure to certain toxins, such as pesticides and heavy metals. In addition, researchers are studying BuChE as a potential target for the development of new drugs for the treatment of neurological disorders, such as Alzheimer's disease.

Butyrates are a group of fatty acids that are derived from butyric acid. They are commonly used in the medical field as a source of energy for the body, particularly for patients who are unable to digest other types of fats. Butyrates are also used in the treatment of certain medical conditions, such as inflammatory bowel disease and liver disease. They have been shown to have anti-inflammatory and immunomodulatory effects, and may help to improve gut health and reduce symptoms of these conditions.

L-Lactate Dehydrogenase (LDH) is an enzyme that plays a crucial role in the metabolism of lactate, a byproduct of cellular respiration. In the medical field, LDH is often used as a diagnostic marker for various diseases and conditions, including liver and heart diseases, cancer, and muscle injuries. LDH is found in many tissues throughout the body, including the liver, heart, muscles, kidneys, and red blood cells. When these tissues are damaged or injured, LDH is released into the bloodstream, which can be detected through blood tests. In addition to its diagnostic use, LDH is also used as a prognostic marker in certain diseases, such as cancer. High levels of LDH in the blood can indicate a more aggressive form of cancer or a poorer prognosis for the patient. Overall, LDH is an important enzyme in the body's metabolism and plays a critical role in the diagnosis and management of various medical conditions.

Alcohol dehydrogenase (ADH) is an enzyme that plays a key role in the metabolism of alcohol in the human body. It is found in many tissues, including the liver, brain, and stomach, but it is particularly abundant in the liver. When alcohol is consumed, it is absorbed into the bloodstream and eventually reaches the liver, where it is metabolized by ADH. ADH catalyzes the conversion of alcohol (ethanol) into acetaldehyde, a toxic substance that can cause a range of symptoms, including nausea, headache, and dizziness. Once acetaldehyde is formed, it is further metabolized by another enzyme called aldehyde dehydrogenase (ALDH) into acetate, a non-toxic substance that can be easily eliminated from the body in the form of carbon dioxide and water. ADH is also involved in the metabolism of other substances, including some drugs and toxins. In some cases, ADH activity can be affected by factors such as genetics, age, gender, and chronic alcohol consumption, which can impact the body's ability to metabolize alcohol and other substances.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in cellular metabolism. It is involved in the glycolytic pathway, which is the process by which cells convert glucose into energy. GAPDH catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate, which is an important step in the breakdown of glucose. In addition to its role in glycolysis, GAPDH has also been implicated in a variety of other cellular processes, including apoptosis (programmed cell death), inflammation, and the regulation of gene expression. It is also a commonly used biomarker in research and clinical settings, as it is expressed in many different types of cells and tissues and is relatively stable under a variety of conditions. GAPDH is a highly conserved enzyme, meaning that it is found in many different species and has a similar structure and function across these species. It is a homotetramer, meaning that it is composed of four identical subunits, and it is found in the cytoplasm of cells.

Aldehyde dehydrogenase (ALDH) is an enzyme that plays a crucial role in the metabolism of aldehydes, which are toxic compounds that can be produced during the breakdown of certain drugs, alcohol, and other substances. ALDH catalyzes the oxidation of aldehydes to their corresponding carboxylic acids, which are less toxic and can be further metabolized by other enzymes in the body. In the medical field, ALDH is important for detoxifying the body and preventing the accumulation of toxic aldehydes. Deficiency in ALDH can lead to a condition called aldehyde dehydrogenase deficiency, which can cause sensitivity to certain drugs and alcohol, as well as other health problems. ALDH is also a target for the development of new drugs for the treatment of various diseases, including cancer, neurodegenerative disorders, and alcohol addiction.

Glutamate dehydrogenase (GDH) is an enzyme that plays a crucial role in the metabolism of amino acids, particularly glutamate. It catalyzes the reversible conversion of glutamate to alpha-ketoglutarate, which is a key intermediate in the citric acid cycle. GDH is found in a variety of tissues, including the liver, kidney, and brain, and is involved in a number of metabolic processes, including gluconeogenesis, amino acid catabolism, and the regulation of nitrogen metabolism. In the medical field, GDH is often measured as a diagnostic marker for liver and kidney function, and it may also be used as a target for the development of new drugs for the treatment of various diseases, including cancer and neurological disorders.

Glucosephosphate dehydrogenase (GPD) is an enzyme that plays a crucial role in the metabolism of glucose. It is involved in the pentose phosphate pathway, which is a metabolic pathway that generates reducing equivalents in the form of NADPH and ribose-5-phosphate. In the context of the medical field, GPD deficiency is a rare genetic disorder that affects the production of NADPH, which is essential for the functioning of various bodily processes, including the production of red blood cells. GPD deficiency can lead to a range of symptoms, including anemia, jaundice, and neurological problems. In addition, GPD is also used as a diagnostic tool in the medical field, particularly in the diagnosis of certain types of cancer. High levels of GPD activity have been observed in certain types of cancer cells, including breast, ovarian, and lung cancer. This has led to the development of diagnostic tests that measure GPD activity in patient samples, which can help in the early detection and diagnosis of cancer.

Malate dehydrogenase (MDH) is an enzyme that plays a crucial role in cellular metabolism. It catalyzes the conversion of malate, a four-carbon compound, to oxaloacetate, a five-carbon compound, in the citric acid cycle. This reaction is reversible and can occur in both directions, depending on the cellular needs and the availability of energy. In the medical field, MDH is often studied in the context of various diseases and disorders. For example, mutations in the MDH gene have been associated with certain forms of inherited metabolic disorders, such as Leigh syndrome and MELAS (mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes). In addition, MDH has been implicated in the development of certain types of cancer, such as breast and prostate cancer, and may play a role in the progression of these diseases. Overall, MDH is an important enzyme in cellular metabolism and its dysfunction can have significant implications for human health.

Isocitrate dehydrogenase (IDH) is an enzyme that plays a critical role in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid cycle. It catalyzes the conversion of isocitrate to alpha-ketoglutarate (α-KG) in the presence of NAD+ as a cofactor. This reaction is an important step in the production of energy in the form of ATP through cellular respiration. In the medical field, IDH is of particular interest because mutations in the IDH1 and IDH2 genes have been implicated in the development of certain types of cancer, including gliomas, acute myeloid leukemia, and chondrosarcoma. These mutations result in the production of an abnormal form of the enzyme that has altered activity and can lead to the accumulation of alpha-ketoglutarate, which can promote tumor growth and progression. As a result, IDH mutations are now considered important biomarkers for the diagnosis and prognosis of certain types of cancer, and targeted therapies that inhibit the activity of mutant IDH enzymes are being developed for their treatment.

Alcohol oxidoreductases are a group of enzymes that catalyze the oxidation of alcohols. In the medical field, these enzymes are of particular interest because they play a key role in the metabolism of alcohol in the body. There are several different types of alcohol oxidoreductases, including alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). ADH is responsible for converting alcohol (ethanol) into acetaldehyde, a toxic substance that can cause a range of symptoms when present in high concentrations, including headache, nausea, and dizziness. ALDH is responsible for converting acetaldehyde into acetate, a non-toxic substance that can be further metabolized by the body. Alcohol oxidoreductases are found in a variety of tissues throughout the body, including the liver, brain, and lungs. In the liver, ADH and ALDH are particularly important for metabolizing alcohol, as this organ is responsible for processing a large amount of the alcohol that is consumed. Disruptions in the activity of alcohol oxidoreductases can lead to a range of health problems, including alcohol dependence, liver disease, and certain types of cancer. For example, individuals who are unable to effectively metabolize alcohol due to a deficiency in ADH or ALDH may be more susceptible to the negative effects of alcohol consumption, such as liver damage and addiction.

Dihydrolipoamide dehydrogenase (DLD) is an enzyme that plays a crucial role in the metabolism of carbohydrates and fatty acids in the body. It is also known as E3 of the pyruvate dehydrogenase complex (PDC) or dihydrolipoyl transacetylase. The PDC is a multi-enzyme complex that converts pyruvate, a product of glycolysis, into acetyl-CoA, which can then enter the citric acid cycle for further metabolism. DLD is the third enzyme in the PDC complex and is responsible for transferring electrons from dihydrolipoamide to ubiquinone, an electron carrier molecule that shuttles electrons to the electron transport chain for ATP production. DLD deficiency is a rare genetic disorder that can cause a range of symptoms, including muscle weakness, developmental delays, and neurological problems. It is caused by mutations in the DLD gene, which leads to a deficiency in the enzyme's activity. Treatment for DLD deficiency typically involves dietary modifications and supplements to support energy metabolism, as well as medications to manage symptoms.

Carbohydrate dehydrogenases are a group of enzymes that catalyze the oxidation of carbohydrates, such as glucose, fructose, and galactose, to produce aldehydes or ketones. These enzymes play important roles in various metabolic pathways, including glycolysis, the citric acid cycle, and the pentose phosphate pathway. There are several types of carbohydrate dehydrogenases, including glucose dehydrogenase, lactate dehydrogenase, and alcohol dehydrogenase. These enzymes are found in a variety of tissues, including the liver, muscle, and brain, and are involved in a range of physiological processes, such as energy metabolism, detoxification, and the synthesis of important molecules like nucleotides and amino acids. In the medical field, carbohydrate dehydrogenases are often used as diagnostic markers for various diseases and conditions. For example, elevated levels of lactate dehydrogenase in the blood can be an indicator of liver or muscle damage, while elevated levels of glucose dehydrogenase can be a sign of certain types of cancer or genetic disorders. Additionally, some carbohydrate dehydrogenases are used as targets for the development of new drugs and therapies.

Succinate dehydrogenase (SDH) is an enzyme that plays a crucial role in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid cycle. It is a complex enzyme that is composed of four protein subunits and one iron-sulfur flavoprotein subunit. In the citric acid cycle, SDH catalyzes the oxidation of succinate to fumarate, which is a key step in the production of energy in the form of ATP. This reaction also generates electrons that are used to reduce coenzyme Q, which is an electron carrier that is involved in the electron transport chain. SDH is found in the mitochondria of cells and is essential for the production of energy in the body. Mutations in the genes that encode the SDH subunits can lead to a group of rare inherited disorders known as succinate dehydrogenase deficiency (SDHD, SDHAF1, SDHB, SDHC, and SDHD2). These disorders can cause a range of symptoms, including muscle weakness, developmental delays, and neurological problems.

L-iditol 2-dehydrogenase is an enzyme that plays a role in the metabolism of L-iditol, a sugar alcohol that is found in some fruits and vegetables. This enzyme catalyzes the conversion of L-iditol to L-idonic acid, which is an intermediate in the metabolism of certain amino acids. L-iditol 2-dehydrogenase is found in a variety of organisms, including bacteria, fungi, and plants. In the medical field, this enzyme has been studied in relation to its potential role in the treatment of certain diseases, such as diabetes and obesity.

Glycerolphosphate dehydrogenase (GPDH) is an enzyme that plays a role in the metabolism of glycerol-3-phosphate, a molecule involved in the breakdown of fats. In the medical field, GPDH is often studied in the context of diseases such as diabetes, where abnormal metabolism of fats can lead to complications such as cardiovascular disease. GPDH is also involved in the production of NADPH, a molecule that plays a role in the detoxification of harmful substances in the body. In addition, GPDH has been proposed as a potential target for the development of new drugs for the treatment of various diseases, including cancer and neurodegenerative disorders.

NAD stands for nicotinamide adenine dinucleotide, which is a coenzyme found in all living cells. It plays a crucial role in various metabolic processes, including energy production, DNA repair, and regulation of gene expression. In the medical field, NAD is often used as a supplement to support cellular health and improve overall well-being. It is also being studied for its potential therapeutic applications in treating conditions such as depression, anxiety, and chronic pain.

Glucose 1-dehydrogenase (G1DH) is an enzyme that plays a role in the metabolism of glucose in the body. It is involved in the conversion of glucose to glucose-6-phosphate, which is an important step in the process of glycolysis, the breakdown of glucose to produce energy. G1DH is found in a variety of tissues in the body, including the liver, muscle, and pancreas. In the liver, G1DH is involved in the production of glucose from non-carbohydrate sources, such as amino acids and fatty acids. In the pancreas, G1DH is involved in the regulation of blood glucose levels by converting glucose to glucose-6-phosphate, which can then be stored as glycogen or used for energy. G1DH is also involved in the metabolism of other sugars, such as galactose and fructose.

Hydroxysteroid dehydrogenases (HSDs) are a group of enzymes that play a crucial role in the metabolism of steroid hormones in the body. These enzymes catalyze the conversion of one form of a steroid hormone to another by removing or adding a hydroxyl group. There are several types of HSDs, each with a specific function and localization in the body. For example, some HSDs are found in the liver, where they help regulate the levels of sex hormones such as estrogen and testosterone. Other HSDs are found in the brain, where they play a role in the regulation of mood and behavior. HSDs are also involved in the metabolism of other types of hormones, such as cortisol and aldosterone. Dysfunction of HSDs can lead to a variety of medical conditions, including hormonal imbalances, mood disorders, and metabolic disorders.

Aldehyde oxidoreductases (ALDHs) are a group of enzymes that play a crucial role in the metabolism of aldehydes, which are toxic compounds that can be produced during normal cellular metabolism or as a result of environmental exposure. ALDHs are found in many tissues throughout the body, including the liver, lungs, and kidneys, and they help to detoxify aldehydes by converting them into less toxic compounds. There are several different types of ALDHs, each with its own specific substrate and activity. Some ALDHs are involved in the metabolism of ethanol, while others are involved in the metabolism of other aldehydes, such as acetaldehyde, formaldehyde, and acrolein. ALDHs are also involved in the metabolism of certain drugs and toxins, and they have been implicated in the development of certain diseases, such as cancer and neurodegenerative disorders. In the medical field, ALDHs are often studied as potential targets for the development of new drugs and therapies. For example, drugs that inhibit ALDH activity have been shown to be effective in the treatment of certain types of cancer, and ALDHs are also being studied as potential biomarkers for the early detection of certain diseases. Additionally, ALDHs are being investigated as potential targets for the development of new therapies for the treatment of alcoholism and other addictions.

The Ketoglutarate Dehydrogenase Complex (KGDHC) is an enzyme complex that plays a crucial role in the citric acid cycle, also known as the Krebs cycle or TCA cycle. It is responsible for the oxidation of alpha-ketoglutarate, a molecule produced during the breakdown of amino acids, to succinyl-CoA, a molecule that enters the citric acid cycle. The KGDHC is a large multi-subunit enzyme complex that contains three different subunits: E1, E2, and E3. The E1 subunit catalyzes the oxidation of alpha-ketoglutarate to succinyl-CoA, while the E2 subunit catalyzes the transfer of electrons from the alpha-ketoglutarate to the E3 subunit. The E3 subunit then transfers the electrons to the electron transport chain, which generates ATP, the energy currency of the cell. The KGDHC is an important enzyme complex in the citric acid cycle because it is the first step in the cycle that requires oxygen. It is also a key enzyme in the metabolism of amino acids, as it is involved in the breakdown of glutamate, a major amino acid in the body. Disruptions in the function of the KGDHC can lead to a variety of metabolic disorders, including Leigh syndrome, a rare genetic disorder that affects the brain and muscles.

Coenzyme A (CoA) is a small molecule that plays a crucial role in many metabolic pathways in the body. It is a thiol group (a sulfur-containing molecule) attached to a fatty acid molecule, and it serves as a carrier molecule for fatty acids in the body. In the medical field, CoA is involved in a variety of processes, including the breakdown of carbohydrates, fats, and proteins, as well as the synthesis of lipids and cholesterol. It is also involved in the metabolism of certain drugs and toxins. Disruptions in CoA metabolism can lead to a variety of medical conditions, including fatty acid oxidation disorders, which are a group of rare genetic disorders that affect the body's ability to break down fatty acids for energy. These disorders can cause a range of symptoms, including muscle weakness, developmental delays, and neurological problems. In addition, CoA is also involved in the metabolism of certain vitamins and minerals, such as vitamin B12 and selenium, and deficiencies in these nutrients can also affect CoA metabolism and lead to health problems.

Glucose dehydrogenases are a group of enzymes that catalyze the oxidation of glucose to gluconolactone, with the concomitant reduction of NADP+ to NADPH. There are several types of glucose dehydrogenases, including glucose dehydrogenase from Leuconostoc mesenteroides, glucose dehydrogenase from Aspergillus niger, and glucose dehydrogenase from Pseudomonas aeruginosa. These enzymes are used in various medical applications, such as the diagnosis of diabetes, the determination of blood glucose levels, and the production of antibiotics.

3-Hydroxysteroid dehydrogenases (3-HSDs) are a group of enzymes that play a crucial role in the metabolism of steroid hormones in the body. These enzymes are responsible for converting 3-hydroxysteroids, which are derivatives of cholesterol, into their corresponding 3-ketosteroids. There are several types of 3-HSDs, including NAD-dependent and NADP-dependent enzymes, which are found in different tissues throughout the body. For example, the NAD-dependent 3-HSD is found in the liver and is involved in the metabolism of cortisol, aldosterone, and other glucocorticoids. The NADP-dependent 3-HSD is found in the adrenal gland and is involved in the metabolism of androgens and estrogens. Disruptions in the activity of 3-HSDs can lead to a variety of medical conditions, including hormonal imbalances, metabolic disorders, and reproductive problems. For example, mutations in the gene encoding the NAD-dependent 3-HSD can cause a rare genetic disorder called 3-beta-hydroxysteroid dehydrogenase deficiency, which can lead to the accumulation of 3-hydroxysteroids in the body and cause a range of symptoms, including adrenal insufficiency, ambiguous genitalia, and adrenal hyperplasia.

Phosphogluconate dehydrogenase (PGD) is an enzyme that plays a crucial role in the pentose phosphate pathway (PPP), a metabolic pathway that generates reducing equivalents (NADPH) and ribose-5-phosphate, a precursor of nucleotides. PGD catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose-5-phosphate, with the concomitant reduction of NADP+ to NADPH. This reaction is the first step in the oxidative branch of the PPP, which generates NADPH for biosynthetic reactions such as fatty acid synthesis and steroidogenesis. PGD is found in many tissues, including liver, kidney, and red blood cells, and its activity is regulated by various factors, including substrate availability, allosteric effectors, and post-translational modifications. Mutations in the gene encoding PGD can lead to inherited disorders such as hereditary fructose intolerance and glucose-6-phosphate dehydrogenase deficiency.

Sugar alcohol dehydrogenases are enzymes that catalyze the oxidation of sugar alcohols, such as sorbitol and xylitol, to their corresponding ketones or aldehydes. These enzymes play an important role in the metabolism of sugar alcohols in the body, particularly in the liver and kidneys. In the medical field, sugar alcohol dehydrogenases are often studied in the context of diabetes and other metabolic disorders, as well as in the development of new treatments for these conditions.

NADH dehydrogenase, also known as Complex I, is a large enzyme complex that plays a central role in the electron transport chain (ETC) in mitochondria. It is responsible for transferring electrons from NADH, a molecule produced during cellular respiration, to ubiquinone (CoQ), a mobile electron carrier that shuttles electrons to the next enzyme in the ETC. The NADH dehydrogenase complex is composed of 45 different subunits, including 14 core subunits that are essential for its function. It is located in the inner mitochondrial membrane and is the first enzyme in the ETC to receive electrons from NADH. The function of NADH dehydrogenase is to pump protons (H+) from the mitochondrial matrix to the intermembrane space, creating a proton gradient that drives the synthesis of ATP, the cell's primary energy currency. In addition, NADH dehydrogenase also plays a role in regulating the flow of electrons through the ETC and the production of reactive oxygen species (ROS), which can cause cellular damage if not properly controlled. Disruptions in the function of NADH dehydrogenase can lead to a variety of diseases, including mitochondrial disorders, neurodegenerative diseases, and certain types of cancer.

IMP dehydrogenase (Inosine 5'-Monophosphate Dehydrogenase) is an enzyme that plays a crucial role in the metabolism of purines, which are essential building blocks of nucleic acids such as DNA and RNA. The enzyme catalyzes the conversion of inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP), which is a precursor for the synthesis of guanine nucleotides. IMP dehydrogenase is involved in the regulation of purine biosynthesis and is a key target for the treatment of certain diseases, including cancer. In cancer cells, the enzyme is often overexpressed, leading to an increased production of guanine nucleotides and promoting cell proliferation and survival. Therefore, inhibitors of IMP dehydrogenase have been developed as potential cancer therapeutics. In addition to its role in purine metabolism, IMP dehydrogenase has also been implicated in the regulation of other cellular processes, such as cell differentiation and apoptosis.

Lactate dehydrogenases (LDHs) are a group of enzymes that play a crucial role in the metabolism of lactate, a byproduct of cellular respiration. In the medical field, LDHs are commonly used as a diagnostic tool to detect and monitor various diseases and conditions, including liver and heart diseases, cancer, and muscle injuries. LDHs are found in many tissues throughout the body, including the liver, heart, muscles, kidneys, and red blood cells. When these tissues are damaged or injured, LDHs are released into the bloodstream, which can be detected through blood tests. Elevated levels of LDH in the blood can indicate a variety of conditions, such as heart attack, liver disease, muscle damage, or cancer. In addition to their diagnostic use, LDHs are also used in research and drug development. For example, they are often used as a marker of cell viability and function in cell culture studies, and they are also used to study the metabolism of lactate in various organisms.

Formate dehydrogenases are enzymes that catalyze the oxidation of formate to carbon dioxide and hydrogen. They are found in a variety of organisms, including bacteria, archaea, and eukaryotes, and play important roles in various metabolic pathways. In the medical field, formate dehydrogenases are of interest because they are involved in the metabolism of certain drugs and toxins. For example, some bacteria and fungi produce formate dehydrogenases as a defense mechanism against antibiotics, allowing them to survive in the presence of these drugs. In addition, formate dehydrogenases are also involved in the metabolism of methanol, a toxic substance that can cause blindness and other health problems if ingested in large quantities. Formate dehydrogenases are also being studied as potential targets for the development of new antibiotics and antifungal agents. By inhibiting these enzymes, it may be possible to disrupt the metabolism of harmful bacteria and fungi, thereby treating infections caused by these organisms.

17-Hydroxysteroid dehydrogenases (17-HSDs) are a group of enzymes that play a crucial role in the metabolism of sex hormones in the human body. These enzymes are responsible for converting one form of a sex hormone into another, which can affect the hormone's activity and impact various physiological processes. There are several types of 17-HSDs, each with a specific function. For example, 17-HSD1 is involved in the conversion of estradiol to estrone, while 17-HSD2 is involved in the conversion of testosterone to dihydrotestosterone. These enzymes are found in various tissues throughout the body, including the liver, adrenal glands, and reproductive organs. Abnormalities in the activity of 17-HSDs can lead to various medical conditions, such as polycystic ovary syndrome (PCOS), which is characterized by hormonal imbalances and irregular menstrual cycles. In addition, some forms of cancer, such as breast and ovarian cancer, have been linked to changes in the activity of 17-HSDs. Overall, 17-HSDs play a critical role in regulating sex hormone metabolism and are an important area of research in the field of endocrinology.

Xanthine dehydrogenase (XDH) is an enzyme that plays a crucial role in the metabolism of purines, which are nitrogen-containing compounds found in all living cells. XDH catalyzes the conversion of xanthine to uric acid, which is the final product of purine metabolism in humans and many other animals. XDH is a mitochondrial enzyme that is encoded by the XDH gene and is found in many tissues throughout the body, including the liver, kidneys, and intestines. It is also present in red blood cells and is involved in the regulation of oxygen transport. In addition to its role in purine metabolism, XDH has been implicated in a number of other biological processes, including the regulation of energy metabolism, the detoxification of reactive oxygen species, and the maintenance of cellular redox balance. Disruptions in XDH activity can lead to a number of medical conditions, including xanthinuria, which is a rare genetic disorder characterized by the accumulation of xanthine in the blood and urine. Xanthinuria can cause a range of symptoms, including abdominal pain, nausea, and vomiting, and can also lead to the formation of kidney stones.

Hydroxybutyrate dehydrogenase (HBDH) is an enzyme that plays a role in the metabolism of ketone bodies, which are produced in the liver when the body is in a state of ketosis. Ketosis occurs when the body is unable to use glucose as its primary source of energy and begins to break down fatty acids instead. The ketone bodies produced during this process are beta-hydroxybutyrate, acetoacetate, and acetone. HBDH is responsible for converting beta-hydroxybutyrate into acetoacetate, which is then further metabolized by other enzymes in the liver. This process is an important part of the body's ability to utilize ketone bodies as a source of energy, particularly during periods of fasting or prolonged exercise. In the medical field, HBDH is sometimes measured as a diagnostic tool to help identify and monitor conditions that can lead to ketosis, such as diabetes, liver disease, and certain types of cancer. Abnormal levels of HBDH can also be an indicator of certain genetic disorders, such as maple syrup urine disease.

Oxidoreductases are a class of enzymes that catalyze redox reactions, which involve the transfer of electrons from one molecule to another. These enzymes play a crucial role in many biological processes, including metabolism, energy production, and detoxification. In the medical field, oxidoreductases are often studied in relation to various diseases and conditions. For example, some oxidoreductases are involved in the metabolism of drugs and toxins, and changes in their activity can affect the efficacy and toxicity of these substances. Other oxidoreductases are involved in the production of reactive oxygen species (ROS), which can cause cellular damage and contribute to the development of diseases such as cancer and aging. Oxidoreductases are also important in the diagnosis and treatment of certain diseases. For example, some oxidoreductases are used as markers of liver disease, and changes in their activity can indicate the severity of the disease. In addition, some oxidoreductases are targets for drugs used to treat diseases such as cancer and diabetes. Overall, oxidoreductases are a diverse and important class of enzymes that play a central role in many biological processes and are the subject of ongoing research in the medical field.

Ketone oxidoreductases are a group of enzymes that catalyze the oxidation of ketone bodies, which are metabolic intermediates produced during the breakdown of fatty acids in the liver. These enzymes play a crucial role in the metabolism of ketone bodies, which are important sources of energy for the brain and other tissues during periods of fasting or starvation. There are several different types of ketone oxidoreductases, including the following: 1. Acetoacetate decarboxylase: This enzyme catalyzes the conversion of acetoacetate to acetone and carbon dioxide. 2. Beta-hydroxybutyrate dehydrogenase: This enzyme catalyzes the conversion of beta-hydroxybutyrate to acetoacetate and NADH. 3. 3-hydroxy-3-methylglutaryl-CoA synthase: This enzyme catalyzes the conversion of acetoacetate to 3-hydroxy-3-methylglutaryl-CoA, which is an intermediate in the synthesis of cholesterol and other lipids. Disruptions in the function of ketone oxidoreductases can lead to metabolic disorders such as maple syrup urine disease, which is caused by a deficiency in the enzyme branched-chain alpha-keto acid dehydrogenase.

11-beta-Hydroxysteroid dehydrogenases (11β-HSDs) are a group of enzymes that play a crucial role in regulating the levels of active glucocorticoids in the body. These enzymes are found in various tissues, including the liver, adipose tissue, and the brain. There are two main isoforms of 11β-HSD: 11β-HSD1 and 11β-HSD2. 11β-HSD1 converts inactive cortisone to its active form, cortisol, in the liver and adipose tissue. This enzyme is involved in the regulation of glucose metabolism, insulin sensitivity, and inflammation. On the other hand, 11β-HSD2 converts active cortisol to its inactive form, cortisone, in the kidneys and other tissues. This enzyme helps to protect the body from the harmful effects of excess cortisol, such as weight gain, insulin resistance, and high blood pressure. Dysregulation of 11β-HSD activity has been implicated in various diseases, including obesity, diabetes, cardiovascular disease, and depression. Therefore, understanding the role of 11β-HSDs in the body and developing drugs that target these enzymes may have therapeutic potential for the treatment of these diseases.

NADP stands for Nicotinamide Adenine Dinucleotide Phosphate. It is a coenzyme that plays a crucial role in various metabolic processes in the body, including the metabolism of carbohydrates, fats, and proteins. NADP is involved in the conversion of glucose to glycogen, the breakdown of fatty acids, and the synthesis of amino acids. It is also involved in the process of photosynthesis in plants, where it acts as a carrier of electrons. In the medical field, NADP is often used as a supplement to support various metabolic processes and to enhance energy production in the body.

Uridine diphosphate glucose dehydrogenase (UDPGD) is an enzyme that plays a crucial role in the metabolism of glucose in the body. It is responsible for converting uridine diphosphate glucose (UDP-Glc) to glucose-6-phosphate (Glc-6-P), which is an important intermediate in the glycolytic pathway. UDP-Glc is a sugar that is synthesized in the liver and transported to other tissues, where it is used as a building block for the synthesis of glycogen, glycoproteins, and glycolipids. UDPGD is located in the cytosol of cells and is found in a variety of tissues, including liver, muscle, and brain. In the medical field, UDPGD is important because it is involved in the metabolism of glucose, which is a key source of energy for the body. Abnormalities in UDPGD activity can lead to a variety of metabolic disorders, including glycogen storage diseases and glucose-6-phosphate dehydrogenase deficiency. In addition, UDPGD is a potential target for the development of new drugs for the treatment of these disorders.

Glucosephosphate dehydrogenase (G6PD) deficiency is a genetic disorder that affects the body's ability to produce energy. It is caused by a deficiency in the enzyme glucose-6-phosphate dehydrogenase (G6PD), which is responsible for producing NADPH, a molecule that is essential for the production of energy in the body's cells. People with G6PD deficiency are more susceptible to certain infections, particularly those caused by the malaria parasite, as well as certain medications and foods. The symptoms of G6PD deficiency can vary widely, but may include anemia, jaundice, and abdominal pain. In severe cases, G6PD deficiency can lead to life-threatening complications, such as hemolytic anemia, which is a condition in which the body destroys its own red blood cells. G6PD deficiency is inherited in an X-linked recessive pattern, which means that it is more common in males than in females. It is estimated that G6PD deficiency affects millions of people worldwide, with the highest prevalence in certain populations in Africa, Asia, and the Mediterranean.

11-beta-Hydroxysteroid Dehydrogenase Type 1 (11β-HSD1) is an enzyme that plays a crucial role in regulating the levels of cortisol, a hormone produced by the adrenal gland. It is expressed in various tissues throughout the body, including the liver, muscle, adipose tissue, and brain. The primary function of 11β-HSD1 is to convert inactive cortisone to its active form, cortisol. This conversion occurs in the liver and adipose tissue, where 11β-HSD1 is highly expressed. Cortisol is a key hormone involved in the body's stress response and plays a role in regulating metabolism, immune function, and blood pressure. In addition to its role in cortisol metabolism, 11β-HSD1 has also been implicated in the development of various diseases, including obesity, diabetes, cardiovascular disease, and depression. For example, increased activity of 11β-HSD1 in adipose tissue has been linked to insulin resistance and the development of type 2 diabetes. Similarly, increased activity of 11β-HSD1 in the brain has been linked to depression and anxiety. Overall, 11β-HSD1 is a critical enzyme involved in regulating cortisol metabolism and has important implications for the development of various diseases.

Alanine dehydrogenase (ALDH) is an enzyme that plays a crucial role in the metabolism of amino acids in the body. It catalyzes the conversion of alanine to pyruvate, which is a key intermediate in the breakdown of glucose to produce energy. ALDH is found in many tissues throughout the body, including the liver, kidneys, and muscles. In the medical field, ALDH is often measured as a diagnostic marker for liver disease, as levels of the enzyme can be elevated in people with liver damage or cirrhosis. ALDH is also used as a target for the development of new drugs for the treatment of liver disease and other conditions. Additionally, ALDH has been studied as a potential therapeutic target for the treatment of certain types of cancer, as high levels of the enzyme have been associated with poor prognosis in some cases.

Mannitol dehydrogenases are enzymes that catalyze the oxidation of mannitol to fructose-1,6-bisphosphate. These enzymes are important in the metabolism of mannitol, a sugar alcohol that is found in some plants and microorganisms. In the medical field, mannitol dehydrogenases are of interest because they are involved in the metabolism of mannitol in the body, and changes in the activity of these enzymes may be associated with certain diseases or conditions. For example, increased activity of mannitol dehydrogenases has been observed in some cases of liver disease, and decreased activity has been associated with certain types of cancer.

Acyl Coenzyme A (acyl-CoA) is a molecule that plays a central role in metabolism. It is formed when an acyl group (a fatty acid or other long-chain hydrocarbon) is attached to the coenzyme A molecule, which is a small molecule that contains a thiol (-SH) group. Acyl-CoA molecules are involved in a variety of metabolic processes, including the breakdown of fatty acids (beta-oxidation), the synthesis of fatty acids (fatty acid synthesis), and the synthesis of other important molecules such as cholesterol and ketone bodies. In the medical field, acyl-CoA is often measured as a way to assess the activity of certain metabolic pathways, and imbalances in acyl-CoA levels can be associated with a variety of diseases and disorders.

In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.

Hydroxyprostaglandin dehydrogenases (HPGDs) are a group of enzymes that play a role in the metabolism of hydroxyprostaglandins (HPGs), which are signaling molecules derived from prostaglandins. HPGs are involved in a variety of physiological processes, including inflammation, pain, and blood pressure regulation. HPGDs are responsible for converting HPGs into their corresponding prostaglandin metabolites, which are inactive forms of the molecule. There are several different HPGD enzymes, each with its own specific substrate specificity and tissue distribution. In the medical field, HPGDs have been studied in relation to a number of diseases and conditions, including inflammatory disorders, cardiovascular disease, and cancer. For example, some studies have suggested that HPGD activity may be involved in the development of certain types of cancer, and that inhibitors of HPGD may have potential as therapeutic agents for these diseases.

Retinal dehydrogenase is an enzyme that plays a crucial role in the visual process. It is responsible for converting the light-sensitive molecule retinal into retinoic acid, which is then used by the retina to detect light and send signals to the brain. Retinal dehydrogenase is found in the retina of the eye and is essential for normal vision. In the medical field, it is studied in the context of various eye diseases, such as retinitis pigmentosa, which is a genetic disorder that leads to progressive vision loss.

Acyl-CoA dehydrogenase, long-chain (ACADL) is an enzyme that plays a crucial role in the metabolism of fatty acids. It is a member of the acyl-CoA dehydrogenase family of enzymes, which are responsible for catalyzing the first step in the breakdown of fatty acids in the mitochondria of cells. Specifically, ACADL catalyzes the oxidative decarboxylation of long-chain fatty acyl-CoAs, which are the primary substrates for fatty acid oxidation. This reaction generates FADH2 and acyl-CoA, which can then be further metabolized through the citric acid cycle to produce energy in the form of ATP. Mutations in the ACADL gene can lead to a deficiency in the enzyme, which can result in a rare inherited disorder called long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHAD deficiency). This disorder is characterized by a deficiency in the ability to break down fatty acids, which can lead to a buildup of toxic intermediates in the body and cause a range of symptoms, including muscle weakness, liver dysfunction, and heart problems.

20-Hydroxysteroid dehydrogenases (20-HSDs) are a group of enzymes that play a crucial role in the metabolism of various hormones, including cortisol, aldosterone, and androgens. These enzymes are responsible for converting the active forms of these hormones into their inactive forms, which are then excreted from the body. In the medical field, 20-HSDs are often studied in the context of various diseases and disorders, including Cushing's syndrome, Addison's disease, and polycystic ovary syndrome (PCOS). In Cushing's syndrome, for example, the overproduction of cortisol is often caused by a malfunction in the 20-HSD enzyme responsible for converting cortisol to its inactive form. In Addison's disease, the deficiency of this enzyme can lead to a deficiency in cortisol production. In PCOS, the activity of 20-HSD enzymes has been shown to be altered, leading to an imbalance in the levels of androgens and estrogens. This can contribute to the development of symptoms such as irregular menstrual cycles, excess hair growth, and infertility. Overall, 20-HSDs play a critical role in regulating hormone levels in the body, and their dysfunction can have significant implications for various medical conditions.

11-beta-Hydroxysteroid Dehydrogenase Type 2 (11β-HSD2) is an enzyme that plays a crucial role in regulating the levels of cortisol, a hormone produced by the adrenal gland. It is primarily found in the liver, kidney, and adipose tissue. The primary function of 11β-HSD2 is to convert cortisol to its inactive form, cortisone. This process helps to prevent cortisol from exerting its effects on various tissues throughout the body, including the brain, muscles, and immune system. In the medical field, 11β-HSD2 is of particular interest because of its role in the development of metabolic disorders such as obesity, insulin resistance, and type 2 diabetes. Studies have shown that individuals with reduced activity of 11β-HSD2 are less likely to develop these conditions, suggesting that the enzyme may play a protective role against metabolic disease. In addition, 11β-HSD2 has been implicated in the development of certain psychiatric disorders, such as depression and anxiety. Research has shown that individuals with reduced activity of 11β-HSD2 may be more susceptible to the effects of stress and may be at increased risk for developing these conditions. Overall, 11β-HSD2 is a critical enzyme that plays a key role in regulating cortisol levels and maintaining metabolic and psychiatric health.

Acetyl Coenzyme A (Acetyl-CoA) is a molecule that plays a central role in metabolism in all living organisms. It is a key intermediate in the breakdown of carbohydrates, fats, and proteins, and is involved in the synthesis of fatty acids, cholesterol, and ketone bodies. In the medical field, Acetyl-CoA is often studied in the context of diseases such as diabetes, obesity, and metabolic disorders. For example, in type 2 diabetes, the body's ability to regulate blood sugar levels is impaired, which can lead to an accumulation of Acetyl-CoA in the liver. This can cause the liver to produce more fatty acids and triglycerides, leading to the development of fatty liver disease. In addition, Acetyl-CoA is also involved in the production of energy in the form of ATP (adenosine triphosphate), which is the primary energy currency of the cell. Therefore, disruptions in Acetyl-CoA metabolism can have significant effects on energy production and overall health.

Isovaleryl-CoA dehydrogenase (IVD) is an enzyme that plays a crucial role in the metabolism of fatty acids. It is a member of the mitochondrial trifunctional protein complex, which is responsible for the oxidative decarboxylation of three different substrates: isovaleryl-CoA, 2-methylbutyryl-CoA, and propionyl-CoA. In the medical field, IVD deficiency is a rare genetic disorder that affects the metabolism of fatty acids. It is caused by mutations in the ACAD8 gene, which encodes the IVD enzyme. The deficiency leads to the accumulation of isovaleryl-CoA and its toxic metabolites in the body, which can cause a range of symptoms, including muscle weakness, developmental delays, and neurological problems. Diagnosis of IVD deficiency typically involves blood tests to measure the levels of isovaleryl-CoA and its metabolites, as well as genetic testing to identify mutations in the ACAD8 gene. Treatment for the disorder typically involves a low-protein diet and supplementation with certain amino acids to help prevent the accumulation of toxic metabolites. In severe cases, liver transplantation may be necessary.

Homoserine dehydrogenase is an enzyme that plays a crucial role in the biosynthesis of the amino acid methionine in the human body. It catalyzes the conversion of homoserine to threonine, which is a precursor to methionine. In the medical field, homoserine dehydrogenase deficiency is a rare genetic disorder that results in the accumulation of homoserine in the body. This can lead to a range of symptoms, including intellectual disability, seizures, and developmental delays. The diagnosis of homoserine dehydrogenase deficiency is typically made through blood tests that measure the levels of homoserine and threonine in the body. Treatment typically involves a special diet that is low in methionine and supplemented with threonine and other essential amino acids. In some cases, enzyme replacement therapy may also be used to treat the condition.

"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 ... 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 ...

https://en.wikipedia.org/wiki/Short-chain_acyl-coenzyme_A_dehydrogenase_deficiency

3-hydroxy butyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent ... Butyryl-CoA is a precursor to and converted from crotonyl-CoA. This interconversion is mediated by butyryl-COA dehydrogenase. ... Butyryl-coenzyme A (or butyryl-CoA) is the coenzyme A-containing derivative of butyric acid. It is acted upon by butyryl-CoA ... "Butyryl-CoA". pubchem.ncbi.nlm.nih.gov. Retrieved 2021-11-18. Acyl-CoA Fatty acyl-CoA esters "Human Metabolome Database: ...

https://en.wikipedia.org/wiki/Butyryl-CoA

... 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 ...

https://en.wikipedia.org/wiki/ACADS

"The deuterium isotope effect upon the reaction of fatty acyl-CoA dehydrogenase and butyryl-CoA". J. Biol. Chem. 255 (19): 9093- ...

https://en.wikipedia.org/wiki/Hydrogen

... (EC 1.3.8.1, butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase, butyryl dehydrogenase, ... Acyl-CoA dehydrogenase Medium-chain acyl-CoA dehydrogenase Butyryl-CoA (also known as butanoyl-CoA) Mahler HR (January 1954). " ... butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl ... Short-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ...

https://en.wikipedia.org/wiki/Short-chain_acyl-CoA_dehydrogenase

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 ...

https://en.wikipedia.org/wiki/3-hydroxy-2-methylbutyryl-CoA_dehydrogenase

... on NADPH dehydrogenase ("old yellow enzyme"), David P. Ballou, and Paul Engel on butyryl-CoA dehydrogenase, among others. I.C.I ... Engel, Paul C.; Massey, V. (1971). "Green butyryl-coenzyme a dehydrogenase. An enzyme-acyl-coenzyme a complex". Biochemical ... Moore, E G; Cardemil, E; Massey, V (1978). "Production of a covalent flavin linkage in lipoamide dehydrogenase - reaction with ... Singer, Thomas P.; Kearney, Edna B.; Massey, Vincent (1956). "Observations on the flavin moiety of succinic dehydrogenase". ...

https://en.wikipedia.org/wiki/Vincent_Massey_(enzymologist)

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 ...

https://en.wikipedia.org/wiki/Methylene_cyclopropyl_acetic_acid

... (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 U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with ...

https://en.wikipedia.org/wiki/Crotonyl-CoA_reductase

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 ...

https://en.wikipedia.org/wiki/CaiA_RNA_motif

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 ...

https://en.wikipedia.org/wiki/Β-Hydroxybutyric_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 ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

... butyryl-CoA dehydrogenase. EC 1.3.99.3: now EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA ... glutaryl-CoA dehydrogenase (ETF) EC 1.3.8.7: medium-chain acyl-CoA dehydrogenase EC 1.3.8.8: long-chain acyl-CoA dehydrogenase ... benzylsuccinyl-CoA dehydrogenase EC 1.3.8.4: isovaleryl-CoA dehydrogenase EC 1.3.8.5: 2-methyl-branched-chain-enoyl-CoA ... 3-hydroxyacyl-CoA dehydrogenase EC 1.1.1.36: acetoacetyl-CoA reductase EC 1.1.1.37: malate dehydrogenase EC 1.1.1.38: malate ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)

"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). ...

https://en.wikipedia.org/wiki/ACAD9

CoA → −O2CCH2−Ac + Ac−CoA Acetoacetyl-CoA can come from beta oxidation of butyryl-CoA: Et−CH2C(O)−CoA + 2NAD+ + H2O + FAD → Ac− ... 3-Hydroxybutyrate dehydrogenase "Front Matter". Nomenclature of Organic Chemistry : IUPAC Recommendations and Preferred Names ... CH2C(O)−CoA + 2NADH + FADH2 Condensation of pair of acetyl CoA molecules as catalyzed by thiolase.: 393 2Ac−CoA → AcCH2C(O)−CoA ... CoA): AcCH2C(O)−CoA + OH− → AcCH2CO−2 + H−CoA The acetoacetate-CoA itself is formed by three routes: 3-hydroxy-3-methylglutaryl ...

https://en.wikipedia.org/wiki/Acetoacetic_acid

... 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 ...

https://en.wikipedia.org/wiki/Propionyl-CoA

... 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 v t e (Articles without EBI source, Articles without KEGG source, ECHA InfoCard ID ... "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 ...

https://en.wikipedia.org/wiki/Crotonyl-CoA

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 ...

https://en.wikipedia.org/wiki/Coenzyme_A

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 ...

https://en.wikipedia.org/wiki/Fatty_acid_synthesis

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. ...

https://en.wikipedia.org/wiki/Chloroplast

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 ...

https://medlineplus.gov/genetics/condition/short-chain-acyl-coa-dehydrogenase-deficiency/

... including butyryl CoA, glutaryl CoA, and isovaleryl CoA. As a result of the inhibition of butyryl CoA dehydrogenase, the ... The inhibition of glutaryl CoA dehydrogenase results in the accumulation of glutaryl CoA, which could inhibit ... Because NADH and acetyl CoA are required as a cofactor of 3-phosphoglyceraldehyde phosphate dehydrogenase and as an activator ... oxidation of long-chain fatty acids stops at the level of hexanoyl CoA and butyryl CoA. This effect leads to the decreased ...

https://emedicine.medscape.com/article/1008792-overview

In addition to the central catalysts, CO dehydrogenase and acetyl-CoA synthase, ATPases are needed in the pathway. This allows ... acetyl-CoA) pathway, also known as the Wood-Ljungdahl pathway, allows reduction and condensation of two molecules of carbon ... dioxide (CO 2 ) to build the acetyl-group of acetyl-CoA. Productive utilization of CO 2 relies on a set of oxygen sensitive ... metalloenzymes exploiting the metal organic chemistry of nickel and cobalt to synthesize acetyl-CoA from activated one-carbon ...

https://www.degruyter.com/document/doi/10.1515/hsz-2013-0290/html

Isovaleryl-CoA dehydrogenase (EC 1.3.8.4). 76%. 606.7. lo. HSERO_RS04640. butyryl-CoA dehydrogenase. glutaryl-CoA dehydrogenase ... isovaleryl-CoA dehydrogenase. glutaryl-CoA dehydrogenase (ETF) (EC 1.3.8.6) (characterized). 37%. 93%. 231.1. ... 2 candidates for gcdH: glutaryl-CoA dehydrogenase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. Other hit. Other id. ... 2-methyl-branched-chain-enoyl-CoA reductase (EC 1.3.8.5). 64%. 496.5. ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&orgId=FitnessBrowser__HerbieS&path=proline&step=gcdH

Butyryl-CoA Dehydrogenase, subunit A; domain 3. MOB kinase activator. 4lqqB00. 1R3BA 4J1VA 4LQQB 5B5VA 4LQSB 5BRKA 4JIZA 5B6BA ...

https://genus.fuw.edu.pl/view/4LQQ/B/

Über das Vorkommen einer Reduktase von Δ²-Carbonsäuren in Clostridium kluyveri mit einer von der Butyryl-CoA-Dehydrogenase ...

https://epub.uni-regensburg.de/view/year/1975.html

https://emedicine.dev01.medscape.com/article/1008792-overview

2-methylacyl-CoA dehydrogenase Medicine & Life Sciences 72% * Butyryl-CoA Dehydrogenase Medicine & Life Sciences 63% ... Short/branched chain acyl-CoA dehydrogenase (SBCAD) deficiency, also known as 2-methylbutyryl-CoA dehydrogenase deficiency, is ... N2 - Short/branched chain acyl-CoA dehydrogenase (SBCAD) deficiency, also known as 2-methylbutyryl-CoA dehydrogenase deficiency ... AB - Short/branched chain acyl-CoA dehydrogenase (SBCAD) deficiency, also known as 2-methylbutyryl-CoA dehydrogenase deficiency ...

https://mayoclinic.elsevierpure.com/en/publications/characterization-of-new-acadsb-gene-sequence-mutations-and-clinic

4-hydroxybutyrate CoA transferase; abfD (CD2341), vinylacetyl-coa-d-isomerase; bcd2 (CD1054), butyryl-CoA dehydrogenase; etfBA ... 3-hydroxybutyryl-CoA dehydrogenase; crt2 (CD1057), 3-hydroxybutyryl-CoA dehydratase; cat1 (CD2343), succinyl-CoA: coenzyme A ... 2-hydroxyisocaproate CoA transferase; hadI (CD0396), activator of dehydratase; acdB (CD0399), acyl-CoA dehydrogenase; gcvTPA ( ... The pathways allowing the synthesis of butyryl-CoA from acetyl-CoA (CD1054- CD1059) or succinate (CD2344-CD2338) and the ...

https://studyres.com/doc/15796727/global-transcriptional-control-by-glucose-and

Butyrate-related genes, mainly encoding butyryl-CoA: acetate CoA-transferase (but), were predominantly associated with ... Among them, D-lactate dehydrogenase (ldhA) and L-lactate dehydrogenase (ldhB) were most important for the transition between D/ ... 3-Ketoacyl-CoA synthase (KCS) is a rate-limiting enzyme for VLCFA biosynthesis. In this study, we isolated KCS10, a KCS gene ... A 3-Ketoacyl-CoA Synthase 10 (KCS10) Homologue from Alfalfa Enhances Drought Tolerance by Regulating Cuticular Wax Biosynthesis ...

https://pesquisa.bvsalud.org/portal/?lang=pt&q=mh:Medicago+sativa/gen%C3%A9tica

... crotonyl-CoA, butanoyl-CoA = butyryl-CoA. Other name(s): butyryl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA ... Glossary: (E)-but-2-enoyl-CoA = crotonyl-CoA Other name(s): bifurcating butyryl-CoA dehydrogenase; butyryl-CoA dehydrogenase/ ... bifurcating butanoyl-CoA dehydrogenase; butanoyl-CoA dehydrogenase/Etf complex; butanoyl-CoA dehydrogenase (NAD+, ferredoxin). ... Glossary: acrylyl-CoA = acryloyl-CoA. propanoyl-CoA = propionyl-CoA. Systematic name: propanoyl-CoA:NADP+ oxidoreductase. ...

https://iubmb.qmul.ac.uk/enzyme/EC1/0301b.html

MonounsaturatedCarnitineButyryl-CoA DehydrogenasePyruvatesTetrahydrofolatesIsocitrate DehydrogenaseCrotonatesAcyl Carrier ... acetyl coenzyme A synthase/carbon monoxide dehydrogenase, acetyl-CoA synthase/carbon monoxide dehydrogenase, ACS/CODH, Carbon ... TransketolaseMalatesEnzyme ReactivatorsEnoyl-CoA HydrataseTerpenesAldehyde DehydrogenaseL-Lactate DehydrogenaseMethylamines ... Phosphate DehydrogenasesNaphthalenesAnticholesteremic AgentsFluorobenzenesPyruvate SynthaseVitaminsAcyl-CoA Dehydrogenases ...

https://lookformedical.com/en/web/enzymes-and-coenzymes

Butiril-CoA Desidrogenase. Butyryl-CoA Dehydrogenase. Butiril-CoA Deshidrogenasa. CDC2-CDC28 Quinases. CDC2-CDC28 Kinases. ... Acil-CoA Desidrogenases. Acyl-CoA Dehydrogenases. Acil-CoA Deshidrogenasas. Acil-CoA Oxidase. Acyl-CoA Oxidase. Acil-CoA ... Acil-CoA Desidrogenase. Acyl-CoA Dehydrogenase. Acil-CoA Deshidrogenasa. Acil-CoA Desidrogenase de Cadeia Longa. Acyl-CoA ... Metilmalonil-CoA Descarboxilase. Methylmalonyl-CoA Decarboxylase. Metilmalonil-CoA Descarboxilasa. Nucleosídeo-Trifosfatase. ...

https://decs2011.bvsalud.org/P/new_2004.htm

Butiril-CoA Deshidrogenasa. Butyryl-CoA Dehydrogenase. Butiril-CoA Desidrogenase. Carboxilesterasa. Carboxylesterase. ... Acil-CoA Deshidrogenasas. Acyl-CoA Dehydrogenases. Acil-CoA Desidrogenases. Acil-CoA Oxidasa. Acyl-CoA Oxidase. Acil-CoA ... Acil-CoA Deshidrogenasa. Acyl-CoA Dehydrogenase. Acil-CoA Desidrogenase. Acil-CoA Deshidrogenasa de Cadena Larga. Acyl-CoA ... Metilmalonil-CoA Descarboxilasa. Methylmalonyl-CoA Decarboxylase. Metilmalonil-CoA Descarboxilase. Nucleósido-Trifosfatasa. ...

https://decs2018.bvsalud.org/E/new_2004.htm

https://decs2012.bvsalud.org/E/new_2004.htm

https://decs2010.bvsalud.org/E/new_2004.htm

Butyryl-CoA Dehydrogenase. Butiril-CoA Desidrogenase. Butiril-CoA Deshidrogenasa. CDC2-CDC28 Kinases. CDC2-CDC28 Quinases. ... Acyl-CoA Dehydrogenases. Acil-CoA Desidrogenases. Acil-CoA Deshidrogenasas. Acyl-CoA Oxidase. Acil-CoA Oxidase. Acil-CoA ... Acyl-CoA Dehydrogenase. Acil-CoA Desidrogenase. Acil-CoA Deshidrogenasa. Acyl-CoA Dehydrogenase, Long-Chain. Acil-CoA ... Methylmalonyl-CoA Decarboxylase. Metilmalonil-CoA Descarboxilase. Metilmalonil-CoA Descarboxilasa. Myosin-Light-Chain ...

https://decs2019.bvsalud.org/I/new_2004.htm

https://decs2016.bvsalud.org/P/new_2004.htm

https://decs2009.bvsalud.org/P/new_2004.htm

https://decs2015.bvsalud.org/I/new_2004.htm

https://decs2013.bvsalud.org/E/new_2004.htm

https://decs2020.bvsalud.org/I/new_2004.htm

https://decs2014.bvsalud.org/E/new_2004.htm

https://decs2007.bvsalud.org/I/new_2004.htm

https://decs.bvsalud.org/I/new_2004.htm

The reaction rates for non-secreted intermediates NADH2, [CH3OH], acetyl-CoA, butyryl-CoA, and acetoacetyl-CoA were set equal ... Six moles of electrons are produced by CO dehydrogenase per mole acetyl-CoA produced, so a theoretical maximum of 6 protons ... that the electron carrier for the reduction crotonyl-CoA to butyryl-CoA is membrane-bound and may thus participate in ETP. ... cell mass was assumed to be produced from acetyl-CoA, as shown in Equation 1:. Acetyl-CoA + yi NADH2 + y2 ATP -, 2 Cell Mass (1 ...

http://banksolar.ru/?cat=2462

Acetyl CoA. Sum so far: 2 Acetyl CoA + H2O -> Acetoacetate + 2 CoA + H+. 4a) D-3-Hydroxybutyrate Dehydrogenase (runs in the ... 2 Acetyl Coa -> Acetoacetyl Coa + CoA. 2) Citrate Synthase-like reaction:. Acetoacetyl CoA + Acetyl CoA + H2O -> HMG CoA. 3) ... thiol group of a second CoA cleaves off and Acetyl CoA. - reactant is Coa. - products are Acetyl CoA and Acyl-(less 2-C) CoA. ... succinyl CoA + acetoacetate -> Acetoacetyl CoA + succinate. 2) THIOLASE Cleavage:. Acetoacetyl CoA + CoA -> 2 Acetyl CoA. ...

https://www.flashcardmachine.com/chapter-22135.html

Butyryl-CoA + FAD ,, Crotonoyl-CoA + FADH2. FAD + Octanoyl-CoA ,, FADH2 + (2E)-Octenoyl-CoA. FAD + Palmityl-CoA ,, FADH2 + (2E ... Involved in acyl-CoA dehydrogenase activity. Specific function:. Catalyzes the dehydrogenation of acyl-CoA. Gene Name:. fadE. ... FAD + Stearoyl-CoA ,, FADH2 + Trans-Octadec-2-enoyl-CoA. Lauroyl-CoA + FAD ,, (2E)-Dodecenoyl-CoA + FADH2. Decanoyl-CoA (N-C10: ... Hexadecenoyl-CoA. FAD + Tetradecanoyl-CoA ,, FADH2 + (2E)-Tetradecenoyl-CoA. FAD + Hexanoyl-CoA ,, FADH2 + trans-2-Hexenoyl-CoA ...

https://ecmdb.ca/compounds/M2MDB000293

L-CHAD use Long-Chain-3-Hydroxyacyl-CoA Dehydrogenase L-Cysteine use Cysteine ... Lactones, Acyl-Butyryl-Homoserine use Acyl-Butyrolactones Lactones, Acyl-Homoserine use Acyl-Butyrolactones ... Lactate Dehydrogenase Virus use Lactate dehydrogenase-elevating virus Lactate Dehydrogenase Viruses use Lactate dehydrogenase- ... Lactic Dehydrogenase Virus use Lactate dehydrogenase-elevating virus Lactic Dehydrogenase Viruses use Lactate dehydrogenase- ...

https://decs2017.bvsalud.org/I/DeCS2017_Alfab-L.htm

Glutaryl-CoA dehydroge ACYL-CoA DEHYDROGE Synthase Phosphate dehydrogenase Deficiency Inhibition Coenzyme NADH Carnitine Carbon Transport Coenzyme A Dehydrogenase Short-chain-acyl SCAD Dehydratase Pyruvate Reactions Beta Group

The inhibition of glutaryl CoA dehydrogenase results in the accumulation of glutaryl CoA, which could inhibit transmitochondrial malate transport, a rate-limiting step in the early phase of gluconeogenesis, and consequently suppress gluconeogenesis. (medscape.com)

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)
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)
Biochemical, molecular, and clinical characteristics of children with short chain acyl-CoA dehydrogenase deficiency detected by newborn screening in California. (medlineplus.gov)
Short/branched chain acyl-CoA dehydrogenase (SBCAD) deficiency, also known as 2-methylbutyryl-CoA dehydrogenase deficiency, is a recently described autosomal recessive disorder of isoleucine metabolism. (elsevierpure.com)

In addition to the central catalysts, CO dehydrogenase and acetyl-CoA synthase, ATPases are needed in the pathway. (degruyter.com)
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. (degruyter.com)
3-Ketoacyl-CoA synthase (KCS) is a rate-limiting enzyme for VLCFA biosynthesis. (bvsalud.org)

Because NADH and acetyl CoA are required as a cofactor of 3-phosphoglyceraldehyde phosphate dehydrogenase and as an activator of pyruvate carboxylase, respectively, their diminished concentration contributes to the inhibition of gluconeogenesis. (medscape.com)

Jethva R, Bennett MJ, Vockley J. Short-chain acyl-coenzyme A dehydrogenase deficiency. (medlineplus.gov)

As a result of the inhibition of butyryl CoA dehydrogenase, the oxidation of long-chain fatty acids stops at the level of hexanoyl CoA and butyryl CoA. (medscape.com)

MCPA forms nonmetabolizable carnitine and coenzyme A (CoA) esters, thereby depressing tissue levels of these cofactors and making them less available for other biochemical reactions. (medscape.com)
The reductive acetyl-coenzyme A (acetyl-CoA) pathway, also known as the Wood-Ljungdahl pathway, allows reduction and condensation of two molecules of carbon dioxide (CO 2 ) to build the acetyl-group of acetyl-CoA. (degruyter.com)

This effect leads to the decreased production of nicotinamide adenine dinucleotide (NADH) and acetyl CoA. (medscape.com)

Hypoglycemia results because both CoA and carnitine are necessary cofactors for long-chain fatty acid oxidation and because oxidation is a requisite for active gluconeogenesis. (medscape.com)

Productive utilization of CO 2 relies on a set of oxygen sensitive metalloenzymes exploiting the metal organic chemistry of nickel and cobalt to synthesize acetyl-CoA from activated one-carbon compounds. (degruyter.com)
Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. (degruyter.com)

What happens if you lack the proteins to transport Acyl-Coa into the matrix? (flashcardmachine.com)

Jethva R, Bennett MJ, Vockley J. Short-chain acyl-coenzyme A dehydrogenase deficiency. (medlineplus.gov)
The effects of aromatic stacking interactions on the stabilization of reduced flavin adenine dinucleotide (FAD) and substrate/product have been investigated in short-chain acyl-coenzyme A dehydrogenase (SCAD) from Megasphaera elsdenii. (umn.edu)

Biochemical, molecular, and clinical characteristics of children with short chain acyl-CoA dehydrogenase deficiency detected by newborn screening in California. (medlineplus.gov)
A comparison of in vitro acylcarnitine profiling methods for the diagnosis of classical and variant short chain acyl-CoA dehydrogenase deficiency. (nih.gov)

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)
Here we report three unrelated cases, two neurologically affected and one asymptomatic, with this abnormal metabolite pattern due either to mutations in the ETHE1 gene or to a short-chain acyl-CoA dehydrogenase (SCAD) defect. (nih.gov)

Funciton: 4-hydroxybutanoyl-CoA dehydratase (EC 4.2.1. (lbl.gov)

Because NADH and acetyl CoA are required as a cofactor of 3-phosphoglyceraldehyde phosphate dehydrogenase and as an activator of pyruvate carboxylase, respectively, their diminished concentration contributes to the inhibition of gluconeogenesis. (medscape.com)
Each pyruvate is converted to acetyl-CoA, which yields 1 NADH each. (greek.doctor)

The reactions forming 2 acetyl-CoA from glucose have yielded -2 + 2 + 2 = 4 ATP and 4 NADH. (greek.doctor)

When considering the ATP yield of fatty acids it's important to remember that for a fatty acid to enter beta oxidation a -CoA group must be attached to this fatty acid. (greek.doctor)
Each cycle of the beta-oxidation will make the fatty acid 2 carbons shorter, but it will yield 1 NADH, 1 FADH 2 and 1 acetyl-CoA. (greek.doctor)
The fatty acid which is now 2 carbons shorter than the one we started with will enter the beta-oxidation, which will yield 1 NADH, 1 FADH 2 , 1 acetyl-CoA and a fatty acid which is 4 carbons shorter than the one we started with, and so on. (greek.doctor)

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)

Organisms1

Diseases1

Chemicals and Drugs59

Phenomena and Processes4

Information Science2

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

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

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

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)

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

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

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

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)

3-Hydroxyacyl CoA Dehydrogenases

Acyl-CoA Dehydrogenases

Acyl-CoA Dehydrogenase

Cocos

Butyryl-CoA Dehydrogenase

Butyrylcholinesterase

Butyrates

L-Lactate Dehydrogenase

Alcohol Dehydrogenase

Glyceraldehyde-3-Phosphate Dehydrogenases

Aldehyde Dehydrogenase

Glutamate Dehydrogenase

Glucosephosphate Dehydrogenase

Malate Dehydrogenase

Isocitrate Dehydrogenase

Alcohol Oxidoreductases

Dihydrolipoamide Dehydrogenase

Carbohydrate Dehydrogenases

Succinate Dehydrogenase

L-Iditol 2-Dehydrogenase

Glycerolphosphate Dehydrogenase

NAD

Glucose 1-Dehydrogenase

Hydroxysteroid Dehydrogenases

Aldehyde Oxidoreductases

Ketoglutarate Dehydrogenase Complex

Coenzyme A

Glucose Dehydrogenases

3-Hydroxysteroid Dehydrogenases

Phosphogluconate Dehydrogenase

Sugar Alcohol Dehydrogenases

NADH Dehydrogenase

IMP Dehydrogenase

Lactate Dehydrogenases

Formate Dehydrogenases

17-Hydroxysteroid Dehydrogenases

Xanthine Dehydrogenase

Hydroxybutyrate Dehydrogenase

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)

Kinetics

Oxidoreductases

Pyruvate Dehydrogenase (Lipoamide)

Ketone Oxidoreductases

11-beta-Hydroxysteroid Dehydrogenases

NADP

Dihydrouracil Dehydrogenase (NADP)

Uridine Diphosphate Glucose Dehydrogenase

Glucosephosphate Dehydrogenase Deficiency

Molecular Sequence Data

11-beta-Hydroxysteroid Dehydrogenase Type 1

Alanine Dehydrogenase

3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)

Mannitol Dehydrogenases

Acyl Coenzyme A

Amino Acid Sequence

Hydroxyprostaglandin Dehydrogenases

Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)

Retinal Dehydrogenase

Oxidation-Reduction

Acyl-CoA Dehydrogenase, Long-Chain

20-Hydroxysteroid Dehydrogenases

11-beta-Hydroxysteroid Dehydrogenase Type 2

Substrate Specificity

Acetyl Coenzyme A

Isovaleryl-CoA Dehydrogenase

Homoserine Dehydrogenase

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

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

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

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)

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

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

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

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)

Short-chain acyl-coenzyme A dehydrogenase deficiency

Butyryl-CoA

ACADS

Hydrogen

Short-chain acyl-CoA dehydrogenase

3-hydroxy-2-methylbutyryl-CoA dehydrogenase