Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.3.99.3 (acyl-CoA dehydrogenase)
 1,425 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The nature of the purple complex formed upon the addition of octanoyl-CoA to the medium chain acyl-CoA dehydrogenase from pig kidney has been addressed by chemical quenching studies. Previous work, using quenching in 0.1 M KOH, suggested that the dehydrogenation product, trans-2-octenoyl-CoA, was not a participant in reduced rat liver enzyme complexes because no octenoic acid was detected after denaturation (Y. Ikeda, D. G. Hine, K. Okamura-Ikeda and K. Tanaka (1985) J. Biol. Chem. 260, 1326-1337). However, when the octanoyl-CoA-reduced pig kidney enzyme is quenched rapidly in 2 M HCl, the ratio of trans-2-octenoyl-CoA/octanoyl-CoA released is 9/1. A milder acid denaturation procedure yields the corresponding ratio of 0.4/1, i.e., now with an excess of the saturated substrate. Similarly, quenching the pig kidney dehydrogenase in 0.1 M KOH reveals only minor levels of octenoyl chains released into the supernatant. When quenching is insufficiently rapid compared to the internal equilibration of oxidized enzyme.octanoyl-CoA and reduced enzyme.octenoyl-CoA forms, the outcome is decided by the greater kinetic lability of the oxidized enzyme species. These data are fully consistent with the original ascription that the purple species observed upon reduction of the acyl-CoA dehydrogenases with substrate represents a charge transfer complex between reduced flavin as the donor and trans-2-octenoyl-CoA as the acceptor.
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PMID:The nature of enzyme-substrate complexes in acyl-coenzyme A dehydrogenases. 335 70

Seven middle-aged men with manifest type II diabetes mellitus underwent an endurance training programme for 10-15 weeks. The maximal aerobic capacity, as well as the endurance capacity, was improved by 10% (p less than 0.05). The intramuscular glycogen store increased by more than 80% (p less than 0.05) from 350 mumol/g dw (dry weight), and the activities of citrate synthase and 3-hydroxy-acyl-CoA dehydrogenase increased by more than 50% (p less than 0.05) and 30% (p less than 0.05). The activity of glycogen synthase was decreased by approximately 20% (p less than 0.05), whereas lactate dehydrogenase remained unchanged. Capillaries/fibre and fibre area increased by more than 50% (p less than 0.05) and 30% (p less than 0.05) leaving the area of supply constant. Training did not influence fasting blood lipids and glucose, glycosylated hemoglobin, oral glucose tolerance, and insulin response to an oral glucose load measured 72 hours post-exercise. It is concluded that patients with manifest type II diabetes, as normoglycaemic individuals, adapt to physical training. However, no persistent effect on glucohomeostasis and lipaemia is produced by short-term training in the diabetic patients.
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PMID:Skeletal muscle adaptations to physical training in type II (non-insulin-dependent) diabetes mellitus. 336 17

The determination of medium chain fatty acids in serum is a useful approach of the diagnosis of medium chain acyl-CoA dehydrogenase deficiency, an increasingly recognized cause of Reye-like syndrome in infants. A reliable and practical method requiring 0.5 ml of serum is presented by which results are obtained within 2.5 h. The preparation of the samples is done by solid phase extraction on reverse phase cartridges, the separation and quantitation by gas chromatography. Reference values for children (n = 24) and adults (n = 40) are given for octanoic, decanoic and dodecanoic acids.
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PMID:Determination of medium chain fatty acids in serum. 337 Aug 37

Hyperammonemia in pediatrics can be due to a number of causes (defects of urea cycle enzymes or transport of its metabolites, organic acidurias, acyl-CoA dehydrogenase or carnitine deficiency, liver bypass or nonspecific insufficiency) requiring differentiated rapid treatment for a satisfactory prognosis. The specific diagnosis cannot be established by clinical means. Thus the work-up rests on biochemical analyses. The methods used are detailed and their interpretation discussed. An algorithm for the interpretation of the data which can easily be computerized is presented. The procedure has proven practicable in 126 patients with urea cycle disorders.
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PMID:Diagnosis of urea cycle disorders. 344 Apr 47

Syntrophomonas wolfei is an anaerobic fatty acid degrader that can only be grown in coculture with H2-using bacteria such as Methanospirillum hungatei. Cells of S. wolfei were selectively lysed by lysozyme treatment, and unlysed cells of M. hungatei were removed by centrifugation. The cell extract of S. wolfei obtained with this method had low levels of contamination by methanogenic cofactors. However, lysozyme treatment was not efficient in releasing S. wolfei protein; only about 15% of the L-3-hydroxyacyl-coenzyme A (CoA) dehydrogenase activity was found in the lysozyme supernatant. Cell extracts of S. wolfei obtained with this method had high specific activities of acyl-CoA dehydrogenase, enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, and 3-ketoacyl-CoA thiolase. These activities were not detected in cell extracts of M. hungatei grown alone, confirming that these activities were present in S. wolfei. The acyl-CoA dehydrogenase activity was high when a C4 but not a C8 or C16 acyl-CoA derivative served as the substrate. S. Wolfei cell extracts had high CoA transferase specific activities and no detectable acyl-CoA synthetase activity, indicating that fatty acid activation occurred by transfer of CoA from acetyl-CoA. Phosphotransacetylase and acetate kinase activities were detected in cell extracts of S. wolfei, indicating that S. wolfei is able to perform substrate-level phosphorylation.
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PMID:Preparation of cell-free extracts and the enzymes involved in fatty acid metabolism in Syntrophomonas wolfei. 345 26

The effect of exercise on the riboflavin status of male rats was studied after 6 or 8 wk of treadmill running. Sedentary and exercised rats were pair fed diets marginal in riboflavin (2.0 or 2.5 mg/kg), and their tissue riboflavin concentrations and erythrocyte glutathione reductase activity coefficients (EGRAC) were compared. The rats exercised for 8 wk had similar body weights but significantly greater weights for heart, gastrocnemius and soleus muscles, less epididymal fat and more total muscle nitrogen and riboflavin than their sedentary controls. Similar changes were evident after 6 wk of exercise, but some were not statistically significant. The EGRAC values of both exercised and sedentary rats responded to changes in dietary riboflavin but were not different from each other. The specific activity of mitochondrial acyl-CoA dehydrogenase (per milligram protein) of the soleus muscle was unaffected by exercise; however, when expressed per gram of tissue or per muscle, the activities in exercised rats were 25% (P less than 0.05) and 60% (P less than 0.01) higher, respectively, than in sedentary rats. On the basis of the riboflavin-dependent parameters measured in this study, exercise did not increase the dietary riboflavin requirement of growing rats but did increase total riboflavin retention in gastrocnemius and soleus muscles.
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PMID:Effect of exercise on riboflavin status of rats. 355 45

We describe two patients with short-chain acyl-coenzyme A (CoA) dehydrogenase (SCADH) deficiency. Neonate I excreted large amounts of ethylmalonate and methylsuccinate; ethylmalonate excretion increased after a medium-chain triglyceride load. Neonate II died postnatally and excreted ethylmalonate, butyrate, 3-hydroxybutyrate, adipate, and lactate. Both neonates' fibroblasts catabolized [1-14C]butyrate poorly (29-64% of control). Neonate I had moderately decreased [1-14C]octanoate catabolism (43-60% of control), while neonate II oxidized this substrate normally; both catabolized radiolabeled palmitate, succinate, and/or leucine normally. Cell sonicates from neonates I and II dehydrogenated [2,3-3H]butyryl-CoA poorly (41 and 53% of control) and [2,3-3H]octanoyl-CoA more effectively (59 and 95% of control). Mitochondrial acyl-CoA dehydrogenase (ADH) activities with butyryl- and octanoyl-CoAs were 37 and 56% of control in neonate I, and 47 and 81% of control in neonate II, respectively. Monospecific medium-chain ADH (MCADH) antisera inhibited MCADH activity towards both butyryl- and octanoyl-CoAs, revealing SCADH activities to be 1 and 11% of control for neonates I and II, respectively. Fibroblast SCADH and MCADH activities were normal in an adult female with muscular SCADH deficiency.
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PMID:Short-chain acyl-coenzyme A dehydrogenase deficiency. Clinical and biochemical studies in two patients. 357 88

Until now, workers in the field of fatty acid metabolism have suggested that the substrates are isopotential with the enzymes and that the reactions are forced to completion by the formation of charge-transfer complexes [Gustafson, W. G., Feinberg, B. A., & McFarland, J. T. (1986) J. Biol. Chem. 261, 7733-7741]. To date, no experimental evidence for this hypothesis exists. The work presented here shows that the butyryl-CoA/crotonyl-CoA couple is not isopotential with the enzymes with which it interacts. The potential of the butyryl-CoA/crotonyl-CoA couple (E ' = -0.013 V) is significantly more positive than the potential of either of the enzymes with which it interacts, bacterial butyryl-CoA dehydrogenase (E ' = -0.079 V) and mammalian general acyl-CoA dehydrogenase (E ' = 0.133 V). These data imply that the regulation of enzyme potential is essential for any electron transfer from substrate to enzyme to occur in mammalian or bacterial systems. In support of this assertion, a significant shift in potential for bacterial butyryl-CoA dehydrogenase (an analogue of the mammalian enzyme) in the presence of butyryl-CoA and crotonyl-CoA is reported. The potential is shifted positive by 60 mV. Larger potential shifts will undoubtedly be observed with the mammalian enzyme, which would be consistent with the catalytic direction of electron transfer.
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PMID:Regulation of the butyryl-CoA dehydrogenase by substrate and product binding. 360 39

cDNA encoding the precursor of rat liver medium chain acyl-CoA dehydrogenase (EC 1.3.99.3) was cloned and sequenced. The longest cDNA insert isolated was 1866 bases in length. This cDNA encodes the entire protein of 421-amino acids including a 25-amino acid leader peptide and a 396-amino acid mature polypeptide. The identity of the medium chain acyl-CoA dehydrogenase clone was confirmed by matching the amino acid sequence predicted from the cDNA to the NH2-terminal and nine internal tryptic peptide sequences derived from pure rat liver medium chain acyl-CoA dehydrogenase. The calculated molecular masses of the precursor medium chain acyl-CoA dehydrogenase, the mature medium chain acyl-CoA dehydrogenase, and the leader peptide are 46,600, 43,700, and 2,900 daltons, respectively. The leader peptide contains five basic amino acids and only one acidic amino acid; thus, it is positively charged, overall. Cysteine residues are unevenly distributed in the mature portion of the protein; five of six are found within the NH2-terminal half of the polypeptide. Comparison of medium chain acyl-CoA dehydrogenase sequence to other flavoproteins and enzymes which act on coenzyme A ester substrates did not lead to unambiguous identification of a possible FAD-binding site nor a coenzyme A-binding domain. The sequencing of other homologous acyl-CoA dehydrogenases will be informative in this regard.
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PMID:Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase. 361 Oct 54

Kinetics of inactivation of general acyl-CoA dehydrogenase from pig kidney by methylenecyclopropaneacetyl-CoA have been analyzed using the theoretical treatment and exact steady-state kinetic solutions reported by Tatsunami (Tatsunami, S., Yago, N., and Hosoe, M. (1981) Biochim. Biophys. Acta 662, 226-235). Thus practical application of these analytical solutions for an important class of enzyme:substrate reactions has been demonstrated for the first time.
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PMID:Kinetics of suicide substrate:enzyme inactivation. Methylenecyclopropaneacetyl-CoA and general acyl-CoA dehydrogenase. 361 32


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