Journal articles: 'Beta-oxidation'

1

Treem, William R. "BETA OXIDATION DEFECTS." Clinics in Liver Disease 3, no. 1 (February 1999): 49–67. http://dx.doi.org/10.1016/s1089-3261(05)70053-2.

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2

Bartlett, Kim, and Simon Eaton. "Mitochondrial beta-oxidation." European Journal of Biochemistry 271, no. 3 (February 2004): 462–69. http://dx.doi.org/10.1046/j.1432-1033.2003.03947.x.

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3

Helser, Terry L. "β[beta]-Oxidation Wordsearch." Journal of Chemical Education 78, no. 4 (April 2001): 483. http://dx.doi.org/10.1021/ed078p483.

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4

Engel, Paul C. "Intramitochondrial beta-oxidation complexes." Biochemical Society Transactions 30, no. 1 (February 1, 2002): A5. http://dx.doi.org/10.1042/bst030a005c.

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5

SCHOLTE, H. R., I. E. M. LUYT-HOUWEN, W. BLOM, H. F. M. BUSCH, P. C. JONGE, M. VISSER, J. G. M. HUIJMANS, et al. "Defects in Mitochondrial Beta Oxidation." Annals of the New York Academy of Sciences 488, no. 1 Membrane Path (December 1986): 511–12. http://dx.doi.org/10.1111/j.1749-6632.1986.tb46585.x.

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6

Schulz, Horst. "Beta oxidation of fatty acids." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1081, no. 2 (January 1991): 109–20. http://dx.doi.org/10.1016/0005-2760(91)90015-a.

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7

Crockett, E. L., and B. D. Sidell. "Substrate selectivities differ for hepatic mitochondrial and peroxisomal β-oxidation in an Antarctic fish, Notothenia gibberifrons." Biochemical Journal 289, no. 2 (January 15, 1993): 427–33. http://dx.doi.org/10.1042/bj2890427.

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Hepatic mitochondrial and peroxisomal beta-oxidation were examined in an Antarctic marine teleost, Notothenia gibberifrons. Enzymic profiles and rates of beta-oxidation by intact organelles were determined by using a range of fatty acyl-CoA substrates to evaluate substrate preferences. Partitioning of beta-oxidation between organelles was estimated. Substrate selectivities are broader for peroxisomal beta-oxidation than for mitochondrial beta-oxidation. Mitochondria show marked preference for the oxidation of a monounsaturated substrate, palmitoleoyl-CoA (C16:1), and two polyunsaturates, eicosapentaenoyl-CoA (C20:5) and docosahexaenoyl-CoA (C22:6). Carnitine palmitoyltransferase activities with palmitoleoyl-CoA (C16:1) are 2.4-fold higher than activities with palmitoyl-CoA (C16:0). Most polyunsaturated acyl-CoA esters measured appear to inhibit by over 40% the oxidation of palmitoyl-CoA by peroxisomes. Our findings suggest that the polyunsaturates, eicosapentaenoic acid (C20:5) and docosahexaenoic acid (C22:6), found in high concentrations in Antarctic fishes [Lund and Sidell (1992) Mar. Biol. 112, 377-382], are utilized as fuels to support aerobic energy metabolism. Metabolic capacities of rate-limiting enzymes and beta-oxidation rates by intact organelles indicate that up to 30% of hepatic beta-oxidation in N. gibberifrons can be initiated by the peroxisomal pathway.

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NANRI, Hayato, Tsuyoshi ATAKA, Nobuyuki TAKEUCHI, Shingo ISHIDA, Koji WATANABE, and Mitsuru WAKAMATSU. "High Temperature Oxidation of .BETA.-SiC." Journal of the Society of Materials Science, Japan 43, no. 493 (1994): 1360–65. http://dx.doi.org/10.2472/jsms.43.1360.

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9

Wang, H. Y., and H. Schulz. "β-oxidation of polyunsaturated fatty acids with conjugated double bonds. Mitochondrial metabolism of octa-2,4,6-trienoic acid." Biochemical Journal 264, no. 1 (November 15, 1989): 47–52. http://dx.doi.org/10.1042/bj2640047.

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The mitochondrial beta-oxidation of octa-2,4,6-trienoic acid was studied with the aim of elucidating the degradation of unsaturated fatty acids with conjugated double bonds. Octa-2,4,6-trienoic acid was found to be a respiratory substrate of coupled rat liver mitochondria, but not of rat heart mitochondria. Octa-2,4,6-trienoyl-CoA, the product of the inner-mitochondrial activation of the acid, was chemically synthesized and its degradation by purified enzymes of beta-oxidation was studied spectrophotometrically and by use of h.p.l.c. This compound is a substrate of NADPH-dependent 2,4-dienoyl-CoA reductase or 4-enoyl-CoA reductase (EC 1.3.1.34), which facilitates its further beta-oxidation. The product obtained after the NADPH-dependent reduction of octa-2,4,6-trienoyl-CoA and one round of beta-oxidation was hex-4-enoyl-CoA, which can be completely degraded via beta-oxidation. It is concluded that polyunsaturated fatty acids with two conjugated double bonds extending from even-numbered carbon atoms can be completely degraded via beta-oxidation because their presumed 2,4,6-trienoyl-CoA intermediates are substrates of 2,4-dienoyl-CoA reductase.

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10

Broadway, N. M., F. M. Dickinson, and C. Ratledge. "Long-chain acyl-CoA ester intermediates of β-oxidation of mono- and di-carboxylic fatty acids by extracts of Corynebacterium sp. strain 7E1C." Biochemical Journal 285, no. 1 (July 1, 1992): 117–22. http://dx.doi.org/10.1042/bj2850117.

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beta-Oxidation of palmitate and tetradecanedioic acid was studied in cell-free extracts of the Gram-positive bacterium Corynebacterium sp. strain 7E1C, and the acyl-CoA ester intermediates formed were analysed by h.p.l.c. beta-Oxidation assays displayed a lag phase before a constant rate of NAD+ reduction was obtained. The length of the lag phase was inversely proportional to the number of units of activity added to assays. This is a characteristic feature of a system of consecutive reactions proceeding via free intermediates. During beta-oxidation of palmitate all the saturated acyl-CoAs from C16 to C8 were detected together with trace amounts of unsaturated and 3-hydroxy-intermediates. The time-course of intermediate formation again indicated a precursor-product relationship indicative of free intermediates being formed. When 3-hydroxyacyl-CoA dehydrogenase was inhibited by completely removing NAD+ from assays, the major acyl-CoAs, detected during palmitate beta-oxidation were palmitoyl-CoA, hexadeca-2-enoyl-CoA and 3-hydroxypalmitoyl-CoA. These compounds also displayed a precursor-product relationship. Under normal assay conditions the acyl-CoA dehydrogenase(s) are the probable rate-limiting enzyme(s) of the beta-oxidation spiral. These results indicate that in cell-free extracts of Corynebacterium sp. strain 7E1C, beta-oxidation proceeds via free acyl-CoA intermediates and is at variance with the concept of substrate channelling or of a ‘leaky hose pipe’ model as proposed for mitochondrial beta-oxidation in eukaryotic cells. The significant accumulation of chain-shortened acyl-CoA esters is similar to the situation observed for mammalian peroxisomal beta-oxidation.

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11

Lamont, L. S., A. J. McCullough, and S. C. Kalhan. "Beta-adrenergic blockade heightens the exercise-induced increase in leucine oxidation." American Journal of Physiology-Endocrinology and Metabolism 268, no. 5 (May 1, 1995): E910—E916. http://dx.doi.org/10.1152/ajpendo.1995.268.5.e910.

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The purpose of this study was to assess the interaction between beta-blockade and exercise on amino acid kinetics. This was a three-way crossover experiment using beta 1-blockade, beta 1,beta 2-blockade, and a placebo control. Three 6-h L-[1-13C]leucine and L-[alpha-15N]lysine infusions were performed. The first 3 h established an isotopic steady state, and 1 h of exercise (approximately 50% of maximal O2 consumption) and 2 h of recovery followed. Plasma glucose decreased with exercise during all trials (P < 0.0001). During beta 1- and beta 1,beta 2-blockade, plasma free fatty acids were reduced during rest and exercise (P < 0.001). Leucine and lysine rates of appearance were unaffected by beta-blockade during rest but were decreased with placebo exercise. Leucine oxidation increased with beta-blockade (P < 0.01) and exercise (P < 0.001). There was a statistical interaction between both treatments (P < 0.004). In conclusion, leucine oxidation increased with exercise, further increased with beta 1-blockade, and was additionally heightened with beta 1,beta 2-blockade. This cumulative response indicates that leucine oxidation was regulated through beta 1- and beta 2-receptors.

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12

Dieuaide, M., I. Couée, A. Pradet, and P. Raymond. "Effects of glucose starvation on the oxidation of fatty acids by maize root tip mitochondria and peroxisomes: evidence for mitochondrial fatty acid β-oxidation and acyl-CoA dehydrogenase activity in a higher plant." Biochemical Journal 296, no. 1 (November 15, 1993): 199–207. http://dx.doi.org/10.1042/bj2960199.

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Fatty acid beta-oxidation was studied in organellar fractions from maize root tips by h.p.l.c. and radiometric analysis of the products of incubations with [1-14C]octanoate and [1-14C]palmitate. In crude organellar fractions containing both mitochondria and peroxisomes, octanoate and palmitate beta-oxidation, as determined by the production of acetyl-CoA, was functional and, for palmitate, was activated 4-12-fold after subjecting the root tips to 48 h of glucose starvation. The sensitivity to a ‘cocktail’ of respiratory-chain inhibitors containing cyanide, azide and salicylhydroxamate depended on the conditions of incubation, with no inhibition in a medium facilitating peroxisomal beta-oxidation and a significant inhibition in a medium potentially facilitating mitochondrial beta-oxidation. Indeed, preparations of highly purified mitochondria from glucose-starved root tips were able to oxidize octanoate and palmitate to give organic acids of the tricarboxylic acid cycle. This activity was inhibited 5-10-fold by the above cocktail of respiratory-chain inhibitors, with no parallel accumulation of acetyl-CoA, thus showing that the inhibition affected beta-oxidation rather than the pathway from acetyl-CoA to the organic acids. This provides the first evidence that the complete beta-oxidation pathway from fatty acids to citrate was functional in mitochondria from a higher plant. Moreover, an acyl-CoA dehydrogenase activity was shown to be present in the purified mitochondria. In contrast with the peroxisomal activity, mitochondrial beta-oxidation showed the same efficiency with octanoate and palmitate and was strictly dependent on glucose starvation.

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13

Kennedy, Todd A., and Daniel C. Liebler. "Peroxyl radical oxidation of .beta.-carotene: formation of .beta.-carotene epoxides." Chemical Research in Toxicology 4, no. 3 (May 1991): 290–95. http://dx.doi.org/10.1021/tx00021a005.

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14

Kimura, Masahiko, and Seiji Yamaguchi. "Screening for fatty acid beta oxidation disorders." Journal of Chromatography B: Biomedical Sciences and Applications 731, no. 1 (August 1999): 105–10. http://dx.doi.org/10.1016/s0378-4347(99)00208-x.

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15

Iafolla, A. Kimberly, Iley B. Browning, and Charles R. Roe. "Familial infantile apnea and immature beta oxidation." Pediatric Pulmonology 20, no. 3 (September 1995): 167–71. http://dx.doi.org/10.1002/ppul.1950200307.

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16

Kionka, C., and W. H. Kunau. "Inducible beta-oxidation pathway in Neurospora crassa." Journal of Bacteriology 161, no. 1 (1985): 153–57. http://dx.doi.org/10.1128/jb.161.1.153-157.1985.

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17

Park, Sang Jun, Inkwon Bae, In-Sik Nam, Byong K. Cho, Seong Moon Jung, and Ju-Hyung Lee. "Oxidation of formaldehyde over Pd/Beta catalyst." Chemical Engineering Journal 195-196 (July 2012): 392–402. http://dx.doi.org/10.1016/j.cej.2012.04.028.

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18

Lennard, M. S. "The polymorphic oxidation of beta-adrenoceptor antagonists." Pharmacology & Therapeutics 41, no. 3 (January 1989): 461–77. http://dx.doi.org/10.1016/0163-7258(89)90126-5.

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19

Armor, John N. "New titanium beta zeolite for selective oxidation." Applied Catalysis A: General 118, no. 2 (October 1994): N14. http://dx.doi.org/10.1016/0926-860x(94)80319-6.

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20

Crockett, E. L., and B. D. Sidell. "Peroxisomal beta-oxidation is a significant pathway for catabolism of fatty acids in a marine teleost." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 264, no. 5 (May 1, 1993): R1004—R1009. http://dx.doi.org/10.1152/ajpregu.1993.264.5.r1004.

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Hepatic beta-oxidation is characterized in a marine teleost, Myoxocephalus octodecimspinosus, to determine mitochondrial and peroxisomal substrate selectivity as well as metabolic partitioning. Substrate selectivity is broad for peroxisomal beta-oxidation. Acyl CoA oxidase activities, with all unsaturated substrates measured, are at least 35% of activity with palmitoyl CoA (16:0), a saturated substrate. Mitochondrial selectivities are more pronounced. Carnitine palmitoyltransferase activity with a monounsaturate, palmitoleoyl CoA (16:1), is nearly 40% greater than activity with palmitoyl CoA, whereas activities with two polyunsaturates are < 10% of activity with the saturate. The presence of polyunsaturated acyl CoA esters inhibits up to 70% the oxidation of palmitoyl CoA by intact peroxisomes. Acyl CoA hydrolase activity is localized to peroxisomal fractions prepared by density-gradient centrifugation. Hydrolytic activity in these fractions is nearly twofold the activity of beta-oxidation. Estimates for metabolic partitioning suggest that at least 50% of hepatic beta-oxidation may be initiated by the peroxisomal compartment.

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21

Nishimaki-Mogami, T., A. Takahashi, K. Toyoda, and Y. Hayashi. "Induction of peroxisomal β-oxidation by a microbial catabolite of cholic acid in rat liver and cultured rat hepatocytes." Biochemical Journal 295, no. 1 (October 1, 1993): 217–20. http://dx.doi.org/10.1042/bj2950217.

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The capability of (4R)-4-(2,3,4,6,6a beta,7,8,9,9a alpha,9b beta-decahydro-6a beta-methyl-3-oxo-1H-cyclopental[f]quinolin-7 beta-yl)valeric acid (DCQVA), a catabolite of cholic acid produced by enterobacteria, to induce peroxisome proliferation in vivo and in vitro was studied. Rats given 0.3% DCQVA in the diet for 2 weeks showed marked increases in peroxisomal beta-oxidation, mitochondrial 2,4-dienoyl-CoA reductase and microsomal laurate omega-oxidation activities in the liver compared with control rats given the diet without DCQVA. Cultured rat hepatocytes treated with DCQVA for 72 h also exhibited greatly enhanced beta-oxidation activity. The increased activity was concentration-dependent and the effective concentrations were comparable with those of clofibric acid that produced the same degree of induction in the assay. The results demonstrate that DCQVA is a potent peroxisome proliferator that occurs naturally in rat intestine.

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22

Advani, R., S. Sorenson, E. Shinar, W. Lande, E. Rachmilewitz, and SL Schrier. "Characterization and comparison of the red blood cell membrane damage in severe human alpha- and beta-thalassemia." Blood 79, no. 4 (February 15, 1992): 1058–63. http://dx.doi.org/10.1182/blood.v79.4.1058.1058.

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Abstract The aim of the present work was to understand the pathophysiology of the severe human thalassemias as represented by beta-thalassemia intermedia and hemoglobin (Hb) H (alpha-thalassemia) disease. We have previously shown that the material properties of the red blood cell (RBC) and its membrane differ in severe alpha- and beta-thalassemia, and we now show that this difference is probably caused by accumulation of alpha-globin chains at the cytoskeleton in beta-thalassemia, whereas beta-globin chains are associated with the cytoskeleton in alpha- thalassemia. In both alpha- and beta-thalassemia, some of these globin chains have become oxidized as evidenced by loss of the free thiols. Furthermore, there is similar evidence of oxidation of protein 4.1 in beta-thalassemia, whereas beta-spectrin appears to be subject to oxidation in alpha-thalassemia. These observations support the idea that the association of partly oxidized globin chains with the cytoskeleton results in oxidation of adjacent skeletal proteins. The abnormality of protein 4.1 in beta-thalassemia is consistent with a prior observation, and is also in accord with the known importance of protein 4.1 in maintenance of membrane stability, a property that is abnormal in beta-thalassemic membranes.

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23

Advani, R., S. Sorenson, E. Shinar, W. Lande, E. Rachmilewitz, and SL Schrier. "Characterization and comparison of the red blood cell membrane damage in severe human alpha- and beta-thalassemia." Blood 79, no. 4 (February 15, 1992): 1058–63. http://dx.doi.org/10.1182/blood.v79.4.1058.bloodjournal7941058.

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The aim of the present work was to understand the pathophysiology of the severe human thalassemias as represented by beta-thalassemia intermedia and hemoglobin (Hb) H (alpha-thalassemia) disease. We have previously shown that the material properties of the red blood cell (RBC) and its membrane differ in severe alpha- and beta-thalassemia, and we now show that this difference is probably caused by accumulation of alpha-globin chains at the cytoskeleton in beta-thalassemia, whereas beta-globin chains are associated with the cytoskeleton in alpha- thalassemia. In both alpha- and beta-thalassemia, some of these globin chains have become oxidized as evidenced by loss of the free thiols. Furthermore, there is similar evidence of oxidation of protein 4.1 in beta-thalassemia, whereas beta-spectrin appears to be subject to oxidation in alpha-thalassemia. These observations support the idea that the association of partly oxidized globin chains with the cytoskeleton results in oxidation of adjacent skeletal proteins. The abnormality of protein 4.1 in beta-thalassemia is consistent with a prior observation, and is also in accord with the known importance of protein 4.1 in maintenance of membrane stability, a property that is abnormal in beta-thalassemic membranes.

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24

Jin, S. J., and K. Y. Tserng. "Biogenesis of dicarboxylic acids in rat liver homogenate studied by 13C labeling." American Journal of Physiology-Endocrinology and Metabolism 261, no. 6 (December 1, 1991): E719—E724. http://dx.doi.org/10.1152/ajpendo.1991.261.6.e719.

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The aim of this investigation is to assess whether long-chain fatty acids can be a substrate for omega-oxidation and the subsequent beta-oxidation to produce medium-chain dicarboxylic acids normally found in urine. Isolated rat liver 10,000 g supernatant and pellet fractions were used as the source of enzymes. The metabolism of palmitate was studied using [1,2,3,4-13C4]hexadecanoic acid as tracer. Selected ion monitoring mass spectrometry was utilized for the determination of isotope enrichments in precursor and products. Palmitate was found to be a good substrate for omega-oxidation; the rate was only slightly slower than decanoate. The beta-oxidation of [1,2,3,4-13C4]hexadecanedioic acid yielded labeled adipic, suberic, and sebacic acids. Isotope distribution in these dicarboxylic acids consisted mostly of unlabeled molecules (M + 0) and molecules labeled with four 13C (M + 4), in agreement with a beta-oxidation initiated equally from both carboxyl ends of the precursor. Significant enrichments (1-8%) with only two 13C labels (M + 2) indicate a partial bidirectional beta-oxidation. The direct metabolic conversion of hexadecanedioate to succinate was documented by the significant enrichment (1.40-1.90%) in M + 4 of succinate. These data indicate that long-chain fatty acids can be a substrate for the production of medium-chain dicarboxylates and the eventual direct conversion to succinate.

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25

Liao, Yanmei, Shuxiang Pan, Chaoqun Bian, Xiangju Meng, and Feng-Shou Xiao. "Improved catalytic activity in methanol electro-oxidation over the nickel form of aluminum-rich beta-SDS zeolite modified electrode." Journal of Materials Chemistry A 3, no. 11 (2015): 5811–14. http://dx.doi.org/10.1039/c4ta06699e.

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26

Van Koevering, M., and S. Nissen. "Oxidation of leucine and alpha-ketoisocaproate to beta-hydroxy-beta-methylbutyrate in vivo." American Journal of Physiology-Endocrinology and Metabolism 262, no. 1 (January 1, 1992): E27—E31. http://dx.doi.org/10.1152/ajpendo.1992.262.1.e27.

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The oxidation of alpha-ketoisocaproate (KIC) to beta-hydroxy-beta-methylbutyrate (HMB) by the enzyme KIC dioxygenase has been previously described in rat and human liver; however, the importance of this pathway in normal leucine metabolism has not yet been assessed. A series of experiments was conducted in young lambs and pigs to determine whether HMB is produced from KIC in vivo and to estimate the importance of this pathway in leucine metabolism. In the first study, lambs were fed a bolus of KIC, and the change in plasma HMB concentration was monitored over a 24-h period. Administration of KIC increased plasma HMB from basal concentrations of 2 to approximately 7 microM 4 h after the supplementation. In the second experiment, lambs were infused with [6,6,6-2H3]KIC into the duodenum, and the appearance of labeled [2H3]HMB was measured. Under basal conditions, a minimum of 18% of the HMB was derived from KIC, but when unlabeled KIC was infused into the duodenum at a rate of 1.6 mumol.kg-1.min-1, plasma HMB concentration doubled, and essentially 100% of the HMB present was derived from KIC. In a third experiment, young pigs were infused with [6,6,6-2H3]leucine. At steady state, [2H3]-leucine and HMB enrichments were nearly identical, indicating that plasma HMB is derived solely from leucine. In a fourth experiment, both lambs and pigs were injected intravenously with 600 mg of HMB daily, and urinary HMB excretion was quantitated.(ABSTRACT TRUNCATED AT 250 WORDS)

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27

Chu, C., L. F. Mao, and H. Schulz. "Estimation of peroxisomal β-oxidation in rat heart by a direct assay of acyl-CoA oxidase." Biochemical Journal 302, no. 1 (August 15, 1994): 23–29. http://dx.doi.org/10.1042/bj3020023.

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The contribution of peroxisomes to palmitate beta-oxidation in rat heart was estimated by either inhibiting mitochondrial beta-oxidation or measuring the activity of acyl-CoA oxidase. When respiratory inhibitors such as KCN or antimycin plus rotenone, or inhibitors of mitochondrial fatty acid uptake such as 2-tetradecylglycidic acid or 2-bromopalmitate, were used, degrees of inhibitions ranging from 24% to 87% were observed for palmitate beta-oxidation by a rat heart homogenate. Although the oxidation of palmitoyl-L-carnitine by coupled rat heart mitochondria was almost completely (94%) inhibited by KCN, the inhibition by antimycin plus rotenone was incomplete (77%) and was stimulated by L-carnitine. A direct assay of acyl-CoA oxidase, based on the spectrophotometric measurement at 300 nm of 2,4-decadienoyl-CoA formation from 4-trans-decenoyl-CoA, was evaluated with the aim of obtaining reliable values for the activity of this enzyme, which is presumed to catalyse the rate-limiting step of peroxisomal beta-oxidation. Activities determined by use of this assay were much higher than activities obtained by a coupled assay [Small, Burdett and Connock (1985) Biochem. J. 227, 205-210] commonly used to measure the activity of acyl-CoA oxidase. However, both methods yielded the same relative activities with different tissue homogenates. Based on an estimated palmitoyl-CoA oxidase activity of 0.3 nmol/min per mg of protein, the contribution of peroxisomes to palmitate beta-oxidation in a rat heart homogenate would optimally be 4%, and most likely is several-fold lower.

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Xu, Jun Qiang, Fang Guo, Jun Li, and Xue Jun Quan. "Preparation of the Modified Mesoporous Beta Materials and its Application in Wet Catalytic Degradation of Methyl Orange." Advanced Materials Research 393-395 (November 2011): 1381–84. http://dx.doi.org/10.4028/www.scientific.net/amr.393-395.1381.

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The heterogeneous beta-supported transition metal catalysts were prepared by incipient wetness impregnation. The catalytic oxidation degradation of methyl orange was carried over the heterogeneous catalyst in the peroxide catalytic oxidation process. The pure beta materials showed quick adsorption equilibrium characterization, and the adsorption ratio was only 30%. Compared with the adsorption of the pure beta carrier, the Cu/beta and Fe/beta catalyst could effectively degrade methyl orange with high catalytic activity and easy catalyst separation from the solution using hydrogen peroxide as oxide. The methyl orange removal efficiency could reach 99% in the optimum experimental conditions. The optimal mental content for Cu, Ag, Mn, Fe and Co was 5%, 8%, 0.3%, 1% and 0.3%, respectively.

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Cherkaoui-Malki, Mustapha, Sailesh Surapureddi, Hammam I. El Hajj, Joseph Vamecq, and Pierre Andreoletti. "Hepatic Steatosis and Peroxisomal Fatty Acid Beta-oxidation." Current Drug Metabolism 13, no. 10 (October 1, 2012): 1412–21. http://dx.doi.org/10.2174/138920012803762765.

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30

Miele, L., A. Grieco, A. Armuzzi, M. Candelli, M. A. Zocco, A. Forgione, B. Alfei, G. L. Rapaccini, G. Gasbarrini, and A. Gasbarrini. "Nonalcoholic-steatohepatitis (NASH) and hepatic mitochondrial beta-oxidation." Journal of Hepatology 38 (April 2003): 197. http://dx.doi.org/10.1016/s0168-8278(03)80059-4.

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31

Bonnefont, Jean-Paul, Jean Bastin, Anthony Behin, and Fatima Djouadi. "Bezafibrate for an Inborn Mitochondrial Beta-Oxidation Defect." New England Journal of Medicine 360, no. 8 (February 19, 2009): 838–40. http://dx.doi.org/10.1056/nejmc0806334.

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32

Vishwanath, Vijay A. "Fatty Acid Beta-Oxidation Disorders: A Brief Review." Annals of Neurosciences 23, no. 1 (2016): 51–55. http://dx.doi.org/10.1159/000443556.

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33

IDE, Takashi. "Mitochondrial and Peroxisomal .BETA.-Oxidation: Enzymes and Regulation." Kagaku To Seibutsu 37, no. 7 (1999): 443–50. http://dx.doi.org/10.1271/kagakutoseibutsu1962.37.443.

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34

Foxworthy, P. S., and P. I. Eacho. "Inhibition of hepatic fatty acid oxidation at carnitine palmitoyltransferase I by the peroxisome proliferator 2-hydroxy-3-propyl-4-[6-(tetrazol-5-yl) hexyloxy]acetophenone." Biochemical Journal 252, no. 2 (June 1, 1988): 409–14. http://dx.doi.org/10.1042/bj2520409.

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Recent studies suggest that the induction of peroxisomal beta-oxidation in rodents may represent an adaptive response to disturbances in hepatic lipid metabolism. The following studies were done to determine the effects of 2-hydroxy-3-propyl-4-[6-(tetrazol-5-yl)hexyloxy]acetophenone (4-THA), a tetrazole-substituted acetophenone which induces peroxisomal beta-oxidation in rodent liver, on fatty acid oxidation in vitro. In isolated hepatocytes, 4-THA inhibited the oxidation of oleate (C18:1) and decreased the mitochondrial redox state. The inhibition was more pronounced in the presence of 0.2 mM-oleate than with 0.5 mM, indicating the inhibition may be competitive. 4-THA had no effect on the oxidation of octanoate (C8:0), suggesting that the site of inhibition of oleate oxidation was the carnitine-dependent transport across the mitochondrial inner membrane. In rat liver mitochondria, 4-THA inhibited carnitine palmitoyltransferase I (CPT-I) competitively with respect to the substrate palmitoyl-CoA, increasing the apparent Km from 19 microM to 86 microM. The inhibition of CPT-I by 4-THA was independent of the concentration of the co-substrate carnitine. Whereas fasting attenuated the inhibition of CPT-I by malonyl-CoA, it did not diminish the inhibition by 4-THA. Inhibition of transferase activity by 4-THA and malonyl-CoA was attenuated in mitochondria which had been solubilized with octyl glucoside to expose the latent form of carnitine palmitoyltransferase (CPT-II), suggesting that the inhibition was specific for CPT-I. The specificity was further demonstrated in studies of mitochondrial beta-oxidation in which 4-THA inhibited the oxidation of palmitoyl-CoA but not palmitoylcarnitine. The results demonstrate that 4-THA inhibits fatty acid oxidation in rat liver in vitro at the site of transport across the mitochondrial inner membrane, CPT-I. Whether this disruption in mitochondrial oxidation is causally related to the induction of peroxisomal beta-oxidation is yet to be determined.

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35

Skorokhodova, A. Yu, and V. G. Debabov. "Study of the Potential of Reversal of the Fatty Acid Beta-Oxidation Pathway for Stereoselective Biosynthesis of (S)-1,3-Butanediol from Glucose by Recombinant Escherichia coli Strains." Biotekhnologiya 35, no. 5 (2019): 12–19. http://dx.doi.org/10.21519/0234-2758-2019-35-5-12-19.

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A possible contribution of collateral enzymes to the formation of key precursor metabolite, 3-hydroxybutyryl-CoA, in a recombinant Escherichia coli strain engineered for 1,3-butanediol biosynthesis from glucose through the inverted fatty acid beta-oxidation pathway has been evaluated. The inactivation of the 3-hydroxyadipyl-CoA dehydrogenase gene, paaH, did not prevent the 1,3-butanol biosynthesis during anaerobic glucose utilization by the strain with the intact essential gene fabG coding for 3-ketoacyl-ACP reductase, which can catalyze the conversion of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA. The subsequent inactivation in the strain of fadB gene coding for (S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase of the fatty acid beta-oxidation led to the abolishment of the 1,3-butanediol synthesis. The respective diol was also not found among the products secreted by the strain possessing the intact fabG and paaH genes upon an individual deletion of fadB gene. It was established that the collateral enzymes did not participate in the formation of 3-hydroxybutyryl-CoA in the studied strains and the respective CoA-derivative was synthesized solely by the (S)-specific enzyme of the fatty acid beta-oxidation pathway. The obtained results indicate that the reversal of the fatty acid beta-oxidation pathway can ensure the enantioselective biosynthesis of the (S)-stereoisomer of 1,3-butanediol in engineered E. coli strains. 1,3-butanediol, fatty acid beta-oxidation, Escherichia coli, glucose, metabolic engineering, stereoisomer. The work was carried out with financial support Russian Foundation for Fundamental Research (No. 18-29-08059).

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Poulos, A., P. Sharp, H. Singh, D. W. Johnson, W. F. Carey, and C. Easton. "Formic acid is a product of the α-oxidation of fatty acids by human skin fibroblasts: deficiency of formic acid production in peroxisome-deficient fibroblasts." Biochemical Journal 292, no. 2 (June 1, 1993): 457–61. http://dx.doi.org/10.1042/bj2920457.

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Human skin fibroblasts in culture can oxidize beta-methyl fatty acids, such as phytanic acid and 3-methylhexadecanoic acid, to CO2 and water-soluble products. The latter are released largely into the culture medium. The major water-soluble product formed from [1-14C]phytanic and [1-14C]3-methylhexadecanoic acids is [14C]formic acid. As phytanic acid and 3-methylhexadecanoic acids contain beta-methyl groups and theoretically cannot be degraded by beta-oxidation, we postulate that formic acid is formed from fatty acids by alpha-oxidation. The marked reduction in formic acid production from beta-methyl fatty acids in peroxisome-deficient skin fibroblasts suggests that peroxisomes are involved in the generation of C1 units.

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Otomo, Ryoichi, Ryota Kosugi, Yuichi Kamiya, Takashi Tatsumi, and Toshiyuki Yokoi. "Modification of Sn-Beta zeolite: characterization of acidic/basic properties and catalytic performance in Baeyer–Villiger oxidation." Catalysis Science & Technology 6, no. 8 (2016): 2787–95. http://dx.doi.org/10.1039/c6cy00532b.

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38

Pan, Hua, Dongmei Xu, Chi He, and Chao Shen. "In Situ Regeneration and Deactivation of Co-Zn/H-Beta Catalysts in Catalytic Reduction of NOx with Propane." Catalysts 9, no. 1 (December 30, 2018): 23. http://dx.doi.org/10.3390/catal9010023.

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Regeneration and deactivation behaviors of Co-Zn/H-Beta catalysts were investigated in NOx reduction with C3H8. Co-Zn/H-Beta exhibited a good water resistance in the presence of 10 vol.% H2O. However, there was a significant drop off in N2 yield in the presence of SO2. The formation of surface sulfate and coke decreased the surface area, blocked the pore structure, and reduced the availability of active sites of Co-Zn/H-Beta during the reaction of NO reduction by C3H8. The activity of catalyst regenerated by air oxidation followed by H2 reduction was higher than that of catalyst regenerated by H2 reduction followed by air oxidation. Among the catalysts regenerated by air oxidation followed by H2 reduction with different regeneration temperatures, the optimal regeneration temperature was 550 °C. The textural properties of poisoned catalysts could be restored to the levels of fresh catalysts by the optimized regeneration process. The regeneration process of air oxidation followed by H2 reduction could recover the active sites of cobalt and zinc species from sulfate species, as well as eliminate coke deposition on poisoned catalysts. The regeneration pathway of air oxidation followed by H2 reduction is summarized as initial removal of coke by air oxidation and final reduction of the sulfate species by H2.

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39

Carpenter, K. L., G. M. Wilkins, B. Fussell, J. A. Ballantine, S. E. Taylor, M. J. Mitchinson, and D. S. Leake. "Production of oxidized lipids during modification of low-density lipoprotein by macrophages or copper." Biochemical Journal 304, no. 2 (December 1, 1994): 625–33. http://dx.doi.org/10.1042/bj3040625.

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The oxidation of low-density lipoprotein (LDL) is implicated in atherosclerosis. Lipids and oxidized lipids were analysed by gas chromatography and gas chromatography-mass spectrometry in human LDL incubated with mouse peritoneal macrophages (MPM) or copper (II) sulphate in Ham's F-10 medium or medium alone (control). MPM-modification and copper-catalysed oxidation of LDL resulted in the formation of oxysterols, mainly cholest-5-en-3 beta,7 beta-diol (7 beta-OH-CHOL); 7%-19% of the initial cholesterol was converted to 7 beta-OH-CHOL in 24 h. 7 beta-OH-CHOL levels in control LDL were very low. The increase in 7 beta-OH-CHOL in MPM and copper-oxidized LDL was accompanied by decreases in linoleate and arachidonate and increases in the electrophoretic mobility and degradation of LDL protein by ‘target’ macrophages. The concerted occurrence of these processes and their similarity in both MPM-modification and copper-catalysed oxidation of LDL were suggested by the highly significant cross-correlations. The fall in polyunsaturated fatty acid (PUFA) was accompanied by a directly proportional increase in electrophoretic mobility of the LDL. Production of 7 beta-OH-CHOL and protein degradation by macrophages showed modest elevations during the initial steep fall in PUFA, and showed their greatest increases as the levels of PUFA slowly approached zero. The levels of 7 beta-OH-CHOL and the degradation of LDL by macrophages were directly proportional. The degradation of LDL by macrophages increased rapidly as the electrophoretic mobility of LDL was slowly approaching its maximum level.

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40

McCall, A. L., I. Sussman, K. Tornheim, R. Cordero, and N. B. Ruderman. "Effects of hypoglycemia and diabetes on fuel metabolism by rat brain microvessels." American Journal of Physiology-Endocrinology and Metabolism 254, no. 3 (March 1, 1988): E272—E278. http://dx.doi.org/10.1152/ajpendo.1988.254.3.e272.

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Glucose and beta-hydroxybutyrate metabolism were compared in isolated cerebral microvessels from chronically diabetic and hypoglycemic rats. As noted previously, glucose oxidation and conversion to lactate are diminished in rats with streptozotocin-induced diabetes. The decrease in glucose metabolism did not result from selective damage to diabetic vessels during isolation, since the ATP level and the ATP/ADP ratio were similar to those of nondiabetic rats, and O2 consumption was increased. In addition, cerebral microvessel oxidation of beta-hydroxybutyrate was enhanced by diabetes. By contrast, microvessels from rats made chronically hypoglycemic by insulinoma engrafting 30 days earlier had a more than twofold increase in glucose oxidation and conversion to lactate, whereas their oxidation of beta-hydroxybutyrate was diminished by 50%. Unlike the insulinoma rats, no consistent increase in glucose metabolism was observed in microvessels from rats made hypoglycemic either by acute insulin administration or by a 4-day infusion of insulin. These results indicate that diabetes, and under some circumstances chronic hypoglycemia, markedly alters fuel metabolism in the cerebral microvasculature.

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Kolodiaznaia, V. S., M. Alnakoud, E. I. Kiprushkina, O. N. Rumiantceva, and D. Y. Mironova. "Kinetics of hydrolysis reactions and triacylglycerols oxidation in olive oil during prolonged storage." IOP Conference Series: Earth and Environmental Science 866, no. 1 (October 1, 2021): 012007. http://dx.doi.org/10.1088/1755-1315/866/1/012007.

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Abstract The article presents the results of studies on the effect of the antioxidant beta-carotene and storage temperature on hydrolytic and oxidative processes occurring during storage of extra virgin olive oil obtained from olives grown in the soil and climatic conditions in Syria. The research aims to study the effect of temperature and beta-carotene on the kinetics of the hydrolysis reactions of triglycerides and fatty acids oxidation in olive oil during storage. The object of the study was extra virgin olive oil obtained from olives grown in Syria according to the generally accepted technology in 2019. And beta-carotene, produced by Ekoresurs, has been used as a natural antioxidant. The kinetics of the hydrolysis and oxidation reaction was evaluated by studying the change in the content of saturated and unsaturated fatty acids during storage of the control sample from olive oil (sample No. 1), and experimental samples with the addition of beta-carotene at concentrations of 400 mg/L (sample No. 2) and 600 mg/L (sample No. 3). These samples were stored at 18 ° C. And sample No. 4 was stored without adding beta-carotene at 4 ° C. Upon receipt for storage and during this process, the content of saturated and unsaturated fatty acids in the test samples was determined periodically by gas chromatography on an LC-20 Shimadzu chromatograph, and organoleptic quality indicators were evaluated on a five-point scale. In addition, the content of triacylglycerols, saturated and unsaturated fatty acids were determined based on the change in beta-carotene dose, temperature, and period of storage. Also, the rate constants of the fatty acid oxidation reaction have been calculated. It was shown that the minimum rate of free fatty acids oxidation during storage of extra virgin olive oil for 7 months was in the olive oil sample stored at + 18 ° C with the addition of 400 mg/L of beta-carotene, as well as in the olive oil sample stored in the refrigerator at + 4 ° C without adding antioxidant.

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Endrizzi, Anne, Yves Pagot, Annick Le Clainche, Jean-Marc Nicaud, and Jean-Marc Belin. "Production of Lactones and Peroxisomal Beta-Oxidation in Yeasts." Critical Reviews in Biotechnology 16, no. 4 (January 1996): 301–29. http://dx.doi.org/10.3109/07388559609147424.

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SHIMADA, Shiro, Takenori AOKI, Kenneth J. D. MACKENZIE, Takeshi OKUTANI, and Katuyoshi SHIMOKAWA. "Oxidation and Mechanical Behavior of Carbothermal .BETA.-SiAlON Ceramics." Journal of the Ceramic Society of Japan 107, no. 1249 (1999): 786–90. http://dx.doi.org/10.2109/jcersj.107.786.

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Wang, Yu-Jie, Noora Mäkelä, Ndegwa Henry Maina, Anna-Maija Lampi, and Tuula Sontag-Strohm. "Lipid oxidation induced oxidative degradation of cereal beta-glucan." Food Chemistry 197 (April 2016): 1324–30. http://dx.doi.org/10.1016/j.foodchem.2015.11.018.

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45

Diczfalusy, U., and SE Alexson. "Identification of metabolites from peroxisomal beta-oxidation of prostaglandins." Journal of Lipid Research 31, no. 2 (February 1990): 307–14. http://dx.doi.org/10.1016/s0022-2275(20)43216-x.

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TAMURA, YASUMITSU, TAKAYUKI YAKURA, HIROAKI TERASHI, JUN-ICHI HARUTA, and YASUYUKI KITA. "Hypervalent iodine oxidation of .ALPHA.,.BETA.-unsaturated carbonyl compounds." CHEMICAL & PHARMACEUTICAL BULLETIN 35, no. 2 (1987): 570–77. http://dx.doi.org/10.1248/cpb.35.570.

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47

EATON, Simon, Douglass M. TURNBULL, and Kim BARTLETT. "Redox control of beta-oxidation in rat liver mitochondria." European Journal of Biochemistry 220, no. 3 (March 1994): 671–81. http://dx.doi.org/10.1111/j.1432-1033.1994.tb18668.x.

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48

Yamauchi, Ryo, Nobuyuki Miyake, Hirohito Inoue, and Koji Kato. "Products formed by peroxyl radical oxidation of .beta.-carotene." Journal of Agricultural and Food Chemistry 41, no. 5 (May 1993): 708–13. http://dx.doi.org/10.1021/jf00029a005.

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49

Clayton, P. T. "Clinical consequences of defects in peroxisomal beta-oxidation enzymes." Biochemical Society Transactions 29, no. 1 (February 1, 2001): A4. http://dx.doi.org/10.1042/bst029a004b.

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50

Ghisla, Sandro. "beta-Oxidation of fatty acids. A century of discovery." European Journal of Biochemistry 271, no. 3 (February 2004): 459–61. http://dx.doi.org/10.1046/j.1432-1033.2003.03952.x.

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Journal articles on the topic 'Beta-oxidation'

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