Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.1 (alcohol dehydrogenase)
9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We observed a contractile action of ethanol (20-500 mM) and other alcohols (methanol and propanol, but not butanol) in guinea pig gastric longitudinal (LM) and circular (CM) smooth muscle preparations. The potency order for the alcohols in the LM preparation was: ethanol = propanol > methanol; and in the CM preparation, propanol > ethanol > methanol. Like epidermal growth factor-urogastrone (EGF), the contractile actions of ethanol in the LM and CM preparations required extracellular calcium and were blocked by the tyrosine kinase inhibitors, genistein and tyrphostin-47 (AG213). The tyrosine phosphatase inhibitor, pervanadate, potentiated the contractile action of ethanol in the LM preparation. Ethanol-induced contractions in both preparations were not affected by 4-methyl pyrazole, an inhibitor of alcohol dehydrogenase, and were unaffected by tetrodotoxin, atropine, prazosine or yohimbine. In the LM preparation, like EGF, the contractile action of ethanol was blocked by the cyclooxygenase inhibitor, indomethacin, and the diacylglycerol lipase inhibitor, U57,908; in the CM preparation, contractions caused by ethanol and EGF were still observed in the presence of these two inhibitors. Contractions caused by ethanol and EGF in the LM preparation were not affected by the epoxygenase inhibitor, ketoconazole; the lipoxygenase inhibitor, nordihydroguaiaretic acid; or the phospholipase A2 inhibitor, mepacrine. In contrast, in the LM preparation, EGF-induced contractions were attentuated by the EGF receptor-kinase inhibitor, PD153035; the MAP-kinase-kinase (MEK) inhibitor, PD98059; the kinase C inhibitor, GF109203X; and the phosphatidylinositol 3'-kinase inhibitors, Wortmannin and LY294002; whereas ethanol-induced contractions were unaffected by these inhibitors. Both ethanol and EGF caused small increases in the phosphotyrosyl protein content of the gastric tissue. We conclude that ethanol causes its contractile effects in the distinct gastric LM and CM preparations independent of nerve-released agonists and via a tyrosine kinase inhibitor-sensitive signal pathway that is in many respects similar to, but distinct from the one activated by EGF.
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PMID:Contractile action of ethanol in guinea pig gastric smooth muscle: inhibition by tyrosine kinase inhibitors and comparison with the contractile action of epidermal growth factor-urogastrone. 922 91

Aldehydes are reduced to alcohols by the enzyme alcohol dehydrogenase (ADH), whereas the enzyme aldehyde dehydrogenase (AldDH) oxidizes aldehydes to carboxylic acids. ADH and AldDH require, respectively, the reduced and oxidized forms of the cofactor NAD (NAD+/NADH). By combining both oxidation and reduction reactions into one process, it is possible to produce alcohols and carboxylic acids simultaneously from aldehydes by continuous recycling of the NAD+/NADH cofactor. However, both enzymes need to be active within the same pH region and buffer system. To test this hypothesis, the pH profile (Vmax and Vmax/Km) as well as the pKa of the prototropic groups involved in catalysis for both dehydrogenases were determined using (Z,Z)-nona-2,4-dienal as a model substrate. The pH profile (Vmax and Vmax/Km) of both enzymes overlapped in the pH range of 6-8 in potassium phosphate buffer. When the coupled enzyme system was used at pH 7 with 10% NAD+ cofactor, over 90% of the starting aldehyde was converted to its corresponding acid and alcohol derivatives in a 1:1 ratio. The sequential action of the enzymes lipoxygenase and hydroperoxide lyase converts polyunsaturated fatty acids to aldehydic fatty acids. The products arising from the oxidation or reduction of the aldehydic functionality are of industrial interest. It was found that 13-oxo-9-(Z),11-(E)-tridecadienoic acid, the product of the sequential reaction of soya bean lipoxygenase and hydroperoxide lyase from Chlorella pyrenoidosa on linoleic acid, is also a substrate in this coupled enzyme system.
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PMID:Cofactor recycling in a coupled enzyme oxidation-reduction reaction: conversion of omega-oxo-fatty acids into omega-hydroxy and dicarboxylic acids. 1033 49

The micro-alga Chlorella pyrenoidosa expresses an enzymatic activity that cleaves the 13-hydroperoxide derivatives of linoleic acid [13-hydroperoxy-9(Z),11(E)-octadecadienoic acid, 13-HPOD] and linolenic acid [13-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid, 13-HPOT] into volatile C(5) and non-volatile C(13) oxo-products. This enzymic activity initially was attributed to a hydroperoxide lyase enzyme; however, subsequent studies showed that this cleavage activity is the result of lipoxygenase activity under anaerobic conditions. Headspace analysis of the volatile products by GC/MS showed the formation of pentane when the substrate was 13-HPOD, whereas a more complex mixture of hydrocarbons was formed when 13-HPOT was the substrate. Analysis of the non-volatile cleavage products from 13-HPOD by liquid chromatography/MS indicated the formation of 13-oxo-9(Z),11(E)-tridecadienoic acid (13-OTA) along with the 13-keto-octadecadienoic acid derivative. When the substrate is 13-HPOT, liquid chromatography/MS analysis indicated the formation of 13-OTA as the major non-volatile product. Aldehyde dehydrogenase (AldDH) oxidizes 13-OTA to an omega-dicarboxylic acid, whereas alcohol dehydrogenase (ADH) reduces 13-OTA to an omega-hydroxy carboxylic acid. AldDH and ADH require the oxidized (NAD(+)) and reduced (NADH) forms of the cofactor NAD, respectively. By combining the action of AldDH and ADH into a continuous cofactor-recycling process, it is possible to simultaneously convert 13-OTA to the corresponding omega-dicarboxylic acid and omega-hydroxy carboxylic acid derivatives.
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PMID:Anaerobic lipoxygenase activity from Chlorella pyrenoidosa. 1117 Dec 68

Many biological C-H activation reactions exhibit nonclassical kinetic isotope effects (KIEs). These nonclassical KIEs are too large (kH/kD > 7) and/or exhibit unusual temperature dependence such that the Arrhenius prefactor KIEs (AH/AD) fall outside of the semiclassical range near unity. The focus of this minireview is to discuss such KIEs within the context of the environmentally coupled hydrogen tunneling model. Full tunneling models of hydrogen transfer assume that protein or solvent fluctuations generate a reactive configuration along the classical, heavy-atom coordinate, from which the hydrogen transfers via nuclear tunneling. Environmentally coupled tunneling also invokes an environmental vibration (gating) that modulates the tunneling barrier, leading to a temperature-dependent KIE. These properties directly link enzyme fluctuations to the reaction coordinate for hydrogen transfer, making a quantum view of hydrogen transfer necessarily a dynamic view of catalysis. The environmentally coupled hydrogen tunneling model leads to a range of magnitudes of KIEs, which reflect the tunneling barrier, and a range of AH/AD values, which reflect the extent to which gating modulates hydrogen transfer. Gating is the primary determinant of the temperature dependence of the KIE within this model, providing insight into the importance of this motion in modulating the reaction coordinate. The potential use of variable temperature KIEs as a direct probe of coupling between environmental dynamics and the reaction coordinate is described. The evolution from application of a tunneling correction to a full tunneling model in enzymatic H transfer reactions is discussed in the context of a thermophilic alcohol dehydrogenase and soybean lipoxygenase-1.
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PMID:Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics. 1208 51

The effect of hot-water treatments of olive fruits before processing on the biosynthesis of virgin olive oil aroma was investigated by quantifying the variation within the major classes of volatile compounds. Data showed that hot-water treatments gave rise to changes in the volatile aroma profile of virgin olive oil from the three olive cultivars under study, Manzanilla, Picual, and Verdial. Different effects by thermal treatments were observed according to cultivar. In general, these changes are mainly due to a decrease in the contents of C(6) aldehydes and C(5) compounds. Contents of C(6) alcohols and esters remained constant or decreased slightly when the temperature of the treatment was increased. Thus, heat treatments seemed to promote a partial deactivation of the lipoxygenase/hydroperoxide lyase enzyme system, whereas other enzymatic activities, within the lipoxygenase pathway, such as alcohol dehydrogenase and alcohol acyltransferase, remained apparently unaffected as a consequence of heat treatments.
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PMID:Modification of volatile compound profile of virgin olive oil due to hot-water treatment of olive fruit. 1455 76

Results obtained in a set of experiments point to an effective participation of olive seeds in the biosynthesis of olive oil aroma through the lipoxygenase pathway during the extraction process to produce virgin olive oil. Data showed that olive seeds should contain enzymatic activities metabolizing 13-hydroperoxides other than hydroperoxide lyase, giving rise to a net decrease in the content of C6 unsaturated aldehydes during the olive oil extraction process. Olive seeds seem also to supply this process with alcohol dehydrogenase activity, being more specific for saturated C6 aldehydes and not acting on C5 alcohols. Moreover, olive seeds would be responsible for the biosynthesis of 30-50% esters during the olive oil extraction process of intact fruits. Thus, olive seeds would afford a load of alcohol acyltransferase activity that might be quite unspecific in terms of substrate, producing any kind of esters.
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PMID:Role of olive seed in the biogenesis of virgin olive oil aroma. 1470 6

Content of aroma compounds and catalytic activity of lipoxygenase (LOX), hydroperoxide lyase (HPL), and alcohol dehydrogenase (ADH) were analyzed in 4- and 15-mm unblanched leek slices packed in atmospheric air (4- and 15-mm) or 100% nitrogen (N) (only 15-mm) seven times during 12 months of frozen storage (12M). Total amount of sulfur compounds was influenced by storage time, slice thickness, and atmosphere (concentration in fresh 4-mm slices = 17.8 mg/L, 4-mm 12M = 3.48 mg/L, fresh 15-mm slices = 2.48 mg/L, 15-mm 12M = 0.418 mg/L and 15-mm N 12M = 1.81 mg/L). The 4-mm slices significantly developed the most aldehydes after 12M (total amount = 9.28 mg/L) compared to 15-mm 12M (6.49 mg/L) and 15-mm N 12M (4.33 mg/L). LOX activity is positively influenced by nitrogen packaging, and HPL activity is influenced by slice thickness, whereas ADH is unaffected by both parameters.
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PMID:Formation of aroma compounds during long-term frozen storage of unblanched leek (Allium ampeloprasum Var. Bulga) as affected by packaging atmosphere and slice thickness. 1499 27

Three continuous assays are described for lipoxygenase (LOX), hydroperoxide lyase (HPL) and alcohol dehydrogenase (ADH) in leek tissue. The catalytic activity of LOX showed significant difference (significance level 5%) between linolenic acid (9.43 x 10(-)(4) katals per kg protein) and linoleic acid (2.53 x 10(-)(4) katals per kg protein), and the pH-optimum of LOX was 4.5-5.5 against linoleic acid. The catalytic activity of HPL was statistically the same for 9-(S)-hydroperoxy-(10E,12Z)-octadecadienoic acid (1.01 x 10(-)(2) katals per kg protein) and 13-(S)-hydroperoxy-(9Z,11E)-octadecadienoic acid (7.69 x 10(-)(3) katals per kg protein). ADH showed a catalytic activity of 5.01 x 10(-)(4) katals/kg of protein toward hexanal. Model experiments with crude enzyme extract from leek mixed with linoleic acid or linolenic acid demonstrated differences in the amount of produced aroma compounds. Linoleic acid resulted in significantly most hexanal, heptanal, (E)-2-heptenal, (E)-2-octenal, (E,E)-2,4-decadienal, pentanol, and hexanol, whereas linolenic acid resulted in significantly most (E)-2-pentenal, (E)-2-hexenal, (E,Z)-2,4-heptadienal, (E,E)-2,4-heptadienal, and butanol. Leek LOX produced only the 13-hydroperoxide of linoleic acid and linolenic acid.
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PMID:Formation of volatile compounds in model experiments with crude leek (Allium ampeloprasum Var. Lancelot) enzyme extract and linoleic acid or linolenic acid. 1508 Jun 39

The content of aroma compounds and the catalytic activity of lipoxygenase (LOX), alliinase, hydroperoxide lyase (HPL), and alcohol dehydrogenase (ADH) were analyzed in unblanched and blanched 15-mm leek slices packed in atmospheric air (21% O2) or 100% nitrogen (0% O2) three times during 12 months of frozen storage (12 M). The total amount of sulfur compounds and the total amount of aldehydes were greatly influenced by storage time, atmosphere, and blanching [concentration of sulfur compounds in fresh unblanched (UNB) slices = 1.35 mg/L, fresh blanched (B) slices = 1.09 mg/L, UNB 21% O2 12 M = 0.656 mg/L, UNB 0% O2 12 M = 2.11 mg/L, B 21% O2 12 M = 1.14 mg/L, B 0% O2 12 M = 1.59 mg/L]. B 0% O2 was closest to the original ratio between sulfur compounds and aldehydes after 12 months. The activities of HPL and alliinase were totally lost after 12 months, and ADH showed minimal activity, whereas LOX (UNB 0% O2) showed approximately 25% of the original activity. LOX was the most and HPL the least heat labile enzyme investigated.
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PMID:Impact of blanching and packaging atmosphere on the formation of aroma compounds during long-term frozen storage of leek (Allium ampeloprasum Var. Bulga) slices. 1526 24

Accumulating experimental evidence suggests that the occurrence of hydrogen tunneling is likely to be widespread in enzyme-catalyzed reactions. The realization that hydrogen can transfer via tunneling mechanisms has far-reaching implications for our understanding of enzyme catalysis involving proton, hydride or hydrogen atom transfer reactions. The current status of the field is highlighted by three enzyme systems that have been under intensive study in recent years, including soybean lipoxygenase-1, thermophilic alcohol dehydrogenase and dihydrofolate reductase. Particular attention has been devoted to the issues of whether protein dynamics modulate hydrogen tunneling probability and whether the tunneling process contributes to the catalytic power of enzymes.
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PMID:Structural bases of hydrogen tunneling in enzymes: progress and puzzles. 1558 87


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