Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The disappearance of pyridine nucleotides during incubation with mosquito homogenates proceeds through the hydrolysis of the pyrophosphate linkage of these compounds as demonstrated by the formation of NMN and AMP from NAD(+). This reaction was also demonstrated by the loss in the coenzyme functioning property of NAD(+) (yeast alcohol dehydrogenase reaction) without a concomitant loss in reactivity towards cyanide. Transglycosidase activity was not observed in the mosquito homogenates, and low concentrations of nicotinamide did not inhibit the NAD(+) splitting activity of these homogenates. These observations are all in accord with the presence in these homogenates of a NAD(+) pyrophosphatase rather than a NADase. 2. The NAD(+) pyrophosphatase is destroyed by boiling, is not heat-activated, and has a pH optimum at pH8.75. In addition to NAD(+), other dinucleotides such as NADP(+), the 3-acetylpyridine and thionicotinamide analogues of NAD(+) and the thionicotinamide analogue of NADP(+), function as substrates in the hydrolysis catalysed by the pyrophosphatase. 3. A decrease in the specific activity of NAD(+) pyrophosphatase was observed during larval development, and a barely detectable activity was found in the pupa and adult. 4. Enzyme activity per organism increased in the larva but decreased to a very low value in the pupa and adult. These results indicate that the decrease in specific activity was due to a decrease in enzyme concentration rather than an increase in amounts of protein.
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PMID:Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and aging mosquito. 438 8

Preparations enriched in plastids were used to investigate the location of ADP-glucose pyrophosphorylase (AGPase) in the developing endosperm of maize (Zea mays L.). These preparations contained more than 25% of the total activity of the plastid marker enzymes alkaline pyrophosphatase and soluble starch synthase, less than 2% of the cytosolic marker enzymes alcohol dehydrogenase and pyrophosphate, fructose 6-phosphate 1-phosphotransferase, and approximately 3% of the AGPase activity. Comparison with the marker enzyme distribution suggests that more than 95% of the activity of AGPase in maize endosperm is extra-plastidial. Two proteins were recognized by antibodies to the small subunit of AGPase from maize endosperm Brittle-2 (Bt2). The larger of the two proteins was the major small subunit in homogenates of maize endosperm, and the smaller, less abundant of the two proteins was enriched in preparations containing plastids. These results suggest that there are distinct plastidial and cytosolic forms of AGPase, which are composed of different subunits. Consistent with this was the finding that the bt2 mutation specifically eliminated the extraplastidial AGPase activity and the larger of the two proteins recognized by the antibody to the Bt2 subunit.
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PMID:The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial. 888 89

In this study we provide evidence for the first time that rat liver microsomal and peroxisomal fractions are able to phosphorylate free farnesol to its diphosphate ester in a CTP dependent manner. The farnesyl diphosphate (FPP) kinase activity is decreased in whole liver homogenates obtained from rats treated with cholesterol and unchanged in homogenates obtained from rats treated with cholestyramine. In contrast, farnesyl pyrophosphatase (FPPase) activity, an enzyme which specifically hydrolyzes FPP to farnesol is only found in the microsomal fraction and is unaffected by treatment of rats with cholesterol or cholestyramine. In addition, we also demonstrate that farnesol can be oxidized to a prenyl aldehyde, presumably by an alcohol dehydrogenase (ADH), and that this activity resides in the mitochondrial and peroxisomal fractions.
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PMID:Metabolism of farnesol: phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions. 901 62

Changes in the properties of extractable vacuolar H+-pumping pyrophosphatase (V-PPase) and vacuolar ATPase activities in chilling-sensitive seedlings of mung bean (Vigna radiata) were investigated. Following chilling at 4[deg]C for 48 h, both hydrolytic and proton-pumping activities of the V-PPase increased 1.5- to 2-fold over controls and remained elevated even after 72 h at low temperatures. Vacuolar ATPase levels did not change significantly throughout the chilling regime. However a large increase in alcohol dehydrogenase activity during chilling suggests a shift toward fermentative metabolism, which can be expected to decrease ATPase activity in situ. Western blotting of vacuolar membrane-enriched fractions from control and treated plants has confirmed that the changes in V-PPase activity are mirrored by increases in the amount of pump protein. Results suggest a specific role for the V-PPase in protecting chill-sensitive plants from the injurious effects of low temperatures via the maintenance of the proton gradient across the vacuolar membrane.
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PMID:Chill-Induced Changes in the Activity and Abundance of the Vacuolar Proton-Pumping Pyrophosphatase from Mung Bean Hypocotyls. 1222 20

Differential centrifugation and Percoll-gradient centrifugation of protoplast lysates of suspension-cultured cells of sycamore (Acer pseudoplatanus L.) yielded pure amyloplasts. Contamination of the final amyloplast preparation by foreign compartments was assessed by measuring marker enzyme activities. The activity of alkaline pyrophosphatase was taken as a 100% plastid marker; relative to this marker, mitochondria (cytochrome c oxidase) averaged 0.34%, microbodies (catalase) 0.61%, and cytosol (alcohol dehydrogenase) 0.09%. Enzymatic activities of the glycolytic, gluconeogenic, pentose phosphate and the starch degradation pathways were found to be present in these amyloplast extracts in appreciable amounts. But the pyrophosphate-dependent phosphofructokinase and phosphoglyceromutase were judged to be essentially absent from amyloplasts because the activities of these enzymes were not enriched above the level of contaminating enzymatic activities in the amyloplast fractions. Additionally, the in vitro activities of starch phosphorylase, ATP dependent phosphofructokinase, NAD dependent glyceraldehyde-3 phosphate dehydrogenase, and glucose-6 phosphate dehydrogenase did not seem to support carbon fluxes from starch to triose phosphates as calculated from the rate of starch disappearance during carbon starvation of the cells. These results provide additional, indirect evidence for the recently emerged view that, in addition to the well known phosphate-triosephosphate translocator, another hexose phosphate and possibly also an ATP/ADP translocating system play major roles in nongreen plastids.
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PMID:Enzyme Sets of Glycolysis, Gluconeogenesis, and Oxidative Pentose Phosphate Pathway Are Not Complete in Nongreen Highly Purified Amyloplasts of Sycamore (Acer pseudoplatanus L.) Cell Suspension Cultures. 1666 46

Pondweed (Potamogeton distinctus A. Benn.), a monocot aquatic plant species, has turions, which are overwintering buds forming underground as an asexual reproductive organ. Turions not only survive for more than one month but also elongate under strict anoxia, maintaining high-energy charge by activation of fermentation. We cloned 82 cDNA fragments of genes, that are up-regulated during anoxic growth of pondweed turions, by suppression subtractive hybridization. The transcript levels of 44 genes were confirmed to be higher under anoxia than those in air by both Northern blot analysis and a semi-quantitative reverse transcription polymerase chain reaction (RT-PCR) method. A homology search for their nucleotide sequences revealed that some of them are highly homologous to known sequences of genes from other plants. They included alcohol dehydrogenase, pyruvate decarboxylase (PDC), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), vacuolar H(+)-translocating pyrophosphatase and a plasma membrane intrinsic protein. Time courses of transcript accumulation of some genes under anoxia were different from those in air. The activity of PDC increased under anoxic conditions but the activities of GAPDH and pyrophosphatase remained constant after anoxic treatment. Anoxically up-regulated genes are possibly involved in physiological events to control energy production, pH regulation and cell growth under anoxia. These results suggest that transcriptional regulation of these genes serves as an essential part of survival and growth of pondweed turions under anoxia.
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PMID:Anoxia-enhanced expression of genes isolated by suppression subtractive hybridization from pondweed (Potamogeton distinctus A. Benn.) turions. 1750 72

1. Electron microscopic studies of the sieve tube sap obtained from the secondary phloem of Robinia pseudoacacia by the method of Hartig (1860) showed the presence of well developed mitochondria in addition to membrane fragments. 2. In this sieve tube sap the following enzymes could be detected qualitatively: UTP-glucose-1-phosphate-uridyl transferase, UDPG-fructose glucosyl transferase, glucose-6-phosphate dehydrogenase, hexokinase (for glucose and fructose), phosphohexose isomerase, phosphofructokinase, and UDPG-pyrophosphatase. 3. The following enzymes were determined quantitatively: phosphorylase, amylase, aldolase, triosephosphate isomerase, NAD(+)-dependent glyceraldehyde-3-phosphate dehydrogenase, phosphoglyceromutase, enolase, pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, isocitrate dehydrogenase, fumarase, malate dehydrogenase, glutamate-pyruvate transaminase, glutamate dehydrogenase, glutamate-oxalacetate transaminase, and anorganic pyrophosphatase. 4. The following enzymes could not be detected: UDGP dehydrogenase, UDPG-fructose-6-phosphate-glucosyltransferase, invertase, phosphoglucomutase, lactate dehydrogenase, and citrate synthase. 5. The enzyme pattern in the sieve tube saps of Tilia platyphyllos, Carpinus betulus, Fraxinus americana, Quercus borealis maxima, and Salix viminalis is qualitatively similar to that of Robinia, but shows quantitative differences (as far as analyzed). 6. The meaning of the results for the metabolism and function of the sieve tubes in situ is discussed.
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PMID:[Enzyme activities in the sieve tube sap of Robinia pseudoacacia L. and of other tree species]. 2449 58