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)

The dependence of the fluorescence emission maximum of the tryptophan residues in several two-tryptophan-containing proteins (horse liver alcohol dehydrogenase, yeast 3-phosphoglycerate kinase, Staphylococcus aureus metalloprotease and bee venom phospholipase A2) on the excitation wavelengths has been studied. Using fluorescence-resolved spectroscopy, we have dissected the contributions of particular tryptophan residues located in different parts of the protein molecule. The results demonstrate that dipolar structural relaxation can occur in the environment of tryptophan residues buried within protein molecules. The observed spectral shifts upon red-edge excitation of these residues can depend on temperature or ligand binding, as demonstrated in case of metalloprotease and alcohol dehydrogenase. No spectral shifts upon red-edge excitation have been observed for tryptophan residues totally exposed to the rapidly relaxing aqueous solvent.
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PMID:Red-edge excitation fluorescence measurements of several two-tryptophan-containing proteins. 158 74

We developed a continuous spectrophotometric assay of the phospholipase A2 activity specific for choline plasmalogen using rat liver lysoplasmalogenase and horse liver alcohol dehydrogenase as coupling enzymes and Naja naja venom phospholipase A2 as a source of the phospholipase A2 activity. In these coupling reactions, choline lysoplasmalogen is hydrolyzed by lysoplasmalogenase to glycerophosphocholine and free aldehyde. The free aldehyde is quantitatively converted to alcohol by alcohol dehydrogenase with the oxidation of NADH. The disappearance of NADH is measured spectrophotometrically at 340 nm. The assay is sensitive to about 0.2 nmol aldehyde produced/ml/min and also is rapid, convenient, and continuous.
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PMID:Continuous spectrophotometric assay of phospholipase A2 activity hydrolyzing plasmalogens using coupling enzymes. 271 87

This study demonstrates that p-bromophenacyl bromide irreversibly inhibits, in a time- and dose-dependent manner, yeast alcohol dehydrogenase, bovine pancreatic alpha-chymotrypsin, human platelet phosphatidylinositol (PI)-specific phospholipase C, in addition to the neutral-active and calcium-dependent phospholipase A2 of human platelets. The PI-specific phospholipase C has maximal activity at pH 5,5 is calcium-dependent, and is strongly inhibited by sulfhydryl reagents 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) and methylmethane thiosulfonate . Increasing concentrations of DTNB produced concomitant inhibition of phospholipase C activity and titration of sulfhydryl groups. In contrast, human platelet phospholipase A2 activity was unaffected by concentrations of DTNB that titrated sulfhydryl groups, and completely inhibited PI-specific phospholipase C activity. Treatment of cysteine with p-bromophenacyl bromide resulted in modification of the amino acid as demonstrated by paper chromatography, and loss of titratable sulfhydryl groups. These data show that p-bromophenacyl bromide inhibits a wide spectrum of enzymatic activities including PI-specific phospholipase C. This reagent modifies amino acid residues other than active-site histidines and therefore has a broader reactivity than previously considered. Thus, it should not be used as a selective inhibitor of enzymes in crude cellular experiments.
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PMID:Nonspecific inhibition of enzymes by p-bromophenacyl bromide. Inhibition of human platelet phospholipase C and modification of sulfhydryl groups. 673 33

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