Search results for "Enzyme activator"

showing 9 items of 39 documents

Biochemistry and pharmacology of novel anthranilic acid derivatives activating heme-oxidized soluble guanylyl cyclase.

2005

The heme-enzyme soluble guanylyl cyclase (sGC) is an ubiquitous NO receptor, which mediates NO downstream signaling by the generation of cGMP. We studied the mechanism of action of the anthranilic acid derivatives 5-chloro-2-(5-chloro-thiophene-2-sulfonylamino-N-(4-(morpholine-4-sulfonyl)-phenyl)-benzamide sodium salt (HMR1766) (proposed international nonproprietary name, ataciguat sodium) and 2-(4-chloro-phenylsulfonylamino)-4,5-dimethoxy-N-(4-(thiomorpholine-4-sulfonyl)-phenyl)-benzamide (S3448) as a new class of sGC agonists. Both compounds activated different sGC preparations (purified from bovine lung, or crude from human corpus cavernosum) in a concentration-dependent and quickly reve…

Vasodilator AgentsBlood PressureHemePharmacologychemistry.chemical_compoundEnzyme activatorAnthranilic acidmedicineCyclic GMP-Dependent Protein KinasesAnimalsortho-AminobenzoatesReceptorHemePharmacologySulfonamidesProtoporphyrin IXActivator (genetics)Enzyme ActivationchemistryMechanism of actionBiochemistryGuanylate CyclaseMolecular MedicineCattlemedicine.symptomSoluble guanylyl cyclaseOxidation-ReductionMolecular pharmacology
researchProduct

Enzymes involved in vinyl acetate decomposition by Pseudomonas fluorescens PCM 2123 strain

2014

Esterases are widely used in food processing industry, but there is little information concerning enzymes involved in decompositions of esters contributing to pollution of environment. Vinyl acetate (an ester of vinyl alcohol and acetic acid) is a representative of volatile organic compounds (VOCs) in decomposition, of which hydrolyses and oxidoreductases are mainly involved. Their activities under periodically changing conditions of environment are essential for the removal of dangerous VOCs. Esterase and alcohol/aldehyde dehydrogenase activities were determined in crude cell extract from Pseudomonas fluorescens PMC 2123 after vinyl acetate induction. All examined enzymes exhibit their hig…

Vinyl alcoholVinyl CompoundsenzymesEnzyme ActivatorsAlcoholPseudomonas fluorescensEsteraseMicrobiologyArticlechemistry.chemical_compoundAcetic acidesterasesEnzyme StabilityVinyl acetateOrganic chemistryEnzyme InhibitorsBiotransformationAlcohol dehydrogenaseEthanolbiologyAcetaldehydeTemperatureGeneral MedicineHydrogen-Ion ConcentrationKineticschemistrybiology.proteinvinyl acetateOxidoreductasesFolia Microbiologica
researchProduct

Sea urchin deciliation induces thermoresistance and activates the p38 mitogen-activated protein kinase pathway.

2003

In this study, we demonstrate by a variety of approaches (ie, morphological analysis, Western blots, immunolocalization, and the use of specific antibodies) that hyperosmotic deciliation stress of sea urchin embryos induces a thermotolerant response. Deciliation is also able to activate a phosphorylation signaling cascade the effector of which might be the p38 stress-activated protein kinase because we found that the administration of the p38 inhibitor SB203580 to sea urchin deciliated gastrula embryos makes the hyperosmotic deciliation stress lethal.

animal structuresHot TemperaturePyridinesp38 mitogen-activated protein kinasesSEA URCHIN DECILIATION p38MAP KINASEBiochemistryp38 Mitogen-Activated Protein KinasesEnzyme activatorStress Physiologicalbiology.animalAnimalsCiliaSettore BIO/06 - Anatomia Comparata E CitologiaPhosphorylationProtein kinase ASea urchinbiologyEffectorImidazolesAntibodies MonoclonalCell BiologyGastrulaOriginal ArticlesMolecular biologyBlotEnzyme ActivationSea Urchinsembryonic structuresPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionMitogen-Activated Protein KinasesSignal TransductionCell stresschaperones
researchProduct

Interactions of the mitochondrial membrane rat liver d-3-hydroxybutyrate dehydrogenase with glass beads during adsorption chromatography

1991

D-3-Hydroxybutyrate dehydrogenase (BDH) is an NAD(+)-dependent dehydrogenase of the mitochondrial inner membrane involved in the energetic balance between the liver and peripheral organs in mammals. It allows the conversion of ketone bodies (acetoacetate and D-3-hydroxybutyrate) and it is one of the best documented lipid-requiring enzymes with a dependence on lecithins. After release of proteins from the membrane by phospholipase A2 treatment of salt-treated mitochondria, the rat liver enzyme is absorbed on controlled-pore glass beads. After batch washing, the enzyme, devoid of lipids (apoBDH), is specifically eluted at pH 8.05-8.15 with a 0.1 M Tris-1 M LiBr buffer under reducing condition…

chemistry.chemical_classificationChromatographyOrganic ChemistryPhospholipidDehydrogenaseGeneral MedicineMitochondrionBiochemistryDithiothreitolAnalytical ChemistryEnzyme activatorchemistry.chemical_compoundEnzymeBiochemistrychemistryNAD+ kinaseInner mitochondrial membraneJournal of Chromatography A
researchProduct

The amphipathic peptide mellitin as a tool to study the membrane-dependent activation of tissue transglutaminase

2001

The role of membrane phospholipids on the cross-linking activity of guinea pig liver (tissue) transglutaminase has been investigated using the amphipathic model peptide melittin as glutaminyl substrate and the primary amine monodansylcadaverine as extrinsic amine donor. A marked increase of transglutaminase catalytic activity was observedin vitro assays in the presence of neutral membrane phospholipids. In contrast, activation was abolished in the presence of membranes containing pure anionic lipids. Enzyme activation could be ascribed to a direct binding of the lipid to the protein as demonstrated in enzymatic assays using a non membrane-interacting peptide (Cbz-Gln-Gly). The data obtained…

chemistry.chemical_classificationbiologyTissue transglutaminaseBioengineeringPeptideBiochemistryMelittinIn vitroAnalytical ChemistryEnzyme activatorchemistry.chemical_compoundMembranechemistryBiochemistryDrug DiscoveryAmphiphilebiology.proteinMolecular Medicinelipids (amino acids peptides and proteins)Lipid bilayerLetters in Peptide Science
researchProduct

2013

Nitric oxide, produced by the neuronal nitric oxide synthase (nNOS) from L-arginine is an important second messenger molecule in the central nervous system: It influences the synthesis and release of neurotransmitters and plays an important role in long-term potentiation, long-term depression and neuroendocrine secretion. However, under certain pathological conditions such as Alzheimer’s or Parkinson’s disease, stroke and multiple sclerosis, excessive NO production can lead to tissue damage. It is thus desirable to control NO production in these situations. So far, little is known about the substrate supply to human nNOS as a determinant of its activity. Measuring bioactive NO via cGMP form…

chemistry.chemical_compoundEnzyme activatorMultidisciplinarychemistryArginineBiochemistrySecond messenger systemCitrullineExtracellularLong-term potentiationBiologyIntracellularNitric oxidePLOS ONE
researchProduct

Allosteric regulation by Mg2+ of the vacuolar H(+)-PPase from Acer pseudoplatanus cells. Ca2+/Mg2+ interactions.

1996

The tonoplast H(+)-PPase was previously characterized in Acer pseudoplatanus cells (Pugin et al (1991) Plant Sci 73, 23-34; Fraichard et al (1993) Plant Physiol Biochem 31, 349-359). Tonoplast vesicles were obtained from vacuoles isolated from protoplasts of A pseudoplatanus suspension cultures and used to study kinetic effects of Mg2+ and Ca2+ on PPi hydrolysis. The concentrations of ionic species (free Mg2+, free PPi, and MgPPi complexes) were calculated with apparent dissociation constants of 55.3 microM for MgPPi and 59.6 microM for CaPPi. Our results indicated that the substrate of the tonoplast PPase was a MgPPi complex and that free Mg2+ was essential for PPi hydrolysis. With fixed f…

inorganic chemicals0106 biological sciencesTrisAllosteric regulation01 natural sciencesBiochemistryTrees03 medical and health sciencesEnzyme activatorchemistry.chemical_compoundOrganophosphorus CompoundsAllosteric Regulation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMagnesiumBinding sitePyrophosphatasesComputingMilieux_MISCELLANEOUSCells Cultured030304 developmental biologychemistry.chemical_classification0303 health sciencesInorganic pyrophosphataseERABLE FAUX PLATANEGeneral MedicineDissociation constantEnzyme ActivationInorganic PyrophosphataseKineticsEnzymechemistryBiochemistryVacuolesCalciumUncompetitive inhibitor010606 plant biology & botanyBiochimie
researchProduct

Different modes of activating phosphofructokinase, a key regulatory enzyme of glycolysis, in working vertebrate muscle

2002

Glycolytic flux in white muscle can be increased several-hundredfold by exercise. Phosphofructokinase (PFK; EC 2.7.1.11) is a key, regulatory enzyme of glycolysis, but how its activity in muscle is controlled is not fully, understood. In order not to neglect integrative aspects of metabolic regulation, we have studied in frogs (Rana temporaria) a physiological form of muscle work (swimming) that can be triggered like a reflex. We analysed swimming to fatigue in well rested frogs, recovery from exercise, and repeated exercise after 2 h of recovery. At various times, gastrocnemius muscles were tested for glycolytic intermediates and effectors of PFK. All metabolites responded similarly to the…

medicine.medical_specialtyFructoseMetabolismBiologyBiochemistrychemistry.chemical_compoundEnzyme activatorEndocrinologychemistryInternal medicineExtracellularReflexmedicineMyocyteGlycolysisPhosphofructokinaseBiochemical Society Transactions
researchProduct

In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor.

1996

AbstractProteolytic processing of the nonstructural proteins of the hepatitis C virus (HCV) is mediated by two viral proteinases: the NS2-3 proteinase cleaving at the NS2/3 junction and the NS3 serine-type proteinase responsible for processing at the NS3/4A, NS4A/B, NS4B/5A, and NS5A/B sites. Activity of the NS3 proteinase is modulated by NS4A. In the absence of this cofactor processing at the NS3-dependent sites does not occur or, in the case of the NS5A/B junction, is poor but increased when NS4A is present. Although recent studies demonstrated that proteinase activation requires direct interaction between NS3 and NS4A, the mechanism by which NS4A exerts the activation function is not kno…

virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsCell LineEnzyme activatorProteinase 3VirologyCricetinaeMicrosomesAnimalsHumansAmino Acid SequenceBinding siteNS5APeptide sequenceSequence Deletionchemistry.chemical_classificationNS3Binding SitesBase Sequencevirus diseasesIntracellular Membranesbiochemical phenomena metabolism and nutritionMolecular biologyIn vitrodigestive system diseasesAmino acidEnzyme ActivationBiochemistrychemistryDNA ViralPeptidesHeLa CellsVirology
researchProduct