Search results for "Substrate specificity"

showing 10 items of 217 documents

Differential modulation of CYP2E1 activity by cAMP-dependent protein kinase upon Ser129 replacement.

1998

Many toxic compounds are activated by cytochrome P450 (CYP) 2E1 to reactive metabolites, which represents a potential hazard for cellular homeostasis. Therefore knowledge about CYP2E1 regulation could be of great biological importance. It has been shown that CYP2E1 is controlled transcriptionally and post-translationally by phosphorylation. In the present study we investigated the role of serine-129 (Ser129) in the protein kinase A (PKA) recognition sequence motif Arg-Arg-Phe-Ser129. To gain further insights into the possible relevance of Ser129 for CYP2E1 function, Ser129 was replaced by alanine (Ala) or glycine (Gly) by site-directed mutations of the cDNA coding for CYP2E1. The mutant cDN…

MaleMutantCellular homeostasisTransfectionDimethylnitrosamineSubstrate SpecificityRats Sprague-DawleyMiceCricetulusCricetinaeIsoniazidSerineAnimalsEnzyme inducerPhosphorylationProtein kinase ALungCells Culturedchemistry.chemical_classificationMice Inbred BALB CbiologyCytochrome P-450 CYP2E1Cell BiologyFibroblastsMolecular biologyCyclic AMP-Dependent Protein KinasesAmino acidRatsEnzymechemistryBiochemistryAmino Acid SubstitutionBucladesineEnzyme InductionInactivation MetabolicMutationbiology.proteinMicrosomes LiverPhosphorylationDemethylaseMutagensExperimental cell research
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Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases.

1992

1. Dihydrodiol dehydrogenase activities were investigated in rabbit liver. Using a five-step purification scheme, eight isoenzymes of dihydrodiol dehydrogenase with isoelectric points of 5.55-9.3 and promoter molecular masses of 34-35 kDa were purified to apparent homogeneity and designated CF-1 to CF-6, CM-1 and CM-2. 2. CF-1 and CF-2 had near-neutral isoelectric points of 7.4 and 6.8 and molecular masses of about 125 kDa in the native state. Both enzymes readily accepted NAD+ as well as NADP+ as coenzymes, had relatively low Km values of 0.33 mM and 0.47 mM for benzene dihydrodiol and resembled previously described carbonyl reductases in their substrate specificity towards ketones and qui…

MaleOxidoreductases Acting on CH-CH Group DonorsCarbonyl ReductaseStereochemistryAldo-Keto ReductasesDehydrogenaseReductaseBiochemistryCofactorCatalysisSubstrate SpecificityAldehyde Reductasepolycyclic compoundsAnimalsTissue DistributionIsoelectric PointAldehyde ReductaseAldo-keto reductasebiologyChemistryHydroxysteroid DehydrogenasesAntibodies MonoclonalHydroxysteroid DehydrogenasesIsoenzymesMolecular WeightAlcohol OxidoreductasesBiochemistryLiverbiology.proteinElectrophoresis Polyacrylamide GelNAD+ kinaseRabbitsOxidoreductasesEuropean journal of biochemistry
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Association of a polyuridylate-specific endoribonuclease with small nuclear ribonucleo-proteins which had been isolated by affinity chromatography us…

1983

Immunoglobulins, containing antibodies against U1-snRNP, have been prepared from a patient with systemic lupus erythematosus. After coupling these antibodies to a Sepharose matrix, U-snRNPs have been isolated and purified from rat liver nuclei by use of immunoaffinity chromatography. The resulting RNPs had the typical protein pattern of U-sn RNPs and a sedimentation coefficient of 12 S. The U-snRNP preparation was associated with an endoribonuclease which required Mg2+ for optimal activity. The enzyme, with an pH optimum of 6.2, degraded only poly(U). Other single-stranded polyribo- and polydeoxyribonucleotides, tRNA, as well as double-stranded RNA and DNA were not digested. The products of…

MalePoly UEndoribonucleaseAntibody AffinityBiologyenvironment and public healthBiochemistryChromatography AffinitySubstrate SpecificitySepharosechemistry.chemical_compoundAffinity chromatographyEndoribonucleasesAnimalsHumansLupus Erythematosus Systemicchemistry.chemical_classificationImmunochemistryRNARats Inbred StrainsRibonucleoproteins Small NuclearMolecular biologyRatsEnzymechemistryLiverRibonucleoproteinsAntibodies AntinuclearImmunoglobulin GRNA splicingTransfer RNADNAEuropean journal of biochemistry
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The major isozyme of rat cardiac glutathione transferases. Its correspondence to hepatic transferase X.

1986

1. A major isozyme of rat heart glutathione transferase was purified to homogeneity by Sephadex G-200 gel filtration, ammonium sulfate precipitation, CM-cellulose chromatography and affinity chromatography on S-hexylglutathione-linked Sepharose 6B. 2. The purified isozyme was a dimer with an apparent relative molecular mass of 50000 composed of two Yb-size subunits (Mr= 26 500). The isozyme is immunologically related to rat liver glutathione transferase X and 3–3, especially closely to transferase X, and no immunological cross-reactivity with subunits 1 and 2 of hepatic glutathione transferases was observed. The isoelectric point (pI = 6.9) of the isozyme was identical with and the substrat…

MalePyruvate dehydrogenase lipoamide kinase isozyme 1ImmunodiffusionBiologyBiochemistryIsozymeChromatography AffinitySubstrate SpecificitySepharosechemistry.chemical_compoundAffinity chromatographyTransferaseAnimalsIsoelectric PointGlutathione TransferaseMolecular massMyocardiumRats Inbred StrainsGlutathioneHydrogen-Ion ConcentrationMolecular biologyRatsIsoenzymesMolecular WeightIsoelectric pointchemistryBiochemistryLiverChromatography GelElectrophoresis Polyacrylamide GelEuropean journal of biochemistry
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Nucleoside phosphotransferase in animal tissues. Tissue distribution and kinetic properties

1985

Amphibian, avian and mammal tissues contain a nucleoside phosphotransferase clearly different from those previously described in vegetables and bacteria. Whatever the animal source, the enzyme showed many similar characteristics as far as substrate specificity, dependence upon Mg2+, instability at 37 degrees C, and the protecting effect of nucleotides were concerned. Moreover, when submitted to gel filtration, the enzyme behaved in all cases as a dissociable high molecular weight protein, whose degree of association was controlled by nucleotides. In amphibian and avian tissues multiple forms of the enzyme seem to be present which differ for the substrate concentration at half-maximal veloci…

MaleRanidaeClinical BiochemistryKineticsSize-exclusion chromatographyChick EmbryoBiologySubstrate SpecificityCricetinaeSettore BIO/10 - BiochimicaNucleoside phosphotransferaseIntestine SmallTestisAnimalsNucleotideMagnesiumHorsesMolecular Biologychemistry.chemical_classificationEffectorPhosphotransferasesTemperatureBrainCell BiologyGeneral Medicinebiology.organism_classificationRatsKineticsEnzymeNucleoside phosphotransferaseTissue distributionchemistryBiochemistryChromatography GelCattleRabbitsChickensPhosphotransferasesBacteriaSpleen
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Mass spectrometric identification of the amino donor and acceptor sites in a transglutaminase protein substrate secreted from rat seminal vesicles.

1991

Four different transglutaminase-modified forms of a protein secreted by the rat seminal vesicles (SV-IV) were synthesized in vitro and characterized. FAB maps of both the native protein and its derivatives, produced by the purified guinea pig liver enzyme in the presence or absence of the polyamine spermidine, were obtained by mass spectrometric analysis after proteolytic digestions. Two differently derivatized SV-IV molecular forms, both possessing only one glutamine residue out of two (Gln-86) cross-linked to endogenous lysine residues, were produced when spermidine was omitted from the reaction mixture: (i) an insoluble homopolymer in which Lys-2, -4, -59, -78, -79, and -80 were involved…

MaleTissue transglutaminaseSeminal Plasma ProteinsLysineGuinea PigsMolecular Sequence DataBiochemistryMass SpectrometrySubstrate SpecificityResidue (chemistry)chemistry.chemical_compoundAnimalsAmino Acid Sequencechemistry.chemical_classificationIsopeptide bondTransglutaminasesbiologyHydrolysisSeminal Plasma ProteinsProstatic Secretory ProteinsProteinsSeminal VesiclesRats Inbred StrainsRatsSpermidineSecretory proteinchemistryBiochemistryLiverbiology.proteinPolyamineChromatography LiquidBiochemistry
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Formation of mono- and diglucuronides and other glycosides of benzo(a)pyrene-3,6-quinol by V79 cell-expressed human phenol UDP-glucuronosyltransferas…

1995

Glucuronidation of quinols of polycyclic aromatic hydrocarbons (PAHs) represents an important detoxication pathway preventing toxic quinone/quinol redox cycles. Therefore, mono- and diglucuronide formation of benzo(a)pyrene-3,6-quinol was investigated and compared to that of structurally related 3,6-dihydroxychrysene and simple phenols (1-naphthol and 4-methylumbelliferone) using V79 cell-expressed human UGT1.6 (= P1) and human UGT1.7 (= P4). Properties of human UGT1.6 were compared to those of the rat ortholog. Cofactors related to UDP-glucuronic acid such as UDP-galacturonic acid and UDP-glucose were also studied. It was found that rat and human UGT1.6 and human UGT1.7 catalyse monoglucur…

MaleUridine Diphosphate GlucoseGlucuronosyltransferaseStereochemistryGlucuronidationGlucuronatesmacromolecular substancesBiochemistryIsozymeSubstrate Specificitychemistry.chemical_compoundGlucosidesAnimalsHumansPhenolsBenzopyrenesGlucuronosyltransferaseRats WistarCarcinogenPharmacologychemistry.chemical_classificationbiologyGlycosideHydroquinonesRatsQuinonechemistryBenzo(a)pyreneBiochemistryUridine Diphosphate Glucuronic Acidbiology.proteinBiochemical Pharmacology
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Genetic and biochemical characterization of little isoxanthopterin (lix), a gene controlling dihydropterin oxidase activity in Drosophila melanogaste…

1991

Dihydropterin oxidase catalyses the oxidation of 7,8-dihydropteridines into their fully oxidized products, and is involved in the biosynthesis of isoxanthopterin. Fifteen Drosophila melanogaster mutants, selected for their low pterin and isoxanthopterin content, were assayed for dihydropterin oxidase activity. The activity was around 100% in most mutants tested, slightly reduced in red, g and dke, and undetectable in lix. In flies carrying various doses of the lix+ allele, a correlation was found between enzyme activity and the number of lix+ copies in the genome. The results suggest that lix is the structural gene for the dihydropterin oxidase enzyme. Isoxanthopterin was quantitated in str…

MaleX ChromosomeGenotypeMutantSubstrate Specificitychemistry.chemical_compoundDihydropterin oxidase activityDrosophilidaeGeneticsAnimalsPterinMolecular BiologyCrosses Geneticchemistry.chemical_classificationbiologyPteridinesStructural geneTemperatureChromosome Mappingbiology.organism_classificationEnzyme assayEnzymeDrosophila melanogasterchemistryBiochemistryMutationbiology.proteinFemaleDrosophila melanogasterOxidoreductasesMoleculargeneral genetics : MGG
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The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates

1995

The present study examined the distribution of the pro-hormone convertases PC1, PC2, furin, PACE4 and PC5 in the rat heart. Northern blot analysis of RNA extracted from cardiac tissues showed high levels of furin and PACE4 mRNA in the atria and ventricles, while PC5 mRNA was found to be expressed at high levels in the dorsal aorta. Although undetectable by Northern blot analysis, both PC1 and PC2 mRNA were detected by in situ hybridization and immunohistochemistry in discrete regions of the intracardiac para-aortic ganglia. In situ hybridization studies also showed that furin mRNA was observed in all cardiac tissues and cells, consistent with the previously reported ubiquitous expression of…

Malemedicine.medical_specialtyHistologyMolecular Sequence DataGene ExpressionIn situ hybridizationSubstrate SpecificityPathology and Forensic MedicineRats Sprague-DawleyDorsal aortaInternal medicineGene expressionmedicineAnimalsAspartic Acid EndopeptidasesAmino Acid SequenceNorthern blotFurinIn Situ HybridizationMessenger RNAbiologyMyocardiumSerine EndopeptidasesRNACell BiologyBlotting NorthernImmunohistochemistryMolecular biologyHormonesRatsEndocrinologycardiovascular systembiology.proteinImmunohistochemistryCell and Tissue Research
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Shedding of interleukin-6 receptor and tumor necrosis factor alpha. Contribution of the stalk sequence to the cleavage pattern of transmembrane prote…

2000

A functionally and structurally diverse group of transmembrane proteins including transmembrane forms of mediators or receptors can be proteolytically cleaved to form soluble growth factors or receptors. Recently, the proteolytic activity responsible for pro-tumor necrosis factor alpha (proTNFalpha) processing has been identified and named TACE (TNFalpha converting enzyme). In experiments with TACE deficient (TACE-/-) fibroblasts we found that 4beta-phorbol 12-myristate 13-acetate (PMA)-induced shedding of the interleukin-6 receptor (IL-6R) is strongly reduced. A basal hydroxamate sensitive release of IL-6R, however, could still be detected. This result demonstrates that TACE plays a role i…

MetalloproteinaseTumor Necrosis Factor-alphaHydrolysisRecombinant Fusion ProteinsMembrane ProteinsMetalloendopeptidasesBiologyADAM17 ProteinFibroblastsCleavage (embryo)BiochemistryFusion proteinMolecular biologyReceptors Interleukin-6Transmembrane proteinSubstrate SpecificityADAM ProteinsMiceComplementary DNAInterleukin-6 receptorCOS CellsAnimalsTetradecanoylphorbol AcetateTumor necrosis factor alphaReceptorEuropean journal of biochemistry
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