Search results for "Substrate Specificity"

showing 10 items of 217 documents

Recombinant laccase from Pediococcus acidilactici CECT 5930 with ability to degrade tyramine

2017

Biogenic amines degradation by bacterial laccases is little known, so we have cloned and heterologously expressed, in E. coli, a new laccase from Pediococcus acidilactici CECT 5930 (Lpa5930), a lactic acid bacterium commonly found in foods able to degrade tyramine. The recombinant enzyme has been characterized by physical and biochemical assays. Here we report the optimization of expression and purification procedures of this laccase. DNA encoding sequence of laccase from P. acidilactici was amplified by PCR and cloned into the expression plasmid pET28a for induction by isopropyl-β-D-thiogalactoipyranoside. Protein expression was performed in E. coli BL21(DE3) harboring pGro7 plasmid expres…

0106 biological sciences0301 basic medicineArabinoseMolecular biologylcsh:MedicineLaccasesBiochemistryBiotecnologia01 natural sciencesSubstrate Specificitylaw.inventionDatabase and Informatics Methodschemistry.chemical_compoundlawRecombinant Protein PurificationCloning MolecularAmineslcsh:Sciencechemistry.chemical_classificationMultidisciplinaryABTSbiologyOrganic CompoundsTemperatureHydrogen-Ion ConcentrationTyramineRecombinant ProteinsEnzymesChemistryRecombination-Based AssayBiochemistryPhysical SciencesRecombinant DNAElectrophoresis Polyacrylamide GelOxidation-ReductionSequence AnalysisResearch ArticleProtein PurificationBioinformaticsTyramineLibrary ScreeningDNA constructionResearch and Analysis Methods03 medical and health sciencesBacterial ProteinsSequence Motif Analysis010608 biotechnologyAmino Acid SequenceBenzothiazolesPediococcus acidilacticiLaccaseMolecular Biology Assays and Analysis TechniquesBase SequenceMolecular massLaccaseOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsPediococcus acidilacticiSequence Analysis DNAbiology.organism_classificationMolecular biology techniques030104 developmental biologyEnzymechemistryPlasmid ConstructionEnzymologySpectrophotometry Ultravioletlcsh:QSulfonic AcidsEnzimsProteïnesPurification TechniquesPLOS ONE
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Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives

2016

The transglycosylation activity of amylosucrase (ASase) has received significant attention owing to its use of an inexpensive donor, sucrose, and broad acceptor specificity, including glycone and aglycone compounds. The transglycosylation reaction of recombinant ASase from Deinococcus radiopugnans (DRpAS) was investigated using various phenolic compounds, and quercetin-3-O-rutinoside (rutin) was found to be the most suitable acceptor molecule used by DRpAS. Two amino acid residues in DRpAS variants (DRpAS Q299K and DRpAS Q299R), assumed to be involved in acceptor binding, were constructed by site-directed mutagenesis. Intriguingly, DRpAS Q299K and DRpAS Q299R produced 10-fold and 4-fold hig…

0106 biological sciences0301 basic medicineGlycosylationGlycosylationStereochemistryRutinAmino Acid Motifs01 natural sciencesApplied Microbiology and BiotechnologySubstrate Specificity03 medical and health sciencesRutinchemistry.chemical_compoundAmylosucraseGlucosyltransferasesBacterial Proteins010608 biotechnologyDeinococcusBinding siteBinding SitesbiologyGeneral Medicinebiology.organism_classificationAcceptorMolecular Docking SimulationKinetics030104 developmental biologyAglyconechemistryGlucosyltransferasesbiology.proteinDeinococcusBiotechnologyJournal of Microbiology and Biotechnology
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Characterization and purification of a bacterial chlorogenic acid esterase detected during the extraction of chlorogenic acid from arbuscular mycorrh…

2016

International audience; A Gram-negative bacterium able to grow using chlorogenic acid (5-caffeoylquinic acid) as sole carbon source has been isolated from the roots of tomato plants inoculated with the arbuscular mycorrhizal fungus Rhizophagus irregularis. An intracellular esterase exhibiting very high affinity (K-m = 2 mu M) for chlorogenic acid has been extracted and purified by FPLC from the chlorogenate-grown cultures of this bacterium. The molecular mass of the purified esterase determined by SDS-PAGE was 61 kDa and its isoelectric point determined by chromatofocusing was 7.75. The esterase hydrolysed chlorogenic acid analogues (caffeoylshikimate, and the 4- and 3-caffeoylquinic acid i…

0106 biological sciences0301 basic medicineRhizophagus irregularisCoumaric AcidsPhysiologyRoot-associated bacteria[SDV]Life Sciences [q-bio]Arbuscular mycorrhizal fungiPlant ScienceBiologyCoumaric acidRoot exudates01 natural sciencesEsterasePlant RootsProtocatechuic acidSubstrate SpecificityFerulic acid03 medical and health scienceschemistry.chemical_compoundHydrolysisChlorogenic acidBacterial ProteinsSolanum lycopersicumMycorrhizaeGeneticsMethyl caffeate[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyBacteriaEthanolMethanolChlorogenic acidbiology.organism_classification6. Clean waterChlorogenase030104 developmental biologychemistryBiochemistry[SDE]Environmental SciencesCarboxylic Ester Hydrolases010606 plant biology & botany
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Characterization of (3H) acifluorfen binding to purified pea etioplasts, and evidence that protoporphyrinogen oxidase specifically binds acifluorfen

1992

It is now generally accepted that protoporphyrinogen oxidase is the target-enzyme for diphenylether-type herbicides. Recent studies [Camadro, J-M., Matringe, M., Scalla, R. & Labbe, P. (1991) Biochem. J. 277, 17–21] have revealed that in maize, diphenyl ethers competitively inhibit protoporphyrinogen oxidase with respect to its substrate, protoporphyrinogen IX. In this study, we show that, in purified pea etioplast, [3H]acifluorfen specifically binds to a single class of high-affinity binding sites with an apparent dissociation constant of 6.2 ± 1.3 nM and a maximum density of 29 ± 5 nmol/g protein. [3H]Acifluorfen binding reaches equilibrium in about 1 min at 30°C. Half dissociation occurs…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]PhthalimidesAcifluorfen01 natural sciencesBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEEtioplastProtoporphyrinogen OxidaseBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOrganelles0303 health sciencesOxidase testBinding SitesPlants MedicinalProtoporphyrin IXMolecular StructureBIOCHIMIEHerbicidesFabaceaeProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryBiochemistryNitrobenzoatesProtoporphyrinogen oxidaseOxidoreductases010606 plant biology & botany
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Evaluation of an amino acid residue critical for the specificity and activity of human Gb3/CD77 synthase

2016

Human Gb3/CD77 synthase (α1,4-galactosyltransferase) is the only known glycosyltransferase that changes acceptor specificity because of a point mutation. The enzyme, encoded by A4GALT locus, is responsible for biosynthesis of Gal(α1–4)Gal moiety in Gb3 (CD77, Pk antigen) and P1 glycosphingolipids. We showed before that a single nucleotide substitution c.631C > G in the open reading frame of A4GALT, resulting in replacement of glutamine with glutamic acid at position 211 (substitution p. Q211E), broadens the enzyme acceptor specificity, so it can not only attach galactose to another galactose but also to N-acetylgalactosamine. The latter reaction leads to synthesis of NOR antigens, which are…

0301 basic medicineAcetylgalactosamineMutation MissenseBiochemistryGlycosphingolipidsSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundGb3/CD77 synthaseBiosynthesisCell Line TumorGlycosyltransferaseAspartic acidHumansAsparagineSite-directed mutagenesisMolecular BiologySite-directed mutagenesisbiologyAntigens NuclearGlutamic acidCell BiologyGalactosyltransferasesMolecular biologyEnzyme assayGlutamineP1PK blood group system030104 developmental biologyAmino Acid SubstitutionBiochemistrychemistryGlycopshingolipidsbiology.proteinNOR polyagglutinationOriginal ArticleGlycoconjugate Journal
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GH57 amylopullulanase from Desulfurococcus amylolyticus JCM 9188 can make highly branched cyclodextrin via its transglycosylation activity.

2018

Abstract Desulfurococcus amylolyticus is an anaerobic and hyperthermophilic crenarchaeon that can use various carbohydrates as energy sources. We found a gene encoding a glycoside hydrolase family 57 amylolytic enzymes (DApu) in a putative carbohydrate utilization gene cluster in the genome of D. amylolyticus . This gene has an open reading frame of 1,878 bp and consists of 626 amino acids with a molecular mass of 71 kDa. Recombinant DApu (rDApu) completely hydrolyzed pullulan to maltotriose by attacking α-1,6-glycosidic linkages, and was able to produce glucose and maltose from soluble starch and amylopectin. Although rDApu showed no activity toward α-cyclodextrin (CD) and β-CD, maltooctao…

0301 basic medicineGlycosylationGlycoside HydrolasesArchaeal ProteinsBioengineeringApplied Microbiology and BiotechnologyBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundHydrolysisOpen Reading FramesGene clusterEnzyme StabilityMaltotrioseGlycoside hydrolaseCloning MolecularMaltoseGlucansCyclodextrins030102 biochemistry & molecular biologyDesulfurococcaceaePullulanMaltoseMolecular Weight030104 developmental biologychemistryBiochemistryAmylopectinEnergy sourceTrisaccharidesBiotechnologyEnzyme and microbial technology
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Analysis of substrate binding in individual active sites of bifunctional human ATIC

2018

Aminoimidazolecarboxamide ribonucleotide formyl transferase (AICARFT): Inosine monophosphate cyclohydrolase (IMPCH, collectively called ATIC) is a bifunctional enzyme that catalyses the penultimate and final steps in the purine de novo biosynthesis pathway. The bifunctional protein is dimeric and each monomer contains two different active sites both of which are capable of binding nucleotide substrates, this means to a potential total of four distinct binding events might be observed. Within this work we used a combination of site-directed and truncation mutants of ATIC to independently investigate the binding at these two sites using calorimetry. A single S10W mutation is sufficient to blo…

0301 basic medicineHydroxymethyl and Formyl TransferasesModels MolecularRibonucleotideStereochemistryBiophysicsBiochemistryAnalytical ChemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMultienzyme ComplexesCatalytic DomainTransferaseHumansNucleotidePhosphofructokinase 2Bifunctional enzymesMolecular Biologychemistry.chemical_classification030102 biochemistry & molecular biologybiologyNucleotidesActive siteCooperative bindingIsothermal titration calorimetryXanthosine monophosphate030104 developmental biologyBiochemistrychemistryNucleotide DeaminasesMultiple binding sitesbiology.proteinIsothermal titration calorimetryProtein Binding
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Conversion of the sensor kinase DcuS ofEscherichia coliof the DcuB/DcuS sensor complex to the C4-dicarboxylate responsive form by the transporter DcuB

2016

Summary The sensor kinase DcuS of Escherichia coli co-operates under aerobic conditions with the C4-dicarboxylate transporter DctA to form the DctA/DcuS sensor complex. Under anaerobic conditions C4-dicarboxylate transport in fumarate respiration is catalyzed by C4-dicarboxylate/fumarate antiporter DcuB. (i) DcuB interacted with DcuS as demonstrated by a bacterial two-hybrid system (BACTH) and by co-chromatography of the solubilized membrane-proteins (mHPINE assay). (ii) In the DcuB/DcuS complex only DcuS served as the sensor since mutations in the substrate site of DcuS changed substrate specificity of sensing, and substrates maleate or 3-nitropropionate induced DcuS response without affec…

0301 basic medicineKinaseAntiporter030106 microbiologyTransporterBiologymedicine.disease_causeMicrobiology03 medical and health sciencesBiochemistrySolubilizationmedicineSubstrate specificityEscherichia coliEcology Evolution Behavior and SystematicsEnvironmental Microbiology
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Diverse relations between ABC transporters and lipids: An overview.

2016

It was first discovered in 1992 that P-glycoprotein (Pgp, ABCB1), an ATP binding cassette (ABC) transporter, can transport phospholipids such as phosphatidylcholine, -ethanolamine and -serine as well as glucosylceramide and glycosphingolipids. Subsequently, many other ABC transporters were identified to act as lipid transporters. For substrate transport by ABC transporters, typically a classic, alternating access model with an ATP-dependent conformational switch between a high and a low affinity substrate binding site is evoked. Transport of small hydrophilic substrates can easily be imagined this way, as the molecule can in principle enter and exit the transporter in the same orientation. …

0301 basic medicineModels MolecularATP Binding Cassette Transporter Subfamily BBiophysicsGene ExpressionATP-binding cassette transporterPhosphatidylserinesBiologyBiochemistrySubstrate SpecificitySerine03 medical and health sciencesLipid translocationHumansProtein IsoformsBinding siteLipid bilayerLipid TransportATP-binding domain of ABC transportersBinding SitesPhosphatidylethanolaminesFatty AcidsTransporterBiological TransportCell BiologyCell biology030104 developmental biologyBiochemistryPhosphatidylcholineslipids (amino acids peptides and proteins)Protein BindingBiochimica et biophysica acta. Biomembranes
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Addition of thiols to the double bond of dipeptide C-terminal dehydroalanine as a source of new inhibitors of cathepsin C.

2017

Addition of thiols to double bond of glycyl-dehydroalanine and phenyl-dehydroalanine esters provided micromolar inhibitors of cathepsin C. The structure-activity studies indicated that dipeptides containing N-terminal phenylalanine exhibit higher affinity towards the enzyme. A series of C-terminal S-substituted cysteines are responsible for varying interaction with S1 binding pocket of cathepsin C. Depending on diastereomer these compounds most likely act as slowly reacting substrates or competitive inhibitors. This was proved by TLC analysis of the medium in which interaction of methyl (S)-phenylalanyl-(R,S)-(S-adamantyl)cysteinate (7i) with the enzyme was studied. Molecular modeling enabl…

0301 basic medicineModels MolecularDouble bondStereochemistryPhenylalanineCysteine Proteinase InhibitorsBiochemistryCathepsin CCathepsin CSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity Relationship0302 clinical medicineDehydroalanineMoietyAnimalsSulfhydryl CompoundsBinding sitechemistry.chemical_classificationDipeptideAlanineBinding SitesDehydropeptidesDiastereomerEnzyme inhibitorsGeneral MedicineDipeptidesKinetics030104 developmental biologychemistryThiol addition030220 oncology & carcinogenesisCattleBiochimie
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