Search results for "Specificity."

showing 10 items of 2232 documents

Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks f…

2015

Δ3,Δ2-Enoyl-CoA isomerases (ECIs) catalyze the shift of a double bond from 3Z- or 3E-enoyl-CoA to 2E-enoyl-CoA. ECIs are members of the crotonase superfamily. The crotonase framework is used by many enzymes to catalyze a wide range of reactions on acyl-CoA thioesters. The thioester O atom is bound in a conserved oxyanion hole. Here, the mode of binding of acyl-CoA substrate analogues to peroxisomalSaccharomyces cerevisiaeECI (ScECI2) is described. The best defined part of the bound acyl-CoA molecules is the 3′,5′-diphosphate-adenosine moiety, which interacts with residues of loop 1 and loop 2, whereas the pantetheine part is the least well defined. The catalytic base, Glu158, is hydrogen-bo…

Models MolecularSaccharomyces cerevisiae ProteinsDouble bondStereochemistryProtein ConformationIsomeraseSaccharomyces cerevisiaeEnoyl CoA isomeraseThioesterPhotochemistryDodecenoyl-CoA Isomerasebeta-oxidationSubstrate SpecificityStructural Biologyddc:570Catalytic DomainEnzyme StabilitySide chainMoietyta116chemistry.chemical_classificationHydrogen bondenoyl-CoA isomeraseta1182Hydrogen BondingGeneral Medicinehydrogen-bond networkcrotonaseoxyanion holechemistryAcyl Coenzyme AOxyanion holeOxidation-ReductionProtein BindingActa crystallographica. Section D, Biological crystallography
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Experimental and Computational Studies of Hydrogen Bonding and Proton Transfer to [Cp*Fe(dppe)H]

2005

The present contribution reports experimental and computational investigations of the interaction between [Cp*Fe(dppe)H] and different proton donors (HA). The focus is on the structure of the proton transfer intermediates and on the potential energy surface of the proton transfer leading to the dihydrogen complex [Cp*Fe(dppe)(H2)]+. With p-nitrophenol (PNP) a UV/Visible study provides evidence of the formation of the ion-pair stabilized by a hydrogen bond between the nonclassical cation [Cp*Fe(dppe)(H2)]+ and the homoconjugated anion ([AHA]-). With trifluoroacetic acid (TFA), the hydrogen-bonded ion pair containing the simple conjugate base (A-) in equilibrium with the free ions is observed…

Models MolecularSpectrophotometry InfraredProtonPropanolsIronInfrared spectroscopyLigands010402 general chemistryPhotochemistrySensitivity and Specificity01 natural sciencesPolarizable continuum modelCatalysisNitrophenolschemistry.chemical_compoundHydride ligandOrganometallic CompoundsTrifluoroacetic acidMoleculeDihydrogen bondingComputer Simulation[CHIM.COOR]Chemical Sciences/Coordination chemistry10. No inequalityMolecular Structure010405 organic chemistryHydrogen bondChemistryOrganic ChemistryProton transfer mechanismHydrogen BondingGeneral Chemistry0104 chemical sciencesQuantum TheoryThermodynamicsPhysical chemistrySpectrophotometry UltravioletDFT CalculationsDihydrogen complexProtonsSolvent effects
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Tarantula Hemocyanin Shows Phenoloxidase Activity

1998

An enzyme generally catalyzes one well defined reaction with high specificity and efficiency. We report here in contrast that the copper protein hemocyanin of the tarantula Eurypelma californicum exhibits two different functions. These occur at the same active site. While hemocyanin usually is an oxygen carrier, its function can be transformed totally to monophenoloxidase and o-diphenoloxidase activity after limited proteolysis with trypsin or chymotrypsin. N-acetyldopamine (NADA) is more effectively oxidized than L-dopa or dopamine. This irreversible functional switch of tarantula hemocyanin function is limited to the two subunits b and c of its seven subunit types. A conserved phenylalani…

Models MolecularStereochemistryCopper proteinDopamineProtein subunitmedicine.medical_treatmentPhenylalanineBiochemistrySubstrate SpecificityLevodopaMetalloproteinsMetalloproteinmedicineAnimalsChymotrypsinTrypsinImmunoelectrophoresisMolecular Biologychemistry.chemical_classificationBinding SitesbiologyMonophenol MonooxygenaseActive siteSpidersHemocyaninCell BiologyTrypsinOxygenEnzymeBiochemistrychemistrySpectrophotometryHemocyaninsbiology.proteinElectrophoresis Polyacrylamide GelCoppermedicine.drugJournal of Biological Chemistry
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Molecular Architecture of Strictosidine Glucosidase: The Gateway to the Biosynthesis of the Monoterpenoid Indole Alkaloid Family[W]

2007

Abstract Strictosidine β-d-glucosidase (SG) follows strictosidine synthase (STR1) in the production of the reactive intermediate required for the formation of the large family of monoterpenoid indole alkaloids in plants. This family is composed of ∼2000 structurally diverse compounds. SG plays an important role in the plant cell by activating the glucoside strictosidine and allowing it to enter the multiple indole alkaloid pathways. Here, we report detailed three-dimensional information describing both native SG and the complex of its inactive mutant Glu207Gln with the substrate strictosidine, thus providing a structural characterization of substrate binding and identifying the amino acids …

Models MolecularStrictosidine synthaseGlutamineGlutamic AcidPlant ScienceCrystallography X-RayLigandsCatalysisProtein Structure SecondaryRauwolfiaIndole AlkaloidsSubstrate Specificitychemistry.chemical_compoundBiosynthesisHydrolaseVinca AlkaloidsResearch ArticlesBinding SitesbiologyATP synthaseIndole alkaloidActive siteCell BiologySecologanin Tryptamine AlkaloidsKineticsBiochemistrychemistryStrictosidinebiology.proteinMutagenesis Site-DirectedMutant ProteinsGlucosidasesGlucosidases
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Meprins, membrane-bound and secreted astacin metalloproteinases

2008

The astacins are a subfamily of the metzincin superfamily of metalloproteinases. The first to be characterized was the crayfish enzyme astacin. To date more than 200 members of this family have been identified in species ranging from bacteria to humans. Astacins are involved in developmental morphogenesis, matrix assembly, tissue differentiation and digestion. Family members include the procollagen C-proteinase (BMP1, bone morphogenetic protein 1), tolloid and mammalian tolloid-like, HMP (Hydra vulgaris metalloproteinase), sea urchin BP10 (blastula protein) and SPAN (Strongylocentrotus purpuratus astacin), the 'hatching' subfamily comprising alveolin, ovastacin, LCE, HCE ('low' and 'high' c…

Models MolecularSubfamilyanimal structuresProtein ConformationClinical BiochemistryMolecular Sequence DataMatrix metalloproteinaseBiochemistryBone morphogenetic protein 1ArticleSubstrate SpecificityExtracellular matrixIntestinal mucosaAnimalsHumansTissue DistributionAmino Acid SequenceIntestinal MucosaMolecular BiologyPhylogenybiologyMetalloendopeptidasesGeneral Medicinebiology.organism_classificationStrongylocentrotus purpuratusMolecular biologyCell biologyProtein Subunitsembryonic structuresMolecular MedicineMATH domainAstacin
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Comprehensive analysis of a Vibrio parahaemolyticus strain extracellular serine protease VpSP37

2015

Proteases play an important role in the field of tissue dissociation combined with regenerative medicine. During the years new sources of proteolytic enzymes have been studied including proteases from different marine organisms both eukaryotic and prokaryotic. Herein we have purified a secreted component of an isolate of Vibrio parahaemolyticus, with electrophoretic mobilities corresponding to 36 kDa, belonging to the serine proteases family. Sequencing of the N-terminus enabled the in silico identification of the whole primary structure consisting of 345 amino acid residues with a calculated molecular mass of 37.4 KDa. The purified enzyme, named VpSP37, contains a Serine protease domain be…

Models MolecularTMPRSS6Proteasesmedicine.medical_treatmentMolecular Sequence Datalcsh:MedicineBiologySettore BIO/19 - Microbiologia GeneraleSubstrate SpecificitySerine03 medical and health sciencesSettore BIO/10 - BiochimicamedicineAnimalsAmino Acid Sequencelcsh:Science030304 developmental biologySerine protease0303 health sciencesMultidisciplinaryProteaseEelsVibrio parahaemolyticuBiochemistry Genetics and Molecular Biology (all)030306 microbiologyAnimalMedicine (all)lcsh:RProteolytic enzymesEelVibrio InfectionTrypsinMolecular biology3. Good healthBiochemistryAgricultural and Biological Sciences (all)Vibrio InfectionsAmino Acid Sequence; Animals; Eels; Models Molecular; Molecular Sequence Data; Sequence Alignment; Serine Proteases; Substrate Specificity; Vibrio Infections; Vibrio parahaemolyticus; Agricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)biology.proteinlcsh:QVibrio parahaemolyticusSerine ProteaseSerine ProteasesSequence AlignmentMASP1medicine.drugResearch Article
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The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins

2006

Abstract The enzyme strictosidine synthase (STR1) from the Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. Moreover, STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ∼2000 compounds in higher plants. The crystal structures of STR1 in complex with its natural substrates tryptamine and secologanin provide structural understanding of the observed substrate preference and identify residues lining the active site surface that contact the substrates. STR1 catalyzes a Pictet-Spengler–type reaction and represents a novel…

Models MolecularTryptamineProtein FoldingStrictosidine synthaseProtein ConformationMolecular Sequence DataSequence alignmentPlant ScienceCatalysisRauwolfiaSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaCarbon-Nitrogen LyasesAmino Acid SequenceResearch ArticlesConserved SequencePlant ProteinsBinding SitesSequence Homology Amino AcidbiologyIndole alkaloidActive siteCell BiologyLyasebiology.organism_classificationTryptamineschemistryBiochemistrybiology.proteinSecologaninSequence AlignmentThe Plant Cell
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Insertion reaction of carbon dioxide into Sn-OR bond. Synthesis, structure and DFT calculations of di- and tetranuclear isopropylcarbonato tin(IV) co…

2006

The reaction of carbon dioxide with the stannane nBu2Sn(OiPr)2 and distannoxane [nBu2(iPrO)Sn]2O leads to the selective insertion into one Sn-OiPr bond generating the corresponding nBu2Sn(OiPr)(OCO2(i)Pr) and nBu2(iPrO)SnOSn(OCO2(i)Pr)nBu2 species. Both compounds are characterised by multinuclear NMR, FT-IR and single-crystal X-ray crystallography. In the solid state, they adopt a dimeric arrangement with bridging isopropoxy and terminal isopropylcarbonato ligands. The X-ray crystal structure of the dinuclear stannane shows that the Sn2O2 ring and the two Sn-OCO2C fragments are nearby coplanar. The same holds for the ladder-type tetranuclear distannoxane. The dimeric structures are also evi…

Models Molecularcrystal structureMagnetic Resonance SpectroscopySolid-statechemistry.chemical_elementCrystal structure[CHIM.INOR]Chemical Sciences/Inorganic chemistryCrystallography X-Ray010402 general chemistryPhotochemistrySensitivity and Specificity01 natural sciencesStannanedinuclear tetranuclear complexInorganic Chemistrychemistry.chemical_compoundisopropoxy stannaneInsertion reactiontinOrganotin CompoundsComputingMilieux_MISCELLANEOUSMolecular Structure010405 organic chemistryChemistrycarbon dioxideStereoisomerism[ CHIM.INOR ] Chemical Sciences/Inorganic chemistry0104 chemical sciencesCrystallographyModels ChemicalCarbon dioxideDFT optimized geometryTin
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Cloning, tissue distribution, pharmacology and three-dimensional modelling of melanocortin receptors 4 and 5 in rainbow trout suggest close evolution…

2004

The rainbow trout (Oncorhynchus mykiss) is one of the most widely used fish species in aquaculture and physiological research. In the present paper, we report the first cloning, 3D (three-dimensional) modelling, pharmacological characterization and tissue distribution of two melanocortin (MC) receptors in rainbow trout. Phylogenetic analysis indicates that these receptors are orthologues of the human MC4 and MC5 receptors. We created 3D molecular models of these rainbow trout receptors and their human counterparts. These models suggest greater divergence between the two human receptors than between their rainbow trout counterparts. The pharmacological analyses demonstrated that ACTH (adreno…

Models Molecularendocrine systemmedicine.medical_specialtyanimal structuresanimal diseasesMolecular Sequence DataAdrenocorticotropic hormoneBiologyKidneyBinding Competitivedigestive systemBiochemistryCell LineEvolution MolecularInternal medicinemedicineAnimalsHumansAmino Acid SequenceCloning MolecularBinding siteReceptorMolecular BiologyPhylogenyPharmacologyCloningBinding Sitesurogenital systemReceptors MelanocortinSequence Analysis DNACell BiologyCell biologyZincEndocrinologyReceptors CorticotropinOrgan SpecificityHypothalamusHormone receptorOncorhynchus mykissReceptor Melanocortin Type 4Rainbow troutMelanocortinSequence AlignmentResearch ArticleBiochemical Journal
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Structural and functional consequences of the replacement of proximal residues Cys172 and Cys192 in the large subunit of ribulose-1,5-bisphosphate ca…

2008

Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, we report the effect of the replacement of Cys(172) and Cys(192) by serine on the catalytic properties, thermostability and three-dimensional structure of Chlamydomonas reinhardtii Rubisco. The most striking effect of the C172S substitution was an 11% increase in the specificity factor when compared wi…

Models Molecularinorganic chemicalsOxygenaseRibulose-Bisphosphate CarboxylaseProtein subunitSpecificity factorChlamydomonas reinhardtiiCrystallography X-RayBiochemistryCatalysischemistry.chemical_compoundEnzyme StabilityAnimalsCysteineMolecular BiologyBinding SitesRibulose 15-bisphosphatebiologyfungiRuBisCOTemperaturefood and beveragesCell Biologybiology.organism_classificationLyaseMolecular biologyProtein Structure TertiaryPyruvate carboxylaseKineticsProtein SubunitsBiochemistrychemistryMutationbiology.proteinChlamydomonas reinhardtiiBiochemical Journal
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