Search results for "DASE"

showing 10 items of 1891 documents

Structures of Alkaloid Biosynthetic Glucosidases Decode Substrate Specificity

2011

Two similar enzymes with different biosynthetic function in one species have evolved to catalyze two distinct reactions. X-ray structures of both enzymes help reveal their most important differences. The Rauvolfia alkaloid biosynthetic network harbors two O-glucosidases: raucaffricine glucosidase (RG), which hydrolyses raucaffricine to an intermediate downstream in the ajmaline pathway, and strictosidine glucosidase (SG), which operates upstream. RG converts strictosidine, the substrate of SG, but SG does not accept raucaffricine. Now elucidation of crystal structures of RG, inactive RG-E186Q mutant, and its complexes with ligands dihydro-raucaffricine and secologanin reveals that it is the…

Models MolecularRauvolfiaStereochemistryIridoid GlucosidesMolecular Sequence DataMutantCrystallography X-RayBiochemistryRauwolfiaSubstrate SpecificityEvolution Molecularchemistry.chemical_compoundHydrolaseSerineAmino Acid SequenceVinca AlkaloidsPlant Proteinschemistry.chemical_classificationBinding SitesbiologyTryptophanSubstrate (chemistry)General Medicinebiology.organism_classificationKineticsEnzymechemistryBiochemistryStrictosidinebiology.proteinMolecular MedicineSecologaninGlucosidasesGlucosidasesProtein BindingACS Chemical Biology
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Sortase A Inhibitors: Recent Advances and Future Perspectives

2015

Here, we describe the most promising small synthetic organic compounds that act as potent Sortase A inhibitors and cater the potential to be developed as antivirulence drugs. Sortase A is a polypeptide of 206 amino acids, which catalyzes two sequential reactions: (i) thioesterification and (ii) transpeptidation. Sortase A is involved in the process of bacterial adhesion by anchoring LPXTG-containing proteins to lipid II. Sortase A inhibitors do not affect bacterial growth, but they restrain the virulence of pathogenic bacterial strains, thereby preventing infections caused by Staphylococcus aureus or other Gram-positive bacteria. The efficacy of the most promising inhibitors needs to be com…

Models MolecularStaphylococcus aureusRhodanineProtein ConformationVirulenceAdamantanemedicine.disease_causeStaphylococcal infectionsSettore BIO/19 - Microbiologia GeneraleBenzoatesBacterial AdhesionSortase A inhibitors review future perspectiveMicrobiologySmall Molecule LibrariesBacterial ProteinsIn vivoDrug DiscoveryNitrilesmedicineAnimalsHumansEnzyme Inhibitorschemistry.chemical_classificationLipid IIbiologyThionesStaphylococcal Infectionsbiology.organism_classificationmedicine.diseaseAminoacyltransferasesSettore CHIM/08 - Chimica FarmaceuticaAmino acidAnti-Bacterial AgentsCysteine EndopeptidasesThiazolesBiochemistrychemistryStaphylococcus aureusSortase AMolecular MedicineBacteriaCarbolines
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A synthetic method for diversification of the P1′ substituent in phosphinic dipeptides as a tool for exploration of the specificity of the S1′ bindin…

2007

Abstract A novel, general, and versatile method of diversification of the P1′ position in phosphinic pseudodipeptides, presumable inhibitors of proteolytic enzymes, was elaborated. The procedure was based on parallel derivatization of the amino group in the suitably protected phosphinate building blocks with appropriate alkyl and aryl halides. This synthetic strategy represents an original approach to phosphinic dipeptide chemistry. Its usefulness was confirmed by obtaining a series of P1′ modified phosphinic dipeptides, inhibitors of cytosolic leucine aminopeptidase, through computer-aided design basing on the structure of homophenylalanyl-phenylalanine analogue (hPheP[CH 2 ]Phe) bound in …

Models MolecularStereochemistryClinical BiochemistryLAP inhibitorsSubstituentPharmaceutical SciencePhosphinateLigandsBiochemistryAminopeptidaseLeucyl AminopeptidaseStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoveryP1′ diversificationcross-couplingMolecular BiologyalkylationBinding SitesDipeptideMolecular StructurebiologyOrganic ChemistryProteolytic enzymesActive siteHydrogen BondingStereoisomerismDipeptidesPhosphinic Acidsphosphinic pseudodipeptideschemistrybiology.proteinMolecular MedicineLeucineLead compoundBioorganic & Medicinal Chemistry
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Tyrosinase versus Catechol Oxidase: One Asparagine Makes the Difference

2015

Tyrosinases mediate the ortho-hydroxylation and two-electron oxidation of monophenols to ortho-quinones. Catechol oxidases only catalyze the oxidation of diphenols. Although it is of significant interest, the origin of the functional discrimination between tyrosinases and catechol oxidases has been unclear. Recently, it has been postulated that a glutamate and an asparagine bind and activate a conserved water molecule towards deprotonation of monophenols. Here we demonstrate for the first time that a polyphenoloxidase, which exhibits only diphenolase activity, can be transformed to a tyrosinase by mutation to introduce an asparagine. The asparagine and a conserved glutamate are necessary to…

Models MolecularStereochemistryCopper proteinTyrosinase010402 general chemistrymedicine.disease_cause01 natural sciencesCatalysischemistry.chemical_compoundDeprotonationmedicineMoleculeAsparagineCatechol oxidaseCatecholMutationbiologyMonophenol Monooxygenase010405 organic chemistryGeneral Chemistry0104 chemical scienceschemistryBiochemistrybiology.proteinAsparagineCatechol OxidaseAngewandte Chemie International Edition
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Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding…

2014

Insight into the structure and inhibition mechanism of O-β-d-glucosidases by deoxa-pyranosylamine type inhibitors is provided by X-ray analysis of complexes between raucaffricine and strictosidine glucosidases and N-(cyclohexylmethyl)-, N-(cyclohexyl)- and N-(bromobenzyl)-β-d-gluco-1,5-deoxa-pyranosylamine. All inhibitors anchored exclusively in the catalytic active site by competition with appropriate enzyme substrates. Thus facilitated prospective elucidation of the binding networks with residues located at <3.9 A distance will enable the development of potent inhibitors suitable for the production of valuable alkaloid glucosides, raucaffricine and strictosidine, by means of synthesis in …

Models MolecularStereochemistryCyclopentanesLigandsRauwolfiaStructure-Activity RelationshipSugar AlcoholsRauvolfia serpentinaDrug DiscoveryHydrolasePharmacologychemistry.chemical_classificationBinding SitesDose-Response Relationship DrugMolecular StructurebiologyAlkaloidActive siteGeneral Medicinebiology.organism_classificationLigand (biochemistry)EnzymeBiochemistrychemistryStrictosidinebiology.proteinGlucosidasesGlucosidasesJournal of Enzyme Inhibition and Medicinal 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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Synthesis, in vitro activity, and three-dimensional quantitative structure-activity relationship of novel hydrazine inhibitors of human vascular adhe…

2010

Vascular adhesion protein-1 (VAP-1) belongs to the semicarbazide-sensitive amine oxidases (SSAOs) that convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases (MAOs), but their substrate specificities are partly overlapping. VAP-1 has been proposed as a target for anti-inflammatory drug therapy because of its role in leukocyte adhesion to endothelium. Here, we describe the synthesis and in vitro activities of novel series of VAP-1 selective inhibitors. In addition, the molecular dynamics simulations performed for VAP-1 reveal that the movements of Met211, Ser496, and especially Leu469 can enlarge the ligand-binding pocket, allowing larger ligands than those s…

Models MolecularSubstrate SpecificitiesQuantitative structure–activity relationshipMolecular ConformationQuantitative Structure-Activity RelationshipMolecular Dynamics SimulationLigandsMolecular dynamicsCricetulusCricetinaeDrug DiscoveryAnimalsHumansMonoamine OxidaseBinding SitesChemistryStereoisomerismIn vitrorespiratory tract diseasesRatsMonoamine neurotransmitterHydrazinesBiochemistryDocking (molecular)Molecular MedicineAmine gas treatingAmine Oxidase (Copper-Containing)Cell Adhesion MoleculesVASCULAR ADHESION PROTEIN 1Protein BindingJournal of medicinal chemistry
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Characterization of aCandida albicansgene encoding a putative transcriptional factor required for cell wall integrity

2003

After screening a Candida albicans genome database the product of an open reading frame (ORF) (CA2880) with 49% homology to the product of Saccharomyces cerevisiae YPL133c, a putative transcriptional factor, was identified. The disruption of the C. albicans gene leads to a major sensitivity to calcofluor white and Congo red, a minor sensitivity to sodium dodecyl sulfate, a major resistance to zymolyase, and an alteration of the chemical composition of the cell wall. For these reasons we called it CaCWT1 (for C. albicans cell wall transcription factor). CaCwt1p contains a putative Zn(II) Cys(6) DNA binding domain characteristic of some transcriptional factors and a PAS domain. The CaCWT1 gen…

Models MolecularTranscription GeneticGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeSequence HomologyMicrobiologyFungal ProteinsCell WallPAS domainGene Expression Regulation FungalCandida albicansGenes RegulatorGeneticsAmino Acid SequenceColoring AgentsCandida albicansMolecular BiologyGeneTranscription factorbiologyReverse Transcriptase Polymerase Chain ReactionGlucan Endo-13-beta-D-GlucosidaseComputational BiologySodium Dodecyl SulfateDNA-binding domainbiology.organism_classificationMolecular biologyCorpus albicansDNA-Binding ProteinsMutagenesis InsertionalOpen reading frameGenome FungalGene DeletionTranscription FactorsFEMS Microbiology Letters
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Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2021

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease ofT. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression ofT. brucei rhodesiensepro-rhodesain inE. coliand determined its crystal structure. The trypanosomal pr…

Models MolecularTrypanosoma brucei rhodesiense0301 basic medicinemedicine.medical_treatmentBiochemistrycysteine proteaseproenzymefluorescence correlation spectroscopy (FCS)Trypanosoma bruceiBBB blood–brain barrierCD circular dichroismchemistry.chemical_classificationEnzyme PrecursorsbiologyChemistryhsCathL human cathepsin LHydrogen-Ion ConcentrationCysteine proteaseFCS fluorescence correlation spectroscopyCysteine EndopeptidasesBiochemistryHAT Human African TrypanosomiasisNTD neglected tropical diseaseResearch Articlecrystal structureProteasesSEC size-exclusion chromatographyPET-FCS photoinduced electron transfer–fluorescence correlation spectroscopyAfrican Sleeping SicknessTrypanosoma bruceiCleavage (embryo)03 medical and health sciencesTbCathB T. brucei cathepsin BProtein DomainsZymogenmedicineMolecular BiologyzymogenrhodesainCathepsinProtease030102 biochemistry & molecular biologyActive siteTrypanosoma brucei rhodesienseCell Biologybiology.organism_classificationmolecular dynamicsEnzyme ActivationEnzyme030104 developmental biologybiology.proteinautoinhibitionHeterologous expressionJournal of Biological Chemistry
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