Search results for "Catalytic Domain"

showing 10 items of 80 documents

Intramolecular electron transfer between molybdenum and iron mimicking bacterial sulphite dehydrogenase

2014

Diferrocenyl/diferrocenium substituted dioxido molybdenum(VI) complexes [Fe2MoO2] 2(Fc)/[2(FC)]²⁺ mimic the catalytic active site including the redox subunits as well as the catalytic function of bacterial sulphite oxidases.

IronSulfite DehydrogenaseMolecular Conformationchemistry.chemical_elementBiocompatible MaterialsElectronsCrystallography X-RayPhotochemistryRedoxCatalysisCatalysisElectron TransportElectron transferCoordination ComplexesCatalytic DomainPolymer chemistryMaterials ChemistrySulfite dehydrogenaseFerrous CompoundsMolybdenumBacteriabiologyMetals and AlloysActive siteGeneral ChemistryElectron transport chainSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryMolybdenumIntramolecular forceCeramics and Compositesbiology.proteinOxidation-ReductionChemical Communications
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A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase

2018

Scientific reports 8(1), 13104 (2018). doi:10.1038/s41598-018-31259-y

IsatinModels Molecular0301 basic medicineStereochemistryGlutaminelcsh:Medicine010402 general chemistry01 natural sciencesArticleAmidohydrolasesCatalysisEvolution Molecular03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsCatalytic DomainHydrolaseCatalytic triadAmino Acid SequenceRhodobacteraceaelcsh:ScienceConserved SequenceKynureninechemistry.chemical_classificationManganeseMultidisciplinarybiologyAmidohydrolaseHydrolysisIsatinlcsh:RActive site6000104 chemical sciencesZinc030104 developmental biologyEnzymechemistryBiocatalysisArylformamidaseBiocatalysisbiology.proteinQuantum Theorylcsh:QProtonsddc:600
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Inhibition Mechanism of SARS‐CoV‐2 Main Protease with Ketone‐Based Inhibitors Unveiled by Multiscale Simulations: Insights for Improved Designs**

2021

Abstract We present the results of classical and QM/MM simulations for the inhibition of SARS‐CoV‐2 3CL protease by a hydroxymethylketone inhibitor, PF‐00835231. In the noncovalent complex the carbonyl oxygen atom of the warhead is placed in the oxyanion hole formed by residues 143 to 145, while P1–P3 groups are accommodated in the active site with interactions similar to those observed for the peptide substrate. According to alchemical free energy calculations, the P1′ hydroxymethyl group also contributes to the binding free energy. Covalent inhibition of the enzyme is triggered by the proton transfer from Cys145 to His41. This step is followed by the nucleophilic attack of the Sγ atom on …

KetoneMolecular modelStereochemistrySubstituentMolecular Dynamics SimulationSARS‐CoV‐2 Inhibitors | Hot PaperCatalysisQM/MM3CL proteasechemistry.chemical_compoundCatalytic DomaininhibitorsHumansHydroxymethylProtease InhibitorsCoronavirus 3C ProteasesResearch Articleschemistry.chemical_classificationPF-00835231Binding SitesbiologySARS-CoV-2molecular modelingActive siteCOVID-19General ChemistryGeneral MedicineKetonesCOVID-19 Drug TreatmentKineticschemistryCovalent bondDrug Designbiology.proteinThermodynamicsOxyanion holeResearch ArticleAngewandte Chemie
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Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions

2019

Time-resolved x-ray scattering reveals light-induced signal transduction in insect cryptochromes.

LightProtein ConformationSpectrum AnalysisbanaanikärpänenSciAdv r-articlesfotobiologiaHydrogen BondingHydrogen-Ion ConcentrationMolecular Dynamics SimulationBiochemistryModels BiologicalCryptochromesStructure-Activity RelationshipDrosophila melanogasterCatalytic DomainAnimalsproteiinitResearch ArticlesvuorokausirytmiResearch ArticleSignal TransductionScience Advances
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Expression inactivation of SMARCA4 by microRNAs in lung tumors

2014

SMARCA4 is the catalytic subunit of the SWI/SNF chromatin-remodeling complex, which alters the interactions between DNA and histones and modifies the availability of the DNA for transcription. The latest deep sequencing of tumor genomes has reinforced the important and ubiquitous tumor suppressor role of the SWI/SNF complex in cancer. However, although SWI/SNF complex plays a key role in gene expression, the regulation of this complex itself is poorly understood. Significantly, an understanding of the regulation of SMARCA4 expression has gained in importance due to recent proposals incorporating it in therapeutic strategies that use synthetic lethal interactions between SMARCA4-MAX and SMAR…

Lung NeoplasmsDeep sequencingHistonesTranscription (biology)Catalytic DomainCell Line TumorGene expressionmicroRNAGeneticsHumansCloning MolecularMolecular BiologyTranscription factorGenetics (clinical)Cell ProliferationCell NucleusRegulation of gene expressionGeneticsbiologyDNA HelicasesHigh-Throughput Nucleotide SequencingNuclear ProteinsReproducibility of ResultsArticlesGeneral MedicineChromatin Assembly and DisassemblyPrognosisUp-RegulationCell biologyGene Expression Regulation NeoplasticMicroRNAsHistonebiology.proteinSMARCA4HeLa CellsTranscription FactorsHuman Molecular Genetics
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TBC1D24-TLDc-related epilepsy exercise-induced dystonia: rescue by antioxidants in a disease model

2019

Genetic mutations in TBC1D24 have been associated with multiple phenotypes, with epilepsy being the main clinical manifestation. The TBC1D24 protein consists of the unique association of a Tre2/Bub2/Cdc16 (TBC) domain and a TBC/lysin motif domain/catalytic (TLDc) domain. More than 50 missense and loss-of-function mutations have been described and are spread over the entire protein. Through whole genome/exome sequencing we identified compound heterozygous mutations, R360H and G501R, within the TLDc domain, in an index family with a Rolandic epilepsy exercise-induced dystonia phenotype (http://omim.org/entry/608105). A 20-year long clinical follow-up revealed that epilepsy was self-limited in…

MaleModels Molecular0301 basic medicineProtein ConformationAmino Acid Motifsalpha-TocopherolMutantCrystallography X-RayPHENOTYPECompound heterozygosityAntioxidantsAnimals Genetically ModifiedEpilepsy0302 clinical medicineCatalytic DomainDrosophila ProteinsMissense mutationoxidative stressChildTLDC DOMAINVITAMIN-EExome sequencingSequence DeletionNeuronsDystoniaGeneticsexercise-induced dystoniaTBC1D24GTPase-Activating ProteinsANNOTATIONSEpilepsy RolandicPhenotypeRecombinant ProteinsPedigree3. Good healthRolandic epilepsyDystoniaDrosophila melanogasterChild PreschoolFemaleSettore MED/26 - NeurologiaSynaptic VesiclesDrosophila melanogasterPROTEIN STABILITYLife Sciences & BiomedicineLocomotionAdolescentPhysical ExertionMutation MissenseClinical NeurologyPREDICTIONSBiology03 medical and health sciencesmedicineAnimalsHumansAmino Acid SequenceCOMPARTMENToxidative streScience & TechnologySequence Homology Amino AcidMUTATIONSNeurosciencesInfantBiological TransportDEGRADATIONmedicine.diseasebiology.organism_classificationAcetylcysteineDisease Models AnimalOxidative Stress030104 developmental biologyrab GTP-Binding ProteinsSEIZURESNeurosciences & NeurologyNeurology (clinical)Reactive Oxygen SpeciesSequence Alignment030217 neurology & neurosurgery
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Substrate promiscuity in DNA methyltransferase M.PvuII. A mechanistic insight

2012

M.PvuII is a DNA methyltransferase from the bacterium Proteus vulgaris that catalyzes methylation of cytosine at the N4 position. This enzyme also displays promiscuous activity catalyzing methylation of adenine at the N6 position. In this work we use QM/MM methods to investigate the reaction mechanism of this promiscuous activity. We found that N6 methylation in M.PvuII takes place by means of a stepwise mechanism in which deprotonation of the exocyclic amino group is followed by the methyl transfer. Deprotonation involves two residues of the active site, Ser53 and Asp96, while methylation takes place directly from the AdoMet cofactor to the target nitrogen atom. The same reaction mechanism…

MethyltransferaseDNA-Cytosine MethylasesDNA methyltransferaseM.PvuIIMolecular Dynamics SimulationBiochemistryDNA methyltransferaseMethylationSubstrate Specificitychemistry.chemical_compoundCytosineDeprotonationCatalytic DomainProteus vulgarisPhysical and Theoretical ChemistrybiologyThermus aquaticusAdenineOrganic ChemistryActive siteMethylationbiology.organism_classificationBiochemistrychemistryDNA methylationbiology.proteinCytosine
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Functional and structural insights into astacin metallopeptidases

2012

The astacins are a family of multi-domain metallopeptidases with manifold functions in metabolism. They are either secreted or membrane-anchored and are regulated by being synthesized as inactive zymogens and also by colocalizing protein inhibitors. The distinct family members consist of N-terminal signal peptides and pro-segments, zincdependent catalytic domains, further downstream extracellular domains, transmembrane anchors, and cytosolic domains. The catalytic domains of four astacins and the zymogen of one of these have been structurally characterized and shown to comprise compact ~200-residue zinc-dependent moieties divided into an N-terminal and a C-terminal sub-domain by an active-s…

MetzincinSignal peptideStereochemistryMolecular Sequence DataClinical BiochemistryTolloidMatrix metalloproteinaseBiologyBiochemistryEvolution Molecular03 medical and health sciencesEnzyme activatorBone morphogenetic proteinsZymogenAnimalsHumansProtease InhibitorsAmino Acid SequenceTyrosineMolecular BiologyPeptide sequence030304 developmental biologyEnzyme Precursors0303 health sciences030302 biochemistry & molecular biologyMetalloendopeptidasesMeprinTransmembrane protein3. Good healthEnzyme ActivationBiochemistryAstacinCatalytic domainsbchm
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The Hammerhead Ribozyme: A Long History for a Short RNA

2017

Small nucleolytic ribozymes are a family of naturally occurring RNA motifs that catalyse a self-transesterification reaction in a highly sequence-specific manner. The hammerhead ribozyme was the first reported and the most extensively studied member of this family. However, and despite intense biochemical and structural research for three decades since its discovery, the history of this model ribozyme seems to be far from finished. The hammerhead ribozyme has been regarded as a biological oddity typical of small circular RNA pathogens of plants. More recently, numerous and new variations of this ribozyme have been found to inhabit the genomes of organisms from all life kingdoms, although th…

Models Molecular0301 basic medicineHammerhead ribozymephosphodiester bondPharmaceutical ScienceReviewHistory 21st CenturyGenomeAnalytical ChemistryRNA Motifslcsh:QD241-44103 medical and health scienceslcsh:Organic chemistryCircular RNACatalytic DomainDrug DiscoveryAnimalsRNA CatalyticPhysical and Theoretical ChemistryBase PairingLigase ribozymeGeneticsRNA catalysisBase SequencebiologyHydrolysisOrganic ChemistryRibozymeRNARNA CircularSchistosoma mansoniHistory 20th CenturyPlantsbiology.organism_classification030104 developmental biologyChemistry (miscellaneous)Biocatalysisbiology.proteinNucleic Acid ConformationRNAMolecular Medicineself-cleavingMammalian CPEB3 ribozymeMolecules
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Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1

2017

Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics. These constructs were found to be potent CARM1 inhibitors and also formed stable complexes with the enzyme. High-resolution crystal structures of CARM1 in complex with these compounds co…

Models Molecular0301 basic medicineProtein-Arginine N-MethyltransferasesAdenosineMethyltransferaseCARM1ArgininePRMTCrystallography X-RayPoly(A)-Binding Protein ICofactorMice03 medical and health sciences0302 clinical medicineCatalytic DomainCoactivatorAnimalsAmino Acid Sequencetransition state mimicschemistry.chemical_classificationBinding SitesMultidisciplinarybiologycocrystal structuresActive siteProtein arginine N-methyltransferase; PRMT; CARM1; Transition state mimics; Cocrystal structuresMethylationBiological Sciencesprotein arginine N-methyltransferase030104 developmental biologyEnzymeCARM1chemistryBiochemistry030220 oncology & carcinogenesisbiology.proteinPeptidesProtein Binding
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