Search results for "NONRIBOSOMAL PEPTIDE"

showing 8 items of 8 documents

The swinholide biosynthesis gene cluster from a terrestrial cyanobacterium, Nostoc sp. strain UHCC 0450

2017

ABSTRACT Swinholides are 42-carbon ring polyketides with a 2-fold axis of symmetry. They are potent cytotoxins that disrupt the actin cytoskeleton. Swinholides were discovered from the marine sponge Theonella sp. and were long suspected to be produced by symbiotic bacteria. Misakinolide, a structural variant of swinholide, was recently demonstrated to be the product of a symbiotic heterotrophic proteobacterium. Here, we report the production of swinholide A by an axenic strain of the terrestrial cyanobacterium Nostoc sp. strain UHCC 0450. We located the 85-kb trans -AT polyketide synthase (PKS) swinholide biosynthesis gene cluster from a draft genome of Nostoc sp. UHCC 0450. The swinholide …

0301 basic medicinemarine environmentterrestrial environmentDIVERSITYcyanobacteria01 natural sciencesApplied Microbiology and BiotechnologyBiochemistryTrans-AT PKSMARINE CYANOBACTERIAGene clusterEnvironmental MicrobiologyskeletonSPONGE THEONELLA-SWINHOEISpotlightAxenicNostocgene transfertoxinSwinholide1183 Plant biology microbiology virologyPhylogenychemistry.chemical_classificationEcologybiologyAnabaena sp.ChemistryAnabaenaHorizontal gene transferKetonesbacteriumenzyme activityphylogeneticsINSIGHTSBiochemistryMultigene Familyhorizontal gene transferscytophycinScandium compoundspolyketidesBiotechnologyNostoctrans-AT PKSScytophycinNONRIBOSOMAL PEPTIDEBiosynthesisCyanobacteriaswinholideCYTOTOXIC DIMERIC MACROLIDES03 medical and health sciencesPolyketideBacterial ProteinsNonribosomal peptidecyanobacteriumPolyketide synthaseProteobacteriaCONGENERSCandidatus Entotheonellabovine spongiform encephalopathygeneNostoc sp.Bacteriacatalysis010405 organic chemistryProteinsSequence Analysis DNAbiology.organism_classificationActin cytoskeletonAnabaenaEVOLUTION"Candidatus Entotheonella"0104 chemical sciencesenzymeNATURAL-PRODUCT DISCOVERY030104 developmental biologyGenesPolyketidesbiology.proteingene expressionbacteria“Candidatus Entotheonella”Theonella sp.Marine ToxinsPolyketide SynthasesFood Sciencecatalyst
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Characterization of sulfhydryl oxidase from Aspergillus tubingensis

2017

Background Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. Results The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initia…

0301 basic medicineentsyymitBOVINE-MILKThioredoxin reductaselcsh:Animal biochemistryBiochemistrySubstrate Specificitychemistry.chemical_compoundNonribosomal peptide synthesisEnzyme Stabilitylcsh:QD415-436DisulfidesDISULFIDE BONDSPeptide Synthaseschemistry.chemical_classificationbiologyGliotoxinChemistrynonribosomal peptide synthesisHydrogen-Ion ConcentrationGlutathioneFAMILYSOXSglutathione oxidationhomesienetAspergillusBiochemistrySENSITIVITYsecreted sulfhydryl oxidaseOxidoreductasesResearch ArticleDithiol oxidaseCofactorlcsh:Biochemistry03 medical and health sciencesNonribosomal peptideNATURAL-PRODUCTSoksidoreduktaasitBIOSYNTHESISlcsh:QP501-801Molecular Biologysecondary metabolismPURIFICATIONIDENTIFICATION030102 biochemistry & molecular biologyCXXC-MOTIFGlutathioneNIGERluonnonaineet030104 developmental biologyEnzymedithiol oxidasebiology.protein1182 Biochemistry cell and molecular biologyAspergillus tubingensisSecreted sulfhydryl oxidaseSecondary metabolismGlutathione oxidationCysteineBMC Biochemistry
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Antifungal activity improved by coproduction of cyclodextrins and anabaenolysins in Cyanobacteria

2015

Department of Chemistry, Nanoscience Center, University of Jyväskylä, FI-40014, Jyväskylä, Finland Cyclodextrins are cyclic oligosaccharides widely used in the pharmaceutical industry to improve drug delivery and to increase the solubility of hydrophobic compounds. Anabaenolysins are lipopeptides produced by cyanobacteria with potent lytic activity in cholesterolcontaining membranes. Here, we identified the 23- To 24-kb gene clusters responsible for the production of the lipopeptide anabaenolysin. The hybrid nonribosomal peptide synthetase and polyketide synthase biosynthetic gene cluster is encoded in the genomes of three anabaenolysin-producing strains of Anabaena.We detected previously u…

hydroxyamino fatty acidAntifungal Agentsnatural productsMolecular Sequence DataBiologyCyanobacteriata3111chemistry.chemical_compoundBacterial ProteinsNonribosomal peptidePolyketide synthaseGene clusterSolubilityCandida albicanschemistry.chemical_classificationCyclodextrinsMultidisciplinarybioactive compoundsAnabaenaNRPSta1182LipopeptideBiological SciencesPKSbiology.organism_classificationchemistryBiochemistryGenes Bacterialbiology.proteinPhotosynthetic bacteriaProceedings of the National Academy of Sciences of the United States of America
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Direct pathway cloning and expression of the radiosumin biosynthetic gene cluster

2023

Radiosumins are a structurally diverse family of low molecular weight natural products that are produced by cyanobacteria and exhibit potent serine protease inhibition. Members of this family are dipeptides characterized by the presence of two similar non-proteinogenic amino acids. Here we used a comparative bioinformatic analysis to identify radiosumin biosynthetic gene clusters from the genomes of 13 filamentous cyanobacteria. We used direct pathway cloning to capture and express the entire 16.8 kb radiosumin biosynthetic gene cluster from Dolichospermum planctonicum UHCC 0167 in Escherichia coli. Bioinformatic analysis demonstrates that radiosumins represent a new group of chorismate-der…

11832 Microbiology and virologyIdentificationDiversityOrganic ChemistryBacillus-subtilis116 Chemical sciencesFresh-waterDNAProtease inhibitorsCyanobacteriaBiochemistryQualityNonribosomal peptidegeneettinen monimuotoisuusNatural-productsTrypsin-inhibitorPhysical and Theoretical Chemistrysyanobakteerit
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The Biosynthesis of Rare Homo-Amino Acid Containing Variants of Microcystin by a Benthic Cyanobacterium

2019

Microcystins are a family of chemically diverse hepatotoxins produced by distantly related cyanobacteria and are potent inhibitors of eukaryotic protein phosphatases 1 and 2A. Here we provide evidence for the biosynthesis of rare variants of microcystin that contain a selection of homo-amino acids by the benthic cyanobacterium Phormidium sp. LP904c. This strain produces at least 16 microcystin chemical variants many of which contain homophenylalanine or homotyrosine. We retrieved the complete 54.2 kb microcystin (mcy) gene cluster from a draft genome assembly. Analysis of the substrate specificity of McyB1 and McyC adenylation domain binding pockets revealed divergent substrate specificity …

CyanobacteriamassaspektrometriaMicrocystinstoksiinitPharmaceutical ScienceMicrocystinPlanktothrixcyanobacteriaArticlebiosynteesi03 medical and health scienceschemistry.chemical_compoundBiosynthesisBacterial ProteinsDrug DiscoveryGene clusterpolycyclic compoundspolyketide synthase (PKS)Protein Interaction Domains and MotifsAmino Acid SequenceAmino AcidssyanobakteeritPharmacology Toxicology and Pharmaceutics (miscellaneous)Genelcsh:QH301-705.5Phylogeny030304 developmental biologymass spectrometrychemistry.chemical_classification0303 health sciencesbiology030302 biochemistry & molecular biologyta1182Sequence Analysis DNAbiology.organism_classificationAmino acidEnzymechemistryBiochemistrylcsh:Biology (General)adenylation domainGenes BacterialMultigene Familynonribosomal peptide synthetase (NRPS)hepatotoxinMarine Drugs
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Discovery of a Pederin Family Compound in a Nonsymbiotic Bloom-Forming Cyanobacterium

2018

The pederin family includes a number of bioactive compounds isolated from symbiotic organisms of diverse evolutionary origin. Pederin is linked to beetle-induced dermatitis in humans, and pederin family members possess potent antitumor activity caused by selective inhibition of the eukaryotic ribosome. Their biosynthesis is accomplished by a polyketide/nonribosomal peptide synthetase machinery employing an unusual trans-acyltransferase mechanism. Here, we report a novel pederin type compound, cusperin, from the free-living cyanobacterium Cuspidothrix issatschenkoi (earlier Aphanizomenon). The chemical structure of cusperin is similar to that of nosperin recently isolated from the lichen cya…

0301 basic medicineNostocSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyGENE-CLUSTERPAEDERUSpederinsPederinCyanobacteriaBiochemistry03 medical and health scienceschemistry.chemical_compoundPolyketideBiosynthesisNonribosomal peptideTandem Mass SpectrometryCHEMISTRYGene clusterBACTERIAL SYMBIONTBIOSYNTHESISPeptide SynthasesSymbiosissyanobakteeritta116chemistry.chemical_classificationbioactive compoundsbiologybioaktiiviset yhdisteetta1182General Medicinebiology.organism_classificationluonnonaineetnaturally occurring substancesamidesPOLYKETIDE SYNTHASES030104 developmental biologychemistryBiochemistryGenes BacterialMultigene FamilyPolyketidesamiditCyanobiontMolecular Medicine1182 Biochemistry cell and molecular biologyEukaryotic Ribosome
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Alternative Biosynthetic Starter Units Enhance the Structural Diversity of Cyanobacterial Lipopeptides

2019

Puwainaphycins (PUWs) and minutissamides (MINs) are structurally analogous cyclic lipopeptides possessing cytotoxic activity. Both types of compound exhibit high structural variability, particularly in the fatty acid (FA) moiety. Although a biosynthetic gene cluster responsible for synthesis of several PUW variants has been proposed in a cyanobacterial strain, the genetic background for MINs remains unexplored. Herein, we report PUW/MIN biosynthetic gene clusters and structural variants from six cyanobacterial strains. Comparison of biosynthetic gene clusters indicates a common origin of the PUW/MIN hybrid nonribosomal peptide synthetase and polyketide synthase. Surprisingly, the biosynthet…

Antifungal AgentsGenetics and Molecular BiologyCyanobacteria01 natural sciencesApplied Microbiology and BiotechnologycyanobacteriaPeptides Cyclicbiosynteesi03 medical and health scienceschemistry.chemical_compoundLipopeptidesBiosynthesisAnti-Infective AgentsBacterial ProteinsNonribosomal peptidePolyketide synthaseGene clusterPeptide SynthasessyanobakteeritGene030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciencesNatural productEcologybiology010405 organic chemistryLipopeptideAnabaenaYeast0104 chemical scienceschemistryBiochemistrypeptiditGenes BacterialMultigene Familybiology.proteinpeptidesbiosynthesisPolyketide SynthasesFood ScienceBiotechnology
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Structure, Biosynthesis, and Bioactivity of Photoditritide from Photorhabdus temperata Meg1

2019

A new cyclic peptide photoditritide (1), containing two rare amino acid d-homoarginine residues, was isolated from Photorhabdus temperata Meg1 after the nonribosomal peptide synthetase encoding gene pdtS was activated via promoter exchange. The structure of 1 was elucidated by HR-MS and NMR experiments. The absolute configurations of amino acids were determined according to the advanced Marfey's method after hydrolysis of 1. Bioactivity testing of 1 revealed potent antimicrobial activity against Micrococcus luteus with an MIC value of 3.0 μM and weak antiprotozoal activity against Trypanosoma brucei rhodesiense with an IC50 value of 13 μM. Additionally, the biosynthetic pathway of 1 was als…

medicine.drug_classPharmaceutical Science01 natural sciencesAnalytical Chemistrychemistry.chemical_compoundHydrolysisBiosynthesisNonribosomal peptideDrug DiscoverymedicinePharmacologychemistry.chemical_classificationbiology010405 organic chemistryOrganic ChemistryTrypanosoma brucei rhodesiensebiology.organism_classificationCyclic peptide0104 chemical sciencesAmino acid010404 medicinal & biomolecular chemistryComplementary and alternative medicinechemistryBiochemistryAntiprotozoalMolecular MedicineMicrococcus luteusJournal of Natural Products
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