0000000000046875

AUTHOR

Juergen Koepke

showing 11 related works from this author

Crystallization of late-stage MORB under varying water activities and redox conditions: Implications for the formation of highly evolved lavas and ox…

2018

Abstract In order to understand late magmatic processes that occur in the deep oceanic crust, we performed a phase-equilibria study in a representative late-stage system at a pressure of 200 MPa with a special focus on the role of water and oxygen fugacity. The starting composition for the experiments was evaluated based on a statistical approach using evolved fresh MORB glasses from the database PETDB highest in FeO and TiO2 (in average 17.92 wt% and 3.73 wt%, respectively), assumed to represent frozen liquids erupted at the seafloor generated by extensive differentiation of MORB. We conducted crystallization experiments in a range of temperatures from 850 to 1050 °C with water activities …

Olivine010504 meteorology & atmospheric sciencesGabbroGeochemistryGeologyLiquidusengineering.material010502 geochemistry & geophysics01 natural sciencesSeafloor spreadingGeochemistry and PetrologyMineral redox bufferOceanic crustengineeringPlagioclaseAmphiboleGeology0105 earth and related environmental sciencesLithos
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Thin crust and exposed mantle control sulfide differentiation in slow-spreading ridge magmas

2017

chemistry.chemical_classification010504 meteorology & atmospheric sciencesSulfidechemistryOceanic crustGeochemistryGeologyCrust010502 geochemistry & geophysics01 natural sciencesGeologyMantle (geology)0105 earth and related environmental sciencesGeology
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Sulfide enrichment at an oceanic crust-mantle transition zone: Kane Megamullion (23°N, MAR)

2018

Abstract The Kane Megamullion oceanic core complex located along the Mid-Atlantic Ridge (23°30′N, 45°20′W) exposes lower crust and upper mantle directly on the ocean floor. We studied chalcophile elements and sulfides in the ultramafic and mafic rocks of the crust-mantle transition and the mantle underneath. We determined mineralogical and elemental composition and the Cu isotope composition of the respective sulfides along with the mineralogical and elemental composition of the respective serpentines. The rocks of the crust-mantle transition zone (i.e., plagioclase harzburgite, peridotite-gabbro contacts, and dunite) overlaid by troctolites are by one order of magnitude enriched in several…

010504 meteorology & atmospheric sciencesGeochemistryCrustengineering.material010502 geochemistry & geophysics01 natural sciencesMantle (geology)Oceanic core complexGeochemistry and PetrologyUltramafic rockOceanic crustTransition zoneengineeringPlagioclasePyrrhotiteGeology0105 earth and related environmental sciencesGeochimica et Cosmochimica Acta
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Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to …

2005

Abstract Strictosidine β- d -glucosidase, a plant enzyme initiating biosynthetic pathways to about 2000 monoterpenoid indole alkaloids with an extremely large number of various carbon skeletons, has been functionally expressed in Escherichia coli and purified to homogeneity in mg scale. Crystals suitable for X-ray analysis were found by robot-mediated screening. Using the hanging-drop technique, optimum conditions were 0.3 M ammonium sulfate, 0.1 M sodium acetate, pH 4.6 and PEG 4000 (10%) as precipitant buffer. The crystals of strictosidine glucosidase belong to the space group P 42 1 2 with unit cell dimensions of a =157.63, c =103.59 A and diffract X-rays to 2.48-A resolution.

Ammonium sulfateCatharanthusStereochemistryBiophysicsCrystallography X-Raymedicine.disease_causeBiochemistryIndole AlkaloidsAnalytical Chemistrychemistry.chemical_compoundRauvolfia serpentinaPEG ratioEscherichia colimedicineCloning MolecularMolecular BiologyEscherichia colichemistry.chemical_classificationbiologyIndole alkaloidbiology.organism_classificationEnzymeBiochemistrychemistryStrictosidineCrystallizationSodium acetateGlucosidasesBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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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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Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina.

2005

Vinorine synthase (VS) is a central enzyme of the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure with significant sequence homology with VS is known. Crystals of VS and selenomethionyl-labelled VS from the medicinal plant Rauvolfia serpentina have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. VS crystals diffract to 2.8 Å and belong to space group P212121, with unit-cell parameters a = 82.3, b = 89.6, c = 136.2 Å. The selenomethionyl VS crystal was nearly isomorphous with the VS crystal.

StereochemistryCrystallography X-RayRauwolfialaw.inventionIndole AlkaloidsLigaseschemistry.chemical_compoundBiosynthesisStructural BiologylawRauvolfia serpentinamedicineCrystallizationSelenomethioninePlant ProteinsPEG 400chemistry.chemical_classificationATP synthasebiologyGeneral Medicinebiology.organism_classificationAjmalineEnzymechemistryAcyltransferasesbiology.proteinCrystallizationmedicine.drugActa crystallographica. Section D, Biological crystallography
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Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family.

2004

Strictosidine synthase is a central enzyme involved in the biosynthesis of almost all plant monoterpenoid indole alkaloids. Strictosidine synthase from Rauvolfia serpentina was heterologously expressed in Escherichia coli. Crystals of the purified recombinant enzyme have been obtained by the hanging-drop technique at 303 K with potassium sodium tartrate tetrahydrate as precipitant. The crystals belong to the space group R3 with cell dimensions of a=b=150.3 A and c=122.4 A. Under cryoconditions (120 K), the crystals diffract to about 2.95 A.

RauvolfiaStrictosidine synthaseDNA PlantStereochemistryBiophysicsmedicine.disease_causeCrystallography X-RayBiochemistryRauwolfiaAnalytical Chemistrylaw.inventionchemistry.chemical_compoundBiosynthesislawRauvolfia serpentinaCarbon-Nitrogen LyasesmedicineEscherichia coliCrystallizationMolecular BiologyEscherichia colichemistry.chemical_classificationTetrahydratebiologyBase Sequencebiology.organism_classificationRecombinant ProteinsEnzymechemistryBiochemistrybiology.proteinBiochimica et biophysica acta
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Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily

2004

Abstract Crystals of vinorine synthase (VS) from medicinal plant Rauvolfia serpentina expressed in Escherichia coli have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. The enzyme is involved in the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure of a member of this enzyme family is known. The crystals belong to the space group P 2 1 2 1 2 1 with cell dimensions of a =82.3 A, b =89.6 A and c =136.2 A. Under cryoconditions (120 K), a complete data set up to 2.8 A was collected at a synchrotron source.

RauvolfiaIndolesStereochemistryBiophysicsCrystallography X-RayBiochemistryRauwolfiaAnalytical Chemistrychemistry.chemical_compoundAlkaloidsBiosynthesisRauvolfia serpentinamedicineMolecular Biologychemistry.chemical_classificationATP synthasebiologybiology.organism_classificationEnzymesAjmalineEnzymechemistryBiochemistryAcyltransferasesAcetyltransferasebiology.proteinCrystallizationmedicine.drugBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine

2005

Strictosidine synthase (STR1) is a central enzyme that participates in the biosynthesis of almost all plant monoterpenoid indole alkaloids. After heterologous expression in Escherichia coli, crystals of STR1 and its substrate complex with tryptamine were obtained by the hanging-drop technique at 302–304 K with potassium sodium tartrate tetrahydrate as precipitant. All crystals belong to space group R3. The native STR1 crystals diffract to 2.95 Å and have unit-cell parameters a = b = 150.3, c = 122.4 Å. The tryptamine complex crystals diffract to 2.38 Å, with unit-cell parameters a = b = 147.3, c = 122.3 Å.

TryptamineStrictosidine synthaseTetrahydratebiologyStereochemistryPotassium sodium tartrateSubstrate (chemistry)General MedicineRauwolfiaTryptamineslaw.inventionchemistry.chemical_compoundchemistryBiosynthesisStructural BiologylawCarbon-Nitrogen Lyasesbiology.proteinHeterologous expressionCrystallizationCrystallizationPlant ProteinsActa Crystallographica Section D Biological Crystallography
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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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Crystal structure of vinorine synthase, the first representative of the BAHD superfamily.

2005

Vinorine synthase is an acetyltransferase that occupies a central role in the biosynthesis of the antiarrhythmic monoterpenoid indole alkaloid ajmaline in the plant Rauvolfia. Vinorine synthase belongs to the benzylalcohol acetyl-, anthocyanin-O-hydroxy-cinnamoyl-, anthranilate-N-hydroxy-cinnamoyl/benzoyl-, deacetylvindoline acetyltransferase (BAHD) enzyme superfamily, members of which are involved in the biosynthesis of several important drugs, such as morphine, Taxol, or vindoline, a precursor of the anti-cancer drugs vincaleucoblastine and vincristine. The x-ray structure of vinorine synthase is described at 2.6-angstrom resolution. Despite low sequence identity, the two-domain structure…

Models MolecularStereochemistryMolecular Sequence DataSequence alignmentBiologyCrystallography X-RayBiochemistryIndole AlkaloidsProtein structureAcetyltransferasesTransferaseCoenzyme AAmino Acid SequenceDihydrolipoyl transacetylaseMolecular BiologyPlant ProteinsAjmalineATP synthaseMolecular StructureActive siteCell BiologyProtein Structure TertiaryBiochemistryAcyltransferasesAcetyltransferasebiology.proteinAnti-Arrhythmia AgentsSequence AlignmentThe Journal of biological chemistry
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