Search results for "Aldo-keto reductase"

showing 5 items of 5 documents

Pyrithione-based ruthenium complexes as inhibitors of aldo-keto reductase 1C enzymes and anticancer agents.

2016

Four ruthenium complexes of clinically used zinc ionophore pyrithione and its oxygen analog 2-hydroxypyridine N-oxide were prepared and evaluated as inhibitors of enzymes of the aldo–keto reductase subfamily 1C (AKR1C). A kinetic study assisted with docking simulations showed a mixed type of inhibition consisting of a fast reversible and a slow irreversible step in the case of both organometallic compounds 1A and 1B. Both compounds also showed a remarkable selectivity towards AKR1C1 and AKR1C3 which are targets for breast cancer drug design. The organoruthenium complex of ligand pyrithione as well as pyrithione itself also displayed toxicity on the hormone-dependent MCF-7 breast cancer cell…

AKR1C1StereochemistryPyridinesIonophoreAldo-Keto Reductaseschemistry.chemical_elementAntineoplastic AgentsZincReductase010402 general chemistry01 natural sciencesRutheniumInorganic ChemistryCoordination ComplexesHumansCell Proliferationchemistry.chemical_classificationAldo-keto reductase010405 organic chemistryChemistryThiones0104 chemical sciencesRutheniumEnzymeDocking (molecular)MCF-7 CellsDalton transactions (Cambridge, England : 2003)
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Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases.

1992

1. Dihydrodiol dehydrogenase activities were investigated in rabbit liver. Using a five-step purification scheme, eight isoenzymes of dihydrodiol dehydrogenase with isoelectric points of 5.55-9.3 and promoter molecular masses of 34-35 kDa were purified to apparent homogeneity and designated CF-1 to CF-6, CM-1 and CM-2. 2. CF-1 and CF-2 had near-neutral isoelectric points of 7.4 and 6.8 and molecular masses of about 125 kDa in the native state. Both enzymes readily accepted NAD+ as well as NADP+ as coenzymes, had relatively low Km values of 0.33 mM and 0.47 mM for benzene dihydrodiol and resembled previously described carbonyl reductases in their substrate specificity towards ketones and qui…

MaleOxidoreductases Acting on CH-CH Group DonorsCarbonyl ReductaseStereochemistryAldo-Keto ReductasesDehydrogenaseReductaseBiochemistryCofactorCatalysisSubstrate SpecificityAldehyde Reductasepolycyclic compoundsAnimalsTissue DistributionIsoelectric PointAldehyde ReductaseAldo-keto reductasebiologyChemistryHydroxysteroid DehydrogenasesAntibodies MonoclonalHydroxysteroid DehydrogenasesIsoenzymesMolecular WeightAlcohol OxidoreductasesBiochemistryLiverbiology.proteinElectrophoresis Polyacrylamide GelNAD+ kinaseRabbitsOxidoreductasesEuropean journal of biochemistry
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Crystal Structure of Perakine Reductase, Founding Member of a Novel Aldo-Keto Reductase (AKR) Subfamily That Undergoes Unique Conformational Changes …

2012

Perakine reductase (PR) catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. Sequence alignment shows that PR is the founder of the new AKR13D subfamily and is designated AKR13D1. The x-ray structure of methylated His(6)-PR was solved to 2.31 Å. However, the active site of PR was blocked by the connected parts of the neighbor symmetric molecule in the crystal. To break the interactions and obtain the enzyme-ligand complexes, the A213W mutant was generated. The atomic structure of His(6)-PR-A213W complex with NADPH was determined at 1.77 Å. Overal…

Models Molecularendocrine systemConformational changeProtein ConformationStereochemistryReductaseCrystallography X-Raycomplex mixturesMethylationBiochemistryProtein Structure SecondaryRauwolfiaEvolution MolecularProtein structurehemic and lymphatic diseasesheterocyclic compoundsMolecular BiologyAldo-keto reductaseCofactor bindingbiologyChemistryorganic chemicalsActive siteCell BiologyEnzyme structureAlcohol OxidoreductasesCrystallographyProtein Structure and Foldingbiology.proteinNADPH bindingSequence AlignmentNADPProtein BindingJournal of Biological Chemistry
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Cloning and expression of two novel aldo-keto reductases fromDigitalis purpurealeaves

2002

The aldo-keto reductase (AKR) superfamily comprises proteins that catalyse mainly the reduction of carbonyl groups or carbon–carbon double bonds of a wide variety of substrates including steroids. Such types of reactions have been proposed to occur in the biosynthetic pathway of the cardiac glycosides produced by Digitalis plants. Two cDNAs encoding leaf-specific AKR proteins (DpAR1 and DpAR2) were isolated from a D. purpurea cDNA library using the rat Δ4-3-ketosteroid 5β-reductase clone. Both cDNAs encode 315 amino acid proteins showing 98.4% identity. DpAR proteins present high identities (68–80%) with four Arabidopsis clones and a 67% identity with the aldose/aldehyde reductase from Medi…

chemistry.chemical_classificationAldo-keto reductasecDNA libraryReductaseBiologyBiochemistryAmino acidchemistry.chemical_compoundEnzymeBiochemistrychemistryBiosynthesisGene expressionAldehyde ReductaseEuropean Journal of Biochemistry
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Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superf…

2006

Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C222(1) and diffract to 2.0 A, with unit-…

endocrine systemStereochemistryAldo-Keto ReductasesBiophysicsAlcohol oxidoreductaseReductaseCrystallography X-Raymedicine.disease_causeBiochemistryRauwolfiachemistry.chemical_compoundBiosynthesisAldehyde ReductaseStructural BiologyRauvolfia serpentinaGeneticsmedicineEscherichia colichemistry.chemical_classificationAldo-keto reductasebiologyCondensed Matter Physicsbiology.organism_classificationAlcohol OxidoreductasesEnzymeBiochemistrychemistryCrystallization CommunicationsHeterologous expressionCrystallizationActa Crystallographica Section F Structural Biology and Crystallization Communications
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