Search results for "Hydro-Lyase"

showing 3 items of 13 documents

Prevention of benzo(a)pyrene-induced mutagenicity by homogeneous epoxide hydratase

1976

Benzo(a)pyrene and benz(a)anthrancene which, in contrast to the K-region epoxides benzo(a)pyrene 4,5-oxide and benz(a)anthracene 5,6-oxide, are not mutagenic to Salmonella typhimurium TA 1537 in the absence of mammalian enzyme preparations, were activated by liver microsomes from C3H mice, which had not received any pretreatment, to mutagens reverting this tester strain to histidine prototrophy. Addition of epoxide hydratase inhibitors greatly increased this mutagenicity and addition of pure epoxide hydratase reduced it by more than 95% down to the range of spontaneous mutations as observed in absence of any added mutagen. This demonstrates that the metabolic pathway responsible for the mut…

Salmonella typhimuriumCancer ResearchMutagenmedicine.disease_causechemistry.chemical_compoundEpoxide HydrataseBenz(a)AnthracenesmedicineBenzopyrenesHydro-LyasesHistidineEpoxide Hydrolaseschemistry.chemical_classificationChemistryfungifood and beveragesMolecular biologyEnzymeOncologyBiochemistryBenzo(a)pyreneHomogeneousMutationMicrosomes LiverMicrosomePyreneNADPInternational Journal of Cancer
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Transcriptional analysis of the nitrile‐degrading operon from Rhodococcus sp. ACV2 and high level production of recombinant amidase with an Escherich…

1999

Northern blotting analysis with RNA probes derived from amidase and nitrile hydratase genes from Rhodococcus sp. ACV2 revealed that both genes are part of the same operon. RNase protection mapping and sequence analysis indicated that the operon is probably under the control of a sigma 70-like promoter located upstream from the amidase gene. Plasmids were constructed with the cloned genes under tac and lac promoter control. Expression of amdA was demonstrated in Escherichia coli. In another construction, the amdA gene was inserted under the control of the bacteriophage T7 promoter. Large amounts of recombinant amidase (at least 20% of total proteins) in a soluble and active form were obtaine…

Transcription GeneticOperonMolecular Sequence Datalac operonBiologymedicine.disease_causeApplied Microbiology and BiotechnologyAmidohydrolasesAmidase03 medical and health sciencesPlasmidNitrile hydrataseBacteriophage T7OperonGene expressionEscherichia colimedicineAmidase activityRhodococcus[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyEscherichia coliHydro-LyasesComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesBase Sequence030306 microbiologyGeneral MedicineMolecular biologyRecombinant Proteins[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryGenes BacterialBiotechnologyJournal of Applied Microbiology
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Purification of rat liver epoxide hydratase to apparent homogeneity.

1975

Epoxide hydratase (EC 4.2.1.63) is a microsomal enzyme which catalyses the conversion of epoxides to trans-dihydrodiols. Epoxides, produced by the action of microsomal monooxygenases (EC 1.14.1.1) from aromatic and olefinic compounds, are thought to be responsible for many of the harinful effects of polycyclic hydrocarbons and related compounds. Thus epoxide hydratase, together with glutathione 9transferases, (EC 2.5.1.18) may play an important role in the removal of carcinogenic and cytotoxic metabolites (for reviews see [l-3]). It has been reported [4,5] that dihydrodiols formed from some polycyclic hydrocarbons (benz(a)anthracene and benzo(a)pyrene) are reactivated by the microsomal mono…

chemistry.chemical_classificationEpoxide HydrolasesMaleAnthraceneBiophysicsCell BiologyGlutathioneMonooxygenaseBiochemistryRatsMolecular Weightchemistry.chemical_compoundEnzymechemistryBiochemistryStructural BiologyGeneticsMicrosomeMicrosomes LiverPyreneAnimalsPolycyclic HydrocarbonsMolecular BiologyCarcinogenHydro-LyasesFEBS letters
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