Search results for "Lactonase"

showing 3 items of 3 documents

Novel Paraoxonase 2-Dependent Mechanism Mediating the Biological Effects of the Pseudomonas aeruginosa Quorum-Sensing Molecule N-(3-Oxo-Dodecanoyl)-l…

2015

ABSTRACT Pseudomonas aeruginosa produces N -(3-oxo-dodecanoyl)- l -homoserine lactone (3OC12), a crucial signaling molecule that elicits diverse biological responses in host cells thought to subvert immune defenses. The mechanism mediating many of these responses remains unknown. The intracellular lactonase paraoxonase 2 (PON2) hydrolyzes and inactivates 3OC12 and is therefore considered a component of host cells that attenuates 3OC12-mediated responses. Here, we demonstrate in cell lines and in primary human bronchial epithelial cells that 3OC12 is rapidly hydrolyzed intracellularly by PON2 to 3OC12 acid, which becomes trapped and accumulates within the cells. Subcellularly, 3OC12 acid acc…

ImmunologyBlotting WesternHomoserineMitochondrionMicrobiologyCell LineHost-Parasite Interactionschemistry.chemical_compoundLactonesLactonaseHomoserineHumansImmunoprecipitationPseudomonas InfectionsChromatography High Pressure LiquidCellular Microbiology: Pathogen-Host Cell Molecular InteractionsMicroscopy ConfocalbiologyKinaseAryldialkylphosphataseQuorum SensingQuorum sensingCytosolInfectious DiseasesBiochemistrychemistryPseudomonas aeruginosabiology.proteinPhosphorylationParasitologyRNA InterferenceIntracellular
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Translocation of Zymomonas mobilis pyruvate decarboxylase to periplasmic compartment for production of acetaldehyde outside the cytosol

2019

Abstract Acetaldehyde, a valuable commodity chemical, is a volatile inhibitory byproduct of aerobic fermentation in Zymomonas mobilis and in several other microorganisms. Attempting to improve acetaldehyde production by minimizing its contact with the cell interior and facilitating its removal from the culture, we engineered a Z. mobilis strain with acetaldehyde synthesis reaction localized in periplasm. For that, the pyruvate decarboxylase (PDC) was transferred from the cell interior to the periplasmic compartment. This was achieved by the construction of a Z. mobilis Zm6 PDC‐deficient mutant, fusion of PDC with the periplasmic signal sequence of Z. mobilis gluconolactonase, and the follow…

Recombinant Fusion Proteinslcsh:QR1-502macromolecular substancesAcetaldehydeMicrobiologyZymomonas mobilislcsh:Microbiologychemistry.chemical_compoundperiplasmZymomonasbiologypyruvate decarboxylaseZymomonas mobilisAcetaldehydeacetaldehyde productionhemic and immune systemsPeriplasmic spaceCompartment (chemistry)Original Articlesbiology.organism_classificationFusion proteinAerobiosisProtein TransportBiochemistrychemistryMetabolic EngineeringFermentationGluconolactonaseFermentationOriginal ArticlePyruvate decarboxylaseMicrobiologyOpen
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One Enzyme, Two Functions

2010

The human enzyme paraoxonase-2 (PON2) has two functions, an enzymatic lactonase activity and the reduction of intracellular oxidative stress. As a lactonase, it dominantly hydrolyzes bacterial signaling molecule 3OC12 and may contribute to the defense against pathogenic Pseudomonas aeruginosa. By its anti-oxidative effect, PON2 reduces cellular oxidative damage and influences redox signaling, which promotes cell survival. This may be appreciated but also deleterious given that high PON2 levels reduce atherosclerosis but may stabilize tumor cells. Here we addressed the unknown mechanisms and linkage of PON2 enzymatic and anti-oxidative function. We demonstrate that PON2 indirectly but specif…

chemistry.chemical_classificationReactive oxygen speciesbiologySuperoxideCytochrome cParaoxonaseCell BiologyMitochondrionBiochemistrychemistry.chemical_compoundchemistryBiochemistryCoenzyme Q – cytochrome c reductasebiology.proteinLactonaseInner mitochondrial membraneMolecular BiologyJournal of Biological Chemistry
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