Search results for "Lactococcus lactis subsp cremoris"

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Cyclopropanation of Membrane Unsaturated Fatty Acids Is Not Essential to the Acid Stress Response of Lactococcus lactis subsp. cremoris

2011

ABSTRACT Cyclopropane fatty acids (CFAs) are synthetized in situ by the transfer of a methylene group from S -adenosyl- l -methionine to a double bond of unsaturated fatty acid chains of membrane phospholipids. This conversion, catalyzed by the Cfa synthase enzyme, occurs in many bacteria and is recognized to play a key role in the adaptation of bacteria in response to a drastic perturbation of the environment. The role of CFAs in the acid tolerance response was investigated in the lactic acid bacterium Lactococcus lactis MG1363. A mutant of the cfa gene was constructed by allelic exchange. The cfa gene encoding the Cfa synthase was cloned and introduced into the mutant to obtain the comple…

CyclopropanesPhysiologyMembrane lipidsMutantApplied Microbiology and BiotechnologyGas Chromatography-Mass SpectrometryMembrane LipidsStress PhysiologicalMembrane fluidityViability assayPhospholipidsUnsaturated fatty acidMicrobial ViabilityEcologybiologyLactococcus lactis subsp cremorisFatty AcidsGenetic Complementation TestLactococcus lactisMethyltransferasesbiology.organism_classificationLactococcus lactisBiochemistryFatty Acids UnsaturatedMutant ProteinsAcidsBacteriaFood ScienceBiotechnologyApplied and Environmental Microbiology
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Cyclopropane Fatty Acid Synthase from Oenococcus oeni: Expression in Lactococcus lactis subsp. Cremoris and Biochemical Characterization

2015

Bacterial cyclopropane fatty acid synthases (CFA synthases) catalyze the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the double bond of a lipid chain, thereby forming a cyclopropane ring. CFAs contribute to resistance to acidity, dryness, and osmotic imbalance in many bacteria. This work describes the first biochemical characterization of a lactic acid bacterium CFA synthase. We have overexpressed Oenococcus oeni CFA synthase in E. coli in order to purify the enzyme. The optimum cyclopropanation activity was obtained at pH 5.6 and 35.8 °C. The high K(m) (AdoMet) value obtained (2.26 mM) demonstrates the low affinity of O. oeni enzyme toward the L. lactis subsp. cremo…

[SDV]Life Sciences [q-bio]medicine.disease_causeBiochemistryMicrobiologySubstrate SpecificityMicrobiology03 medical and health scienceschemistry.chemical_compoundEscherichia coliGeneticsmedicineCyclopropane fatty acidMolecular BiologyEscherichia coliOenococcusPhospholipidsComputingMilieux_MISCELLANEOUS030304 developmental biologyOenococcus oenichemistry.chemical_classification0303 health sciences[ SDV ] Life Sciences [q-bio]biologyATP synthase030306 microbiologyLactococcus lactis subsp cremorisFatty AcidsLactococcus lactisGene Expression Regulation BacterialMethyltransferasesGeneral Medicinebiology.organism_classification[SDV] Life Sciences [q-bio]Lactococcus lactisEnzymechemistryBiochemistryMutationbiology.proteinOenococcus
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