Search results for "Trehalase activity"

showing 10 items of 11 documents

Yeast trehalases: Two enzymes, one catalytic mission

2016

Abstract Background Trehalose is a non-reducing disaccharide highly conserved throughout evolution. In yeasts, trehalose hydrolysis is confined to the enzyme trehalase, an α-glucosidase specific for trehalose as sole substrate. Two kinds of trehalase activity exist in yeasts: neutral and acid enzymes. Scope of the review This review makes a comparative survey of the main biochemical and genetic parameters, regulatory systems, tridimensional structure and catalytic mechanism of the two yeast trehalases. Major conclusions The yeast neutral and acid trehalases display sharp differences in biochemical features (optimum pH, Mr or amino acid sequence) physiological roles, subcellular location (cy…

0301 basic medicineCytoplasm030106 microbiologyBiophysicsCatabolite repressionTrehalase activitySaccharomyces cerevisiaeBiologyBiochemistryCatalysis03 medical and health scienceschemistry.chemical_compoundCell WallTrehalaseTrehalaseMolecular BiologyPeptide sequencechemistry.chemical_classificationHydrolysisTrehaloseTrehaloseYeastCytosol030104 developmental biologyEnzymechemistryBiochemistryBiochimica et Biophysica Acta (BBA) - General Subjects
researchProduct

In Candida parapsilosis the ATC1 Gene Encodes for an Acid Trehalase Involved in Trehalose Hydrolysis, Stress Resistance and Virulence

2014

An ORF named CPAR2-208980 on contig 005809 was identified by screening a Candida parapsilosis genome data base. Its 67% identity with the acid trehalase sequence from C. albicans (ATC1) led us to designate it CpATC1. Homozygous mutants that lack acid trehalase activity were constructed by gene disruption at the two CpATC1 chromosomal alleles. Phenotypic characterization showed that atc1Δ null cells were unable to grow on exogenous trehalose as carbon source, and also displayed higher resistance to environmental challenges, such as saline exposure (1.2 M NaCl), heat shock (42°C) and both mild and severe oxidative stress (5 and 50 mM H2O2). Significant amounts of intracellular trehalose were …

Fungal PhysiologyMutantGlycobiologyTrehalase activitylcsh:MedicineMicrobiologiaPathogenesisPathology and Laboratory MedicineCandida parapsilosisBiochemistrychemistry.chemical_compoundNucleic AcidsMicrobial PhysiologyMedicine and Health SciencesTrehalaseTrehalaselcsh:ScienceFungal BiochemistryCandida albicansCandidaMultidisciplinaryVirulencebiologyOrganic CompoundsSalt ToleranceCatalaseEnzymesChemistryPhysical SciencesResearch ArticleGenes FungalMolecular Sequence DataCarbohydratesMycologyMicrobiologyMicrobiologyFungal ProteinsAmino Acid SequenceHeat shockGlycoproteinslcsh:ROrganismsFungiChemical CompoundsWild typeTrehaloseBiology and Life Sciencesbiology.organism_classificationTrehaloseYeastOxidative StressMetabolismchemistryProteolysisEnzymologylcsh:QHeat-Shock ResponsePLoS ONE
researchProduct

Homozygous deletion of ATC1 and NTC1 genes in Candida parapsilosis abolishes trehalase activity and affects cell growth, sugar metabolism, stress res…

2015

A double homozygous atc1Δ/atc1Δ/ntc1Δ/ntc1Δ mutant (atc1Δ/ntc1Δ KO) was constructed in the pathogen opportunistic yeast Candida parapsilosis by disruption of the two chromosomal alleles coding for NTC1 gene (encoding a neutral trehalase) in a Cpatc1Δ/atc1Δ background (atc1Δ KO strain, deficient in acid trehalase). The Cpatc1Δ/ntc1Δ KO mutant failed to counteract the inability of Cpatc1Δ cells to metabolize exogenous trehalose and showed a similar growth pattern on several monosaccharides and disaccharides. However, upon prolonged incubation in either rich medium (YPD) or nutrient-starved medium the viability of Cpatc1Δ cells exhibited a sensitive phenotype, which was augmented by further Cp…

Fungal proteinVirulencebiologyMutantTrehalase activityTrehaloseCandida parapsilosisbiology.organism_classificationMicrobiologyTrehaloseYeastMicrobiologyFungal ProteinsOxidative Stresschemistry.chemical_compoundchemistryStress PhysiologicalBiofilmsGeneticsCarbohydrate MetabolismTrehalaseTrehalaseGene knockoutCandidaSequence DeletionFungal Genetics and Biology
researchProduct

Long-term effects of the trehalase inhibitor trehazolin on trehalase activity in locust flight muscle.

2010

SUMMARY Trehalase (EC 3.2.1.28) hydrolyzes the main haemolymph sugar of insects, trehalose, into the essential cellular substrate glucose. Trehalase in locust flight muscle is bound to membranes that appear in the microsomal fraction upon tissue fractionation, but the exact location in vivo has remained elusive. Trehalase has been proposed to be regulated by a novel type of activity control that is based on the reversible transformation of a latent (inactive) form into an overt (active) form. Most trehalase activity from saline-injected controls was membrane-bound (95%) and comprised an overt form (∼25%) and a latent form (75%). Latent trehalase could be assayed only after the integrity of …

MalePhysiologyTrehalase activityLocusta migratoriaAquatic ScienceDisaccharideschemistry.chemical_compoundIn vivoHemolymphExtracellularAnimalsTrehalaseTrehalaseEnzyme InhibitorsMuscle SkeletalMolecular BiologyEcology Evolution Behavior and SystematicsbiologyBehavior Animalbiology.organism_classificationTrehalosechemistryBiochemistryInsect ScienceFlight AnimalMicrosomeAnimal Science and ZoologyLocustThe Journal of experimental biology
researchProduct

Fate and effects of the trehalase inhibitor trehazolin in the migratory locust (Locusta migratoria).

2009

Abstract Trehalose is the main haemolymph sugar in many insect species. To be utilized trehalose must be hydrolysed into its glucose units by trehalase (EC 3.2.1.28). Inhibitors of trehalase have attracted interest as possible pesticides and tools for studying the regulation of trehalose metabolism in insects. To make full use of these inhibitors requires knowledge of their fate and effects in vivo. To this end we have measured trehazolin in locusts using a method based on the specific inhibition of a trehalase preparation. After injection of 20 μg, trehazolin decreased in haemolymph with a half-life of 2.6 days and after 10 days almost 95% had disappeared. Trehazolin did not reach the intr…

Maleanimal structuresPhysiologyTrehalase activityLocusta migratoriaDisaccharideschemistry.chemical_compoundEatingFecesHemolymphHemolymphAnimalsTrehalaseTrehalasechemistry.chemical_classificationbiologyMusclesMetabolismMigratory locustbiology.organism_classificationTrehaloseKineticsEnzymechemistryBiochemistryInsect ScienceLocustHalf-LifeJournal of insect physiology
researchProduct

The regulation of trehalose metabolism in insects.

1996

Trehalose is a non-reducing disaccharide comprising two glucose molecules. It is present in high concentration as the main haemolymph (blood) sugar in insects. The synthesis of trehalose in the fat body (an organ analogous in function to a combination of liver and adipose tissue in vertebrates) is stimulated by neuropeptides (hypertrehalosaemic hormones), released from the corpora cardiaca, a neurohaemal organ associated with the brain. The peptides cause a decrease in the content of fructose 2,6-bisphosphate in fat body cells. Fructose 2,6-bisphosphate, acting synergistically with AMP, is a potent activator of the glycolytic enzyme 6-phosphofructokinase-1 and a strong inhibitor of the gluc…

PharmacologyInsectaMolecular Sequence DataTrehalase activityAdipose tissueTrehaloseFructoseCell BiologyBiologyTrehaloseCellular and Molecular Neurosciencechemistry.chemical_compoundFructose 26-bisphosphatechemistryBiochemistryCarbohydrate SequenceHemolymphMolecular MedicineAnimalsGlycolysisAmino Acid SequenceTrehalaseMolecular BiologyExperientia
researchProduct

Inhibition of trehalose breakdown increases new carbon partitioning into cellulosic biomass in Nicotiana tabacum

2010

Abstract Validamycin A was used to inhibit in vivo trehalase activity in tobacco enabling the study of subsequent changes in new C partitioning into cellulosic biomass and lignin precursors. After 12-h exposure to treatment, plants were pulse labeled using radioactive 11 CO 2 , and the partitioning of isotope was traced into [ 11 C]cellulose and [ 11 C]hemicellulose, as well as into [ 11 C]phenylalanine, the precursor for lignin. Over this time course of treatment, new carbon partitioning into hemicellulose and cellulose was increased, while new carbon partitioning into phenylalanine was decreased. This trend was accompanied by a decrease in phenylalanine ammonia-lyase activity. After 4 d o…

PhenylalanineNicotiana tabacumTrehalase activityPhenylalaninePhenylalanine ammonia-lyaseLigninBiochemistryAnalytical Chemistrychemistry.chemical_compoundPolysaccharidesTobaccoLigninOrganic chemistryHemicelluloseBiomassCarbon RadioisotopesTrehalaseFood scienceCelluloseCellulosePhenylalanine Ammonia-LyasebiologyOrganic ChemistryTrehalosefood and beveragesGeneral MedicineCarbon DioxideValidamycinbiology.organism_classificationCarbonEnzyme ActivationchemistryInositolCarbohydrate Research
researchProduct

The ATC1 gene encodes a cell wall-linked acid trehalase required for growth on trehalose in Candida albicans.

2004

After screening a Candida albicans genome data base, the product of an open reading frame (IPF 19760/CA2574) with 41% identity to Saccharomyces cerevisiae vacuolar acid trehalase (Ath1p) was identified and named Atc1p. The deduced amino acid sequence shows that Atc1p contains an N-terminal hydrophobic signal peptide and 20 potential sites for N-glycosylation. C. albicans homozygous mutants that lack acid trehalase activity were constructed by gene disruption at the two ATC chromosomal alleles. Analysis of these null mutants shows that Atc1p is localized in the cell wall and is required for growth on trehalose as a carbon source. An Atc1p endowed with acid trehalase activity was obtained by …

Saccharomyces cerevisiae ProteinsTime FactorsTranscription GeneticMutantBlotting WesternMolecular Sequence DataTrehalase activityBiologyBiochemistrychemistry.chemical_compoundOpen Reading FramesCell WallCandida albicansAmino Acid SequenceRNA MessengerTrehalaseTrehalaseCandida albicansMolecular BiologyPeptide sequenceAlleleschemistry.chemical_classificationCell-Free SystemModels GeneticSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionStructural geneHomozygoteNuclear ProteinsTrehaloseCell BiologyDNAbiology.organism_classificationPhosphoproteinsTrehaloseCarbonAmino acidProtein Structure TertiaryGlucosechemistryBiochemistryProtein BiosynthesisMutationElectrophoresis Polyacrylamide GelCell DivisionPlasmidsThe Journal of biological chemistry
researchProduct

Acid trehalase is involved in intracellular trehalose mobilization during postdiauxic growth and severe saline stress in Saccharomyces cerevisiae.

2008

The role of the acid trehalase encoded by the ATH1 gene in the yeast Saccharomyces cerevisiae is still unclear. In this work, we investigated the regulation of ATH1 transcription and found a clear involvement of the protein kinase Hog1p in the induction of this gene under severe stress conditions, such as high salt. We also detected changes in the acid trehalase activity and trehalose levels, indicating a role of the acid trehalase in intracellular trehalose mobilization. Finally, the growth analysis for different mutants in neutral and acid trehalases after high salt stress implicates acid trehalase activity in saline stress resistance.

SalinitySaccharomyces cerevisiae ProteinsTranscription GeneticSaccharomyces cerevisiaeMutantTrehalase activitySaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyMicrobiologychemistry.chemical_compoundOsmotic PressureGene Expression Regulation FungalTrehalaseTrehalaseProtein kinase AGene Expression ProfilingTrehaloseGeneral Medicinebiology.organism_classificationTrehaloseYeastBiochemistrychemistryMitogen-Activated Protein KinasesIntracellularGene DeletionFEMS yeast research
researchProduct

On the biochemical classification of yeast trehalases: Candida albicans contains two enzymes with mixed features of neutral and acid trehalase activi…

2009

Abstract Two enzymes endowed with trehalase activity are present in Candida albicans . The cytosolic trehalase (Ntc1p), displayed high activity in exponential phase regardless of the carbon source (glucose, trehalose or glycerol). Ntc1p activity was similar in neutral (pH 7.1) or acid (pH 4.5) conditions, strongly inhibited by ATP, weakly stimulated by divalent cations (Ca 2+ or Mn 2+ ) and unaffected in the presence of cyclic AMP. The Ntc1p activity decreased in stationary phase, except in glycerol-grown cultures, but the catalytic properties did not change. In turn, the cell wall-linked trehalase (Atc1p) showed elevated activity in resting cells or in cultures growing on trehalose or glyc…

chemistry.chemical_classificationbiologyBiophysicsTrehalase activityCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationBiochemistryTrehaloseYeastDivalentFungal ProteinsIsoenzymesCytosolchemistry.chemical_compoundAdenosine TriphosphateEnzymechemistryBiochemistryCandida albicansCyclic AMPTrehalaseTrehalaseCandida albicansMolecular BiologyBiochemical and Biophysical Research Communications
researchProduct