Search results for "Uncompetitive inhibitor"

showing 3 items of 3 documents

Natural products as inhibitors of recombinant cathepsin L of Leishmania mexicana.

2015

Cysteine proteinases (cathepsins) from Leishmania spp. are promising molecular targets against leishmaniasis. Leishmania mexicana cathepsin L is essential in the parasite life cycle and a pivotal in virulence factor in mammals. Natural products that have been shown to display antileishmanial activity were screened as part of our ongoing efforts to design inhibitors against the L. mexicana cathepsin L-like rCPB2.8. Among them, agathisflavone (1), tetrahydrorobustaflavone (2), 3-oxo-urs-12-en-28-oic acid (3), and quercetin (4) showed significant inhibitory activity on rCPB2.8 with IC50 values ranging from 0.43 to 18.03 µM. The mechanisms of inhibition for compounds 1–3, which showed Ki values…

Cathepsin LImmunologyLeishmania mexicanaVirulence factorLeishmania mexicanaCathepsin BCathepsin LInhibitory Concentration 50Non-competitive inhibitionparasitic diseasesmedicineBiflavonoidsHumansCathepsinBiological ProductsbiologyGeneral Medicinebiology.organism_classificationLeishmaniaRecombinant ProteinsKineticsInfectious DiseasesMechanism of actionBiochemistrybiology.proteinParasitologyQuercetinmedicine.symptomUncompetitive inhibitorExperimental parasitology
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A hypothetical model of the influence of inorganic phosphate on the kinetics of pyruvate kinase

2000

This paper presents a simple solution to the problem of approximating the calculated curve of reaction progress to the measured curve which is usually disturbed by initial oscillation of auxiliary lactate dehydrogenase (LDH) reaction. The experiments leading to the determination of the apparent Km for phosphoenolpyruvate (PEP) and Vm were performed. For precise estimation of kinetic parameters (Km and Vm) of the M1 isozyme of pyruvate kinase (PK), measured by coupling it to LDH reaction, the sequence of Michaelis‐Menten for pyruvate kinase and second-order kinetics for lactate dehydrogenase reaction as well as a non-zero initial concentration of lactate was assumed. The functions of apparen…

Statistics and ProbabilityStereochemistryPyruvate KinaseIn Vitro TechniquesModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyPhosphatesPhosphoenolpyruvatechemistry.chemical_compoundAdenosine TriphosphateLactate dehydrogenaseAnimalsEnzyme kineticsEnzyme InhibitorsL-Lactate DehydrogenaseKinaseApplied MathematicsGeneral MedicineNADPhosphateAdenosine DiphosphateDissociation constantKineticsBiochemistrychemistryModeling and SimulationCattleUncompetitive inhibitorPhosphoenolpyruvate carboxykinasePyruvate kinaseBiosystems
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Allosteric regulation by Mg2+ of the vacuolar H(+)-PPase from Acer pseudoplatanus cells. Ca2+/Mg2+ interactions.

1996

The tonoplast H(+)-PPase was previously characterized in Acer pseudoplatanus cells (Pugin et al (1991) Plant Sci 73, 23-34; Fraichard et al (1993) Plant Physiol Biochem 31, 349-359). Tonoplast vesicles were obtained from vacuoles isolated from protoplasts of A pseudoplatanus suspension cultures and used to study kinetic effects of Mg2+ and Ca2+ on PPi hydrolysis. The concentrations of ionic species (free Mg2+, free PPi, and MgPPi complexes) were calculated with apparent dissociation constants of 55.3 microM for MgPPi and 59.6 microM for CaPPi. Our results indicated that the substrate of the tonoplast PPase was a MgPPi complex and that free Mg2+ was essential for PPi hydrolysis. With fixed f…

inorganic chemicals0106 biological sciencesTrisAllosteric regulation01 natural sciencesBiochemistryTrees03 medical and health sciencesEnzyme activatorchemistry.chemical_compoundOrganophosphorus CompoundsAllosteric Regulation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMagnesiumBinding sitePyrophosphatasesComputingMilieux_MISCELLANEOUSCells Cultured030304 developmental biologychemistry.chemical_classification0303 health sciencesInorganic pyrophosphataseERABLE FAUX PLATANEGeneral MedicineDissociation constantEnzyme ActivationInorganic PyrophosphataseKineticsEnzymechemistryBiochemistryVacuolesCalciumUncompetitive inhibitor010606 plant biology & botanyBiochimie
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