Search results for "alcohol dehydrogenases"

showing 4 items of 4 documents

Heavy enzymes and the rational redesign of protein catalysts

2019

Abstract An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Comparison between isotopically labelled “heavy” dihydrofolate reductases and their natural‐abundance counterparts has suggested that the coupling of protein motions to the chemistry of the catalysed reaction is minimised in the case of hydride transfer. In alcohol dehydrogenases, unnatural, bulky substrates that induce additional electrostatic rearrangements of the active site enhance coupled motions. This finding could provide a new route to engineering enzymes with altered substrate specificity, because amino acid residues responsible for dynamic coupling with a given substrate present…

010402 general chemistryProtein Engineering01 natural sciencesBiochemistryCatalysisEnzyme catalysisisotope effectsCatalytic DomainDihydrofolate reductaseMolecular BiologyAlcohol dehydrogenasechemistry.chemical_classificationalcohol dehydrogenasesCarbon Isotopesdihydrofolate reductasesbiologyBacteriaNitrogen Isotopes010405 organic chemistryConceptOrganic ChemistryAlcohol DehydrogenaseActive siteSubstrate (chemistry)Protein engineeringDeuteriumCombinatorial chemistrymolecular dynamics0104 chemical sciencesKineticsTetrahydrofolate Dehydrogenaseenzyme engineeringEnzymechemistrybiology.proteinBiocatalysisMolecular MedicineConcepts
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Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina

2006

The mould Hypocrea jecorina (Trichoderma reesei) has two genes coding for enzymes with high similarity to the NADP-dependent glycerol dehydrogenase. These genes, called gld1 and gld2, were cloned and expressed in a heterologous host. The encoded proteins were purified and their kinetic properties characterized. GLD1 catalyses the conversion of d-glyceraldehyde and l-glyceraldehyde to glycerol, whereas GLD2 catalyses the conversion of dihydroxyacetone to glycerol. Both enzymes are specific for NADPH as a cofactor. The properties of GLD2 are similar to those of the previously described NADP-dependent glycerol-2- dehydrogenases (EC 1.1.1.156) purified from different mould species. It is a reve…

HypocreaDihydroxyacetoneGlyceraldehydeBiochemistrychemistry.chemical_compoundHypocreaGlyceraldehydeGlycerolCloning MolecularMolecular BiologyTrichoderma reeseichemistry.chemical_classificationbiologyGlycerol dehydrogenaseGlyceraldehyde-3-Phosphate DehydrogenasesHypocrea jecorinaCell Biologybiology.organism_classificationRecombinant ProteinsL-glyceraldehydeEnzymeGlycerol-3-phosphate dehydrogenasechemistryBiochemistryDihydroxyacetoneGlycerol dehydrogenaseNADP-specific glycerol dehydrogenaseNADPSugar Alcohol DehydrogenasesFEBS Journal
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Responses of Prunus ferganensis, Prunus persica and two interspecific hybrids to moderate drought stress

2003

Prunus ferganensis (Kost. & Riab) Kov. & Kost, a close relative of the cultivated peach (Prunus persica (L.) Batsch.), is native to arid regions of central Asia and may possess traits valuable for improving drought tolerance of commercial peach varieties. One distinguishing feature of P. ferganensis is its prominent, elongated, unbranched leaf venation pattern, which behaves as a simple recessive trait in segregating populations of P. ferganensis x P. persica hybrids. To understand whether this trait could be used as a marker in breeding for drought tolerance, we investigated the association between leaf morphological and physiological parameters related to drought response in P. ferganensi…

L-Iditol 2-DehydrogenaseSpecific leaf areaPhysiologyClimatic adaptationDrought tolerancePlant ScienceBiologyTreesPrunusDry weightSorbitolLeaf sizePhotosynthesisgas exchange non-hydraulic signals peach photosynthesis sorbitol water potentialHybridDehydrationfungiWaterfood and beveragesPlant TranspirationPlant LeavesSettore AGR/03 - Arboricoltura Generale E Coltivazioni ArboreeAgronomyPrunusRootstockSugar Alcohol DehydrogenasesTree Physiology
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Active surfaces engineered by immobilizing protein-polymer nanoreactors for selectively detecting sugar alcohols.

2016

We introduce active surfaces generated by immobilizing protein-polymer nanoreactors on a solid support for sensitive sugar alcohols detection. First, such selective nanoreactors were engineered in solution by simultaneous encapsulation of specific enzymes in copolymer polymersomes, and insertion of membrane proteins for selective conduct of sugar alcohols. Despite the artificial surroundings, and the thickness of the copolymer membrane, functionality of reconstituted Escherichia coli glycerol facilitator (GlpF) was preserved, and allowed selective diffusion of sugar alcohols to the inner cavity of the polymersome, where encapsulated ribitol dehydrogenase (RDH) enzymes served as biosensing e…

Models MolecularMaterials scienceMembrane permeabilityPolymersSurface PropertiesBiophysicsBioengineering02 engineering and technologyNanoreactorBiosensing Techniques010402 general chemistryRibitolAquaporins01 natural sciencesPermeabilityBiomaterialschemistry.chemical_compoundSugar AlcoholsEscherichia coliOrganic chemistrySugar alcoholRibitolchemistry.chemical_classificationEscherichia coli Proteins021001 nanoscience & nanotechnology0104 chemical sciencesNanostructuresMembraneImmobilized ProteinschemistryMechanics of MaterialsPolymersomeCeramics and Composites0210 nano-technologyBiosensorSugar Alcohol DehydrogenasesSugar Alcohol DehydrogenasesBiomaterials
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