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13 results for “enzyme stability”
The process of HDAC11 Assay Development: enzyme stability
<p>Before performing the kinetic study for calculating the Km for HDAC11, it is important to know the duration of the stability of the protein under the assay conditions. This is being analyzed here.</p> <p> </p> <p><strong>Note: </strong>1. In the assay buffer, BSA conc. is 0.5 mg/ml (instead of 0.5%).</p> <p> 2. In the 7.5 ul developer solution, 40 uM of TSA (Trichostatin A) is also included.</p>
Understanding Activity-Stability Tradeoffs in Biocatalysts by Enzyme Proximity Sequencing
<p>Data and scripts of the manuscript "<strong>Understanding Activity-Stability Tradeoffs in Biocatalysts by Enzyme Proximity Sequencing</strong>" by Rosario Vanella, Christoph Küng, Alexandre A. Schoepfer, Vanni Doffini, Jin Ren and Michael A. Nash.</p>
Data from: Characterisation of a cold-adapted, thermostable glucokinase from psychrophilic <em>Pseudoalteromonas</em> sp. AS-131 reveals how the enzyme achieves high thermal stability without loss of cold adaptation
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Data for: The galactokinase enzyme of yeast senses metabolic flux to stabilize GAL pathway regulation
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Fig. 3 in Stabilization of dhurrin biosynthetic enzymes from Sorghum bicolor using a natural deep eutectic solvent
Fig. 3. NADES-based stabilization of the dhurrin biosynthetic enzymes. A) Illustration of proteoliposomes comprising the POR2B, CYP79A1, CYP71E1 and UGT85B1 reconstituted in liposomes composed of phospholipids extracted from etiolated sorghum seedlings (Metabolon). B) Recovery of activity upon storage of enzymes in NADES and glycerol compared to buffer upon dilution displayed as relative conversion of tyrosine for the Metabolon samples and conversion of cyanohydrin to dhurrin for the UGT85B1 samples. Values are mean of three technical replicates± SD. C) Stability of dhurrin biosynthetic enzymes stored at room temperature in aqueous buffer, NADES and glycerol. Samples were diluted in buffer prior to activity assay. Values are mean of three technical replicates ±SD and fitted to a double exponential decay. D) Bar plot showing relative activity of the enzymes following incubation at various temperatures for 30 min in aqueous buffer, NADES and glycerol. Samples were diluted in buffer prior to activity assay. All values are mean of three independent technical replicates ± SD.
Fig. 2 in Stabilization of dhurrin biosynthetic enzymes from Sorghum bicolor using a natural deep eutectic solvent
Fig. 2. Dhurrin biosynthesis in the presence of different NADESs. A) Etiolated sorghum seedlings used for preparation of microsomes. B) Tyrosine conversion assay in microsomes at different NADES concentrations indicates an optimum at 5% NADES for both glucose:tartrate and glucose:malate. Values are mean of three technical replicates ± SD.
Fig. 1 in Stabilization of dhurrin biosynthetic enzymes from Sorghum bicolor using a natural deep eutectic solvent
Fig. 1. Formation of NADES derived from natural occurring metabolites in plants. A) Chemical structures of D-glucose, tartaric acid, malic acid, choline, glycerol and dhurrin. Mixtures of these metabolites were tested for their ability to form NADES and their potential role in stabilizing the dhurrin biosynthetic enzymes. B) Stoichiometric mixture of glucose and tartrate constitute a NADES with significantly lowered melting point compared to the individual components. C) Biosynthetic pathway of the natural product dhurrin in S. bicolor.
Unrecognized controls on microbial functioning in Blue Carbon ecosystems: the role of mineral enzyme stabilization and allochthonous substrate supply
Tidal wetlands are effective carbon sinks, mitigating climate change through the long-term removal of atmospheric CO2. Studies along surface-elevation and thus flooding-frequency gradients in tidal wetlands are often used to understand the effects of accelerated sea-level rise on carbon sequestration, a process that is primarily determined by the balance of primary production and microbial decomposition. It has often been hypothesized that rates of microbial decomposition would increase with elevation and associated increases in soil oxygen availability; however, previous studies yield a wide range of outcomes and equivocal results. Our mechanistic understanding of the elevation-decomposition relationship is limited because most effort has been devoted to understanding the terminal steps of the decomposition process. Few studies assessed microbial exo-enzyme activities (EEAs) as initial and rate-limiting steps that often reveal important insight into microbial energy and nutrient constraints. The present study assessed EEAs and microbial abundance along a coastal ecotone stretching a flooding gradient from tidal flat to high marsh in the European Wadden Sea. We found that stabilization of exo-enzymes to mineral sediments leads to high specific EEAs at low substrate concentrations in frequently flooded, sediment rich zones of the studied ecotone. We argue that the high background activity of a mineral-associated enzyme pool provides a stable decomposition matrix in highly dynamic, frequently flooded zones. Furthermore, we demonstrate that microbial communities are less nutrient limited in frequently flooded zones, where inputs of nutrient-rich marine organic matter are higher. This was reflected in both increasing exo-enzymatic carbon-vs.-nutrient acquisition and decreasing fungal-vs.-bacterial abundance with increasing flooding frequency. Our findings thereby suggest two previously unrecognized mechanisms that may contribute to stimulated microbial activity despite decreasing oxygen availability in response to accelerated sea-level rise.
Data from: An appraisal of the enzyme stability-activity trade-off
A longstanding idea in evolutionary physiology is that an enzyme cannot jointly optimize performance at both high and low temperatures due to a trade-off between stability and activity. Although a stability-activity trade-off has been observed for well-characterized examples, such a trade-off is not imposed by any physical chemical constraint. To better understand the pervasiveness of this trade-off, I investigated the stability-activity relationship for comparative biochemical studies of purified orthologous enzymes identified by a literature search. The nature of this relationship varied greatly among studies. Notably, studies of enzymes with low mean synonymous nucleotide sequence divergence were less likely to exhibit the predicted negative correlation between stability and activity. Similarly, a survey of directed evolution investigations of the stability-activity relationship indicated that these traits are often uncoupled among nearly identical yet phenotypically divergent enzymes. This suggests that the presumptive trade-off often reported for investigations of enzymes with high mean sequence divergence may in some cases instead be a consequence of the degeneration over time of enzyme function in unselected environments, rather than a direct effect of thermal adaptation. The results caution against the general assertion of a stability-activity trade-off during enzyme adaptation.
Enzyme inhibitors employ different mechanisms to stabilize broad-spectrum antiviral ACE2-Fc fusion proteins
<p>Drugs effective for all variants of a virus are urgently needed to fight current and future pandemics. This can be achieved by creating fusion proteins between the extracellular domains of the virus docking sites on human cells and the Fc part from a human immunoglobulin. The angiotensin-converting enzyme 2 (ACE2) is a viral receptor used by sarbeco betacorona-viruses to infect cells. Fusion proteins comprising extracellular ACE2 domains exhibit high virus neutralization efficiency, but the structure and stability of these molecules are poorly understood. Here we analyzed the structure and stability of an ACE2-IgG4-Fc. We show that the hinge between the ACE2 region and the IgG4-FC is highly flexible, and the conformational dynamics of the fusion protein is restricted by the ACE2 domain[MS1] . Interestingly, chemical compounds inhibiting the enzymatic activity of ACE2 such as DX600 and MLN4760 employ different binding mechanisms to increase the thermal stability of the ACE2 by 8.8 and 14.3 °C, respectively. In particular, MLN4760 induced allosteric effects in the ACE2 domain consistent with structural rearrangements observed in the inhibitor-bound crystal structure. Thus, our findings reveal a general concept for stabilizing the labile receptor segment of therapeutic antiviral fusion proteins[MS2] .</p>
Data from: An appraisal of the enzyme stability-activity trade-off
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Unrecognized controls on microbial functioning in Blue Carbon ecosystems: the role of mineral enzyme stabilization and allochthonous substrate supply
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Major satellite repeat RNA stabilize heterochromatin retention of Suv39h enzymes by RNA-nucleosome association and RNA:DNA hybrid formation
GEO Series GSE100222. Mus musculus. 24 samples. Type: Expression profiling by high throughput sequencing.
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