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5 results for “malate dehydrogenase”
Data from: Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases.
<p>This data accompanies the paper entitled <strong><em>Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases.</em></strong></p> <p>The zip archive contains the results of molecular dynamics simulations of the 2 systems investigated in the paper: <em>S. rum</em> and <em>T. mar</em> LDHs. The systems have been simulated at 315 K for <em>S. rum </em>and 340 K for <em>T. mar</em>. Final configurations of the proteins after productions are provided for all the systems in GRO Gromos87 format. Trajectories with the positions of the proteins every 100 ps are provided for all the systems in XTC gromacs format.</p>
Data from: Protein Conformational Space at the Edge of Allostery: Turning a Non-allosteric Malate Dehydrogenase into an "Allosterized" Enzyme using Evolution Guided Punctual Mutations
<p>This data accompanies the paper entitled <em>Protein Conformational Space at the Edge of Allostery: Turning a Non-allosteric Malate Dehydrogenase into an “Allosterized” Enzyme using Evolution Guided Punctual Mutations</em></p> <p>The zip archive contains the results of molecular dynamics simulations of the 4 systems investigated in the paper: wt of A. ful MalDH and three mutants. Each system has been simulated at two temperatures, 300 K and 340 K. Starting configurations of the proteins after equilibration are provided for all the systems in GRO Gromos87 format. Trajectories with the positions of the proteins every 100 ps are provided for all the systems in XTC gromacs format.</p>
Tree and amino acid alignments of thioredoxin, glucose-6-phosphate dehydrogenase, and malate dehydrogenase
<p>Redox regulation in phytoplankton is critical to monitor and stabilize metabolic pathways under changing environmental conditions. In plastids, the thioredoxin (TRX) system is linked to photosynthetic electron transport and fine tuning the metabolism to fluctuating light levels. Expansion of the number of redox signal transmitters and their protein targets, as seen in plants, is believed to increase cell robustness. In this study, we searched for genes related to redox regulation in the genome of the photosynthetic amoeba <i>Paulinella micropora </i>KR01 (hereafter, KR01). The genus <i>Paulinella </i>includes testate filose amoebae, in which a single clade acquired a photosynthetic organelle, the chromatophore, from an alpha cyanobacterial donor<i>. </i>This independent primary endosymbiosis occurred relatively recently (~ 124 Ma), when compared to Archaeplastida (> 1 Ga), making photosynthetic <i>Paulinella </i>a valuable model for studying the earlier stages of primary endosymbiosis.<i> </i>Our comparative analysis demonstrates that this lineage has<i> </i>evolved a thioredoxin system similar to that from other algae, relying however on genes with diverse phylogenetic origins (i.e., the endosymbiont, host, bacteria, red algae). One TRX of eukaryotic provenance is targeted to the chromatophore, implicating host-endosymbiont coordination of redox regulation. A chromatophore targeted glucose-6-phosphate dehydrogenase of red algal origin suggests that <i>Paulinella </i>exploited the existing redox regulation system in Archaeplastida to foster integration. Our study elucidates the independent evolution of the thioredoxin system in photosynthetic <i>Paulinella</i>, whose parts derive from the existing genetic toolkit in diverse organisms.</p>
Metabolic regulation of the glioblastoma stem cell epitranscriptome by malate dehydrogenase 2 (MDH2)
GEO Series GSE255535. Homo sapiens. 18 samples. Type: Expression profiling by high throughput sequencing; Other.
Tree and amino acid alignments of thioredoxin, glucose-6-phosphate dehydrogenase, and malate dehydrogenase
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