Results 51 to 60 of about 1,971,711 (246)
Structure and allosteric regulation of human NAD-dependent isocitrate dehydrogenase
Cell Discovery, 2020 Human NAD-dependent isocitrate dehydrogenase or HsIDH3 catalyzes the decarboxylation of isocitrate into α-ketoglutarate in the TCA cycle. HsIDH3 exists and functions as a heterooctamer composed of the αβ and αγ heterodimers, and is regulated ...
Pengkai Sun +3 more
doaj +1 more source
A non-equilibrium dynamic mechanism for the allosteric effect [PDF]
Phys. Rev. Lett. 99, 168103 (2007), 2007 Allosteric regulation is often viewed as thermodynamic in nature. However protein internal motions during an enzymatic reaction cycle can be slow hopping processes over numerous potential barriers. We propose that regulating molecules may function by modifying the nonequilibrium protein dynamics.
arxiv +1 more source
Biochemical Journal, 2015 We have studied enzyme kinetics, nucleotide binding and allosteric modulation of six recombinant AMP-activated protein kinase (AMPK) isoforms by known allosteric activators.
F. Rajamohan +11 more
semanticscholar +1 more source
Applied and Environmental Microbiology, 2011 Product feedback inhibition of allosteric enzymes is an essential issue for the development of highly efficient microbial strains for bioproduction.
Zhen Chen +4 more
semanticscholar +1 more source
Allostery and Kinetic Proofreading [PDF]
J. Phys. Chem. B 2019, 123, 51, 10990-11002, 2020 Kinetic proofreading is an error correction mechanism present in the processes of the central dogma and beyond, and typically requires the free energy of nucleotide hydrolysis for its operation. Though the molecular players of many biological proofreading schemes are known, our understanding of how energy consumption is managed to promote fidelity ...
arxiv +1 more source
Nature Communications, 2017 Pyruvate kinase (PYK) controls glycolytic flux. Here, the authors combine biochemical, structural and computational modelling studies to characterize the allosteric mechanisms regulating Mycobacterium tuberculosis PYK activity and show that AMP and ...
Wenhe Zhong +11 more
doaj +1 more source
Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase
Nature Communications, 2023 Allosteric drugs have the potential to revolutionize biomedicine due to their enhanced selectivity and protection against overdosage. However, we need to better understand allosteric mechanisms in order to fully harness their potential in drug discovery.
Federica Maschietto +10 more
doaj +1 more source
Nature Communications, 2019 Allosteric interactions are an important contributor to the catalytic properties of enzyme. Here the authors demonstrate—using the prototypical protein kinase PKA—that the allosteric cooperativity underscoring substrate recognition and product release ...
Yingjie Wang +7 more
doaj +1 more source
Biomolecules, 2021 Glutamate dehydrogenase (GDH) is a ubiquitous enzyme that catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate. It acts as an important branch-point enzyme between carbon and nitrogen metabolisms.
Shaherin Basith +3 more
doaj +1 more source
Allostery and cooperativity in multimeric proteins: bond-to-bond propensities in ATCase [PDF]
Scientific Reports, volume 8, Article number: 11079 (2018), 2019 Aspartate carbamoyltransferase (ATCase) is a large dodecameric enzyme with six active sites that exhibits allostery: its catalytic rate is modulated by the binding of various substrates at distal points from the active sites. A recently developed method, bond-to-bond propensity analysis, has proven capable of predicting allosteric sites in a wide range
arxiv +1 more source