Results 91 to 100 of about 1,971,711 (246)
Mechanism of allosteric activation of SIRT6 revealed by the action of rationally designed activators
Acta Pharmaceutica Sinica B, 2021 The recent discovery of activator compounds binding to an allosteric site on the NAD+-dependent protein lysine deacetylase, sirtuin 6 (SIRT6) has attracted interest and presents a pharmaceutical target for aging-related and cancer diseases.
Shaoyong Lu +6 more
doaj
A model for the allosteric regulation of pH-sensitive enzymes [PDF]
Biochemical Journal, 1977 1. In an enzyme that has two independent binding sites for a ligand, any inhibitor that binds solely to the free enzyme will give rise to positive co-operativity. 2. A model is considered for the allosteric control of enzymes by effectors in which their effects are mediated by ligand-induced perturbations of the ionization constants of a group or ...
K F Tipton, J S Shindler
openaire +3 more sources
Journal of Biological Chemistry, 2002 The catalytic activity of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is allosterically regulated. The hydrogen bond between the helix betaH6 residue betaSer(178) and the loop alphaL6 residue Gly(181) was shown to be ...
M. Weyand +4 more
semanticscholar +1 more source
Unraveling the activation mechanism of the potato tuber ADP-glucose pyrophosphorylase. [PDF]
PLoS ONE, 2013 ADP-glucose pyrophosphorylase regulates the synthesis of glycogen in bacteria and of starch in plants. The enzyme from plants is mainly activated by 3-phosphoglycerate and is a heterotetramer comprising two small and two large subunits.
Carlos M Figueroa +6 more
doaj +1 more source
SOD1 Exhibits Allosteric Frustration to Facilitate Metal Binding Affinity [PDF]
, 2013 Superoxide dismutase-1 (SOD1) is a ubiquitous, Cu and Zn binding, free radical defense enzyme whose misfolding and aggregation play a potential key role in amyotrophic lateral sclerosis, an invariably fatal neurodegenerative disease. Over 150 mutations in SOD1 have been identified with a familial form of the disease, but it is presently not clear what ...
arxiv +1 more source
Purine Nucleoside Phosphorylase: Allosteric Regulation of a Dissociating Enzyme
Journal of Biological Chemistry, 1991 Purine nucleoside phosphorylase (EC 2.4.2.1) from bovine spleen is a trimeric enzyme that readily dissociates to the monomer. Dilution of enzyme from 20 to 0.02 microgram of protein/ml is accompanied by a greater than 50-fold increase in the specific activity (vtrimer = 0.23 nmol/min/microgram; vmonomer = 12.5 nmol/min/micrograms).
T W, Traut, P A, Ropp, A, Poma
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A model for the regulation of D‐3‐phosphoglycerate dehydrogenase, a Vmax‐type allosteric enzyme
Protein Science, 1996 Escherichia coli D‐3‐phosphoglycerate dehydrogenase (ePGDH) is a tetramer of identical subunits that is alloste‐rically inhibited by L‐serine, the end product of its metabolic pathway.
G. A. Grant, D. Schuller, L. Banaszak
semanticscholar +1 more source
eLife, 2018 Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function. Here,
Daniel A Keedy +9 more
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Stochastic approach to molecular interactions and computational theory of metabolic and genetic regulations [PDF]
, 2006 Binding and unbinding of ligands to specific sites of a macromolecule are one of the most elementary molecular interactions inside the cell that embody the computational processes of biological regulations. The interaction between transcription factors and the operators of genes and that between ligands and binding sites of allosteric enzymes are ...
arxiv +1 more source
Human Genomics, 2020 Background Gain-of-function mutations in the GLUD1 gene, encoding for glutamate dehydrogenase (GDH), result in the hyperinsulinism/hyperammonemia HI/HA syndrome.
Karolina Luczkowska +6 more
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