Results 31 to 40 of about 57,293 (304)
Mammalian Alkaline Phosphatases Are Allosteric Enzymes [PDF]
Journal of Biological Chemistry, 1997 Mammalian alkaline phosphatases (APs) are zinc-containing metalloenzymes encoded by a multigene family and functional as dimeric molecules. Using human placental AP (PLAP) as a paradigm, we have investigated whether the monomers in a given PLAP dimer are subject to cooperativity during catalysis following an allosteric model or act via a half-of-sites ...
M F, Hoylaerts, T, Manes, J L, Millán
openaire +2 more sources
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 +1 more source
PLoS ONE, 2014 The role of tertiary conformational changes associated to ligand binding was explored using the allosteric enzyme glucosamine-6-phosphate (GlcN6P) deaminase from Escherichia coli (EcGNPDA) as an experimental model.
Sergio Zonszein +3 more
doaj +1 more source
Organism-adapted specificity of the allosteric regulation of pyruvate kinase in lactic acid bacteria. [PDF]
PLoS Computational Biology, 2013 Pyruvate kinase (PYK) is a critical allosterically regulated enzyme that links glycolysis, the primary energy metabolism, to cellular metabolism. Lactic acid bacteria rely almost exclusively on glycolysis for their energy production under anaerobic ...
Nadine Veith +5 more
doaj +1 more source
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
Frontiers in Molecular Biosciences, 2022 5-Aminolevulinate synthase (ALAS; E.C. 2.3.1.37) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the key regulatory step of porphyrin biosynthesis in metazoa, fungi, and α-proteobacteria.
Gregory A. Hunter +3 more
doaj +1 more source
Journal of Enzyme Inhibition and Medicinal Chemistry, 2023 The formal mechanism of linear mixed and non-competitive enzyme inhibition implies the binding of inhibitors to both the active site of the free enzyme in competition with the substrate, and to an allosteric site on the enzyme-substrate complex. However,
Alessandro Pesaresi
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
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
Real‐time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer
FEBS Letters, EarlyView.Ribonucleotide reductases (RNR) synthesize DNA building blocks de novo, making them crucial in DNA replication and drug targeting. FLARE introduces the first single‐tube real‐time coupled RNR assay, which enables isothermal tracking of RNR activity at nanomolar enzyme levels and allows the reconstruction of allosteric regulatory patterns and rapid ...
Jacopo De Capitani +4 more
wiley +1 more source