Allosteric RegulationEnzyme ControlAllosteric SiteConformational ChangeShape ChangeAffinitySubstrate Concentration GraphAllosteric ActivationPositive S-shaped CurveLag TimeSubstrate BindingRapid Reaction SpeedEffector MoleculeAllosteric InhibitionEnzyme FunctionChemical Reaction RateEnzymatic Activity JoVE...
ALLOSTERIC regulationDNADECARBOXYLATIONNAD (Coenzyme)HETERODIMERSHuman 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 ...
Conformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart. F. Conformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart. Biochemistry... RS ...
Our structural and functional data together reveal the molecular mechanism of the allosteric regulation of the αγ heterodimer. Isocitrate dehydrogenases (IDHs) are a family of enzymes that catalyze the oxidative decarboxylation of isoc- itrate (ICT) into α-ketoglutarate (α-KG) using ...
An important advance in the understanding of the PanK catalysis and regulation is the concept that the pantothenate substrate binding site overlaps with the docking site for the allosteric regulator, acetyl-CoA. A comparison between the PanK3⋅acetyl-CoA and SaPanK⋅ATP⋅Mg2+ structures reveals...
Functional and regulatory properties of the beta S178P mutant. The alpha(2)beta(2) tryptophan synthase complex is a model enzyme for understanding allosteric regulation. We report the functional and regulatory properti... Marabotti,A. - 《Journal of Biological Chemistry》 被引量: 50发表: 2001...
catalyses the fourth step of the pathway, is competitively inhibited by CoA and its product dephospho-CoA31,32. However, nothing was known about the regulation of CoaBC in any organism. We therefore examined the effect of CoA and several of its thioesters (acetyl-CoA, malonyl-CoA and ...
[54,66], while mutagenesis studies in NAGS fromPseudomonas aeruginosa, which is similar toE. coliNAGS, indicate that the arginine binding site is localized in the kinase domain [67]. Microbial and plant NAGS are inhibited by arginine, as part of feedback regulation of arginine biosynthesis [58...
mTOR pathway hyper activation is a common feature in many cancers, including in nearly 90% of Glioblastomas. mTOR exists in two multiprotein complexes, which differ in regulation, function, and response to the allosteric mTOR inhibitor r... B Gini,D Guo,D Nathanson,... - 《Cancer Research...
Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate. The reaction occurs in two separate catalytic domains, coupled by the long-range translocation of a biotinylated carrier domain (BCCP). Here, we use a series