Results 1 to 10 of about 2,040,864 (360)

The endocannabinoid hydrolase FAAH is an allosteric enzyme. [PDF]

open access: yesSci Rep, 2020
Fatty acid amide hydrolase (FAAH) is a membrane-bound homodimeric enzyme that in vivo controls content and biological activity of N-arachidonoylethanolamine (AEA) and other relevant bioactive lipids termed endocannabinoids.
Dainese E   +9 more
europepmc   +11 more sources

Patterns of Spatiotemporal Organization in an Allosteric Enzyme Model [PDF]

open access: greenProceedings of the National Academy of Sciences, 1973
The behavior of a model for an allosteric enzyme oscillator activated by the reaction product is analyzed in the presence of diffusion. When the concentrations of the chemicals are fixed at the boundaries, dynamic dissipative structures are shown to ...
Albert Goldbeter
semanticscholar   +6 more sources

Allosteric Enzyme-Based Biosensors—Kinetic Behaviours of Immobilised L-Lysine-α-Oxidase from Trichoderma viride: pH Influence and Allosteric Properties [PDF]

open access: goldBiosensors, 2020
The present study describes the kinetics of L-lysine-α-oxidase (LO) from Trichoderma viride immobilised by co-crosslinking onto the surface of a Pt electrode. The resulting amperometric biosensor was able to analyse L-lysine, thus permitting a simple but
Antonio Guerrieri   +4 more
doaj   +4 more sources

Uncoupling conformational states from activity in an allosteric enzyme. [PDF]

open access: yesNat Commun, 2017
ATP-phosphoribosyltransferase (ATP-PRT) is a hexameric enzyme in conformational equilibrium between an open and seemingly active state and a closed and presumably inhibited form. The structure-function relationship of allosteric regulation in this system
Pisco JP   +8 more
europepmc   +2 more sources

Recombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activity. [PDF]

open access: yesSci Rep, 2016
L-asparaginase (L-ASNase) (EC 3.5.1.1) is an important enzyme for the treatment of acute lymphoblastic leukaemia. Currently, the enzyme is obtained from bacteria, Escherichia coli and Erwinia chrysanthemi.
Costa IM   +7 more
europepmc   +2 more sources

Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase. [PDF]

open access: yesStructure, 2004
Glucokinase is a monomeric enzyme that displays a low affinity for glucose and a sigmoidal saturation curve for its substrate, two properties that are important for its playing the role of a glucose sensor in pancreas and liver. The molecular basis for these two properties is not well understood.
K. Kamata   +4 more
semanticscholar   +4 more sources

DNA Detection and Signal Amplification via an Engineered Allosteric Enzyme [PDF]

open access: greenJournal of the American Chemical Society, 2002
Rapid, sensitive, and sequence-specific DNA detection can be achieved in one step using an engineered intrasterically regulated enzyme. The semi-synthetic inhibitor-DNA-enzyme (IDE) construct (left) rests in the inactive state but upon exposure to a ...
Alan Saghatelian   +3 more
openalex   +2 more sources

Redesigning allosteric activation in an enzyme [PDF]

open access: greenProceedings of the National Academy of Sciences, 2011
Enzyme activation by monovalent cations is widely documented in plants and the animal world. In type II enzymes, activation entails two steps: binding of the monovalent cation to its allosteric site and transduction of this event into enhanced catalytic activity.
Sadhna Rana   +3 more
openalex   +5 more sources

Comparison of Plant-Type Phospho enol pyruvate Carboxylases from Rice: Identification of Two Plant-Specific Regulatory Regions of the Allosteric Enzyme [PDF]

open access: bronzePlant and Cell Physiology, 2014
Phosphoenolpyruvate carboxylase (PEPC) is a key enzyme of primary metabolism in bacteria, algae and vascular plants, and it undergoes allosteric regulation by various metabolic effectors.
Masayuki Muramatsu   +3 more
openalex   +2 more sources

Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation [PDF]

open access: hybridJournal of Biological Chemistry, 2009
The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven three-dimensional structures of the enzyme, of enzyme variants, or of enzyme complexes from two yeast ...
S. Kutter   +5 more
openalex   +2 more sources

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