Results 101 to 110 of about 1,971,711 (246)
GlnK facilitates the dynamic regulation of bacterial nitrogen assimilation [PDF]
, 2017 Ammonium assimilation in E. coli is regulated by two paralogous proteins (GlnB and GlnK), which orchestrate interactions with regulators of gene expression, transport proteins and metabolic pathways. Yet how they conjointly modulate the activity of glutamine synthetase (GS), the key enzyme for nitrogen assimilation, is poorly understood.
arxiv +1 more source
Analysis of neutral mutational drift in an allosteric enzyme. [PDF]
Protein Sci, 2023 Liechty ET +6 more
europepmc +1 more source
On the hydrodynamics of swimming enzymes [PDF]
arXiv, 2015 Several recent experiments suggest that rather generally the diffusion of enzymes may be augmented through their activity. We demonstrate that such swimming motility can emerge from the interplay between the enzyme energy landscape and the hydrodynamic coupling of the enzyme to its environment.
arxiv
Journal of Experimental Biology, 2007 SUMMARY Temperature and heavy metals such as cadmium (Cd) are important environmental stressors that can strongly affect mitochondrial function of marine poikilotherms.
A. A. Cherkasov +3 more
semanticscholar +1 more source
Sensitivity Amplification in the Phosphorylation-Dephosphorylation Cycle: Nonequilibrium steady states, chemical master equation and temporal cooperativity [PDF]
Journal of Chemical Physics 2008, 2009 A new type of cooperativity termed temporal cooperativity [Biophys. Chem. 105 585-593 (2003), Annu. Rev. Phys. Chem. 58 113-142 (2007)], emerges in the signal transduction module of phosphorylation-dephosphorylation cycle (PdPC). It utilizes multiple kinetic cycles in time, in contrast to allosteric cooperativity that utilizes multiple subunits in a ...
arxiv
iScience, 2020 Summary: Insulin regulates glucose metabolism through thousands of regulatory mechanisms; however, which regulatory mechanisms are keys to control glucose metabolism remains unknown.
Satoshi Ohno +10 more
doaj
Dynamic regulation of phenylalanine hydroxylase
Pteridines, 2014 Phenylalanine hydroxylase (PAH) is the key enzyme in phenylalanine metabolism, catalyzing its oxidative breakdown to tyrosine. Its function in the committed step of amino acid metabolism requires strict regulation. Thus, several regulatory mechanisms are
Fuchs Julian E. +2 more
doaj +1 more source
Studies on medium-chain fatty acyl-coenzyme A synthetase. Enzyme fraction I: mechanism of reaction and allosteric properties [PDF]
, 1968 Jacob Bar‐Tana, G. Rose
openalex +1 more source
Frontiers in Bioengineering and Biotechnology, 2015 Modeling metabolism is fundamental for cell factory design. Central carbon metabolism (CCM) is particularly important as it provides the energy and precursors for other biological processes.
Daniel eMachado +2 more
doaj +1 more source
The nature of the inhibition and activation of epidermal phosphofructokinase: an allosteric enzyme.
Journal of Investigative Dermatology, 1972 Phosphofructokinase (PFK) was partially purified (× 50) from rhesus monkey epidermis. Kinetic studies showed a biphasic regulation of this enzyme by ATP, i.e., activation at low concentrations and inhibition at high concentrations. The partially purified
S. Kondo, K. Adachi
semanticscholar +1 more source