ArticleThe journal of physical chemistry. B2010
Evidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa.
Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Simulations suggest double sodium binding induces unexpected conformational changes in thrombin.Journal of molecular modeling · 2022Article
- The active site region plays a critical role in NaThe Journal of biological chemistry · 2022Article
- Article
- Mechanisms of ligand binding.Biophysics reviews · 2020Review
- Article
- Residues W215, E217 and E192 control the allosteric E*-E equilibrium of thrombin.Scientific reports · 2019Article
- Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa.Scientific reports · 2018Article
- Interplay between conformational selection and zymogen activation.Scientific reports · 2018Article
- Molecular Mechanisms of Enzyme Activation by Monovalent Cations.The Journal of biological chemistry · 2016Review
- Why Ser and not Thr brokers catalysis in the trypsin fold.Biochemistry · 2015Article
- Essential role of conformational selection in ligand binding.Biophysical chemistry · 2014Review
- Conformational selection is a dominant mechanism of ligand binding.Biochemistry · 2013Article
- Conformational selection in trypsin-like proteases.Current opinion in structural biology · 2012Review
- Conformational selection or induced fit? A critical appraisal of the kinetic mechanism.Biochemistry · 2012Article
- Rigidification of the autolysis loop enhances Na(+) binding to thrombin.Biophysical chemistry · 2011Article
- Allostery in trypsin-like proteases suggests new therapeutic strategies.Trends in biotechnology · 2011Review
- Article
- Crystal structure of prethrombin-1.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Na(+) binding to thrombin enhances the procoagulant and prothrombotic functions of the enzyme and obeys a mechanism that produces two kinetic phases: one fast (in the microsecond time scale) due to Na(+) binding to the low activity form E to produce the high activity form E:Na(+) and another considerably slower (in the millisecond time scale) that reflects a pre-equilibrium between E and the inactive form E*. In this study, we demonstrate that this mechanism also exists in other Na(+)-activated clotting proteases like factor Xa and activated protein C. These findings, along with recent structural data, suggest that the E*-E equilibrium is a general feature of the trypsin fold.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.