ArticleBiochemistry2010
Global fit analysis of glucose binding curves reveals a minimal model for kinetic cooperativity in human glucokinase.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Unravelling the intricate cooperativity of subunit gating in P2X2 ion channels.Scientific reports · 2020Article
- Nanosecond-Timescale Dynamics and Conformational Heterogeneity in Human GCK Regulation and Disease.Biophysical journal · 2020Article
- Solution NMR Spectroscopy for the Study of Enzyme Allostery.Chemical reviews · 2016Review
- Dual allosteric activation mechanisms in monomeric human glucokinase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain.Angewandte Chemie (International ed. in English) · 2015Article
- Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study.Intrinsically disordered proteins · 2015Article
- Analysis of the co-operative interaction between the allosterically regulated proteins GK and GKRP using tryptophan fluorescence.The Biochemical journal · 2014Article
- A phospho-BAD BH3 helix activates glucokinase by a mechanism distinct from that of allosteric activators.Nature structural & molecular biology · 2014Article
- Dynamic localization of glucokinase and its regulatory protein in hypothalamic tanycytes.PloS one · 2014Article
- Conformational transition pathway in the activation process of allosteric glucokinase.PloS one · 2013Article
- Thermal stability of glucokinase (GK) as influenced by the substrate glucose, an allosteric glucokinase activator drug (GKA) and the osmolytes glycerol and urea.Biochimica et biophysica acta · 2012Article
- Insights into mechanism of glucokinase activation: observation of multiple distinct protein conformations.The Journal of biological chemistry · 2012Article
- A novel type of allosteric regulation: functional cooperativity in monomeric proteins.Archives of biochemistry and biophysics · 2012Review
- Homotropic allosteric regulation in monomeric mammalian glucokinase.Archives of biochemistry and biophysics · 2012Review
- Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase.PLoS biology · 2012Article
- Mutational analysis of allosteric activation and inhibition of glucokinase.The Biochemical journal · 2011Article
- Binding of ATP at the active site of human pancreatic glucokinase--nucleotide-induced conformational changes with possible implications for its kinetic cooperativity.The FEBS journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Human pancreatic glucokinase is a monomeric enzyme that displays kinetic cooperativity, a feature that facilitates enzyme-mediated regulation of blood glucose levels in the body. Two theoretical models have been proposed to describe the non-Michaelis-Menten behavior of human glucokinase. The mnemonic mechanism postulates the existence of one thermodynamically favored enzyme conformation in the absence of glucose, whereas the ligand-induced slow transition model (LIST) requires a preexisting equilibrium between two enzyme species that interconvert with a rate constant slower than turnover. To investigate whether either of these mechanisms is sufficient to describe glucokinase cooperativity, a transient-state kinetic analysis of glucose binding to the enzyme was undertaken. A complex, time-dependent change in enzyme intrinsic fluorescence was observed upon exposure to glucose, which is best described by an analytical solution comprised of the sum of four exponential terms. Transient-state glucose binding experiments conducted in the presence of increasing glycerol concentrations demonstrate that three of the observed rate constants decrease with increasing viscosity. Global fit analyses of experimental glucose binding curves are consistent with a kinetic model that is an extension of the LIST mechanism with a total of four glucose-bound binary complexes. The kinetic model presented herein suggests that glucokinase samples multiple conformations in the absence of ligand and that this conformational heterogeneity persists even after the enzyme associates with glucose.
Indexed as
Identifiers
What OpenQuestion holds
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.