ReviewArchives of biochemistry and biophysics2012
Homotropic allosteric regulation in monomeric mammalian glucokinase.
Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- Description of the rate-limiting hydrogen tunneling mechanism for plant 9- and 13-lipoxygenases.Protein science : a publication of the Protein Society · 2026Article
- The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026Review
- β-Carotene alleviates substrate inhibition caused by asymmetric cooperativity.Nature communications · 2025Article
- Conformational flexibility associated with remote residues regulates the kinetic properties of glutamate dehydrogenase.Protein science : a publication of the Protein Society · 2025Article
- Biochemical methods to map and quantify allosteric motions in human glucokinase.Methods in enzymology · 2023Article
- Moonlighting Proteins: The Case of the Hexokinases.Frontiers in molecular biosciences · 2021Review
- Expression and purification of the 5'-nucleotidase YitU from Bacillus species: its enzymatic properties and possible applications in biotechnology.Applied microbiology and biotechnology · 2020Article
- Nanosecond-Timescale Dynamics and Conformational Heterogeneity in Human GCK Regulation and Disease.Biophysical journal · 2020Article
- Mechanistic Origins of Enzyme Activation in Human Glucokinase Variants Associated with Congenital Hyperinsulinism.Biochemistry · 2018Article
- Solution NMR Spectroscopy for the Study of Enzyme Allostery.Chemical reviews · 2016Review
- Measuring specificity in multi-substrate/product systems as a tool to investigate selectivity in vivo.Biochimica et biophysica acta · 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
- A general framework for thermodynamically consistent parameterization and efficient sampling of enzymatic reactions.PLoS computational biology · 2015Article
- Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study.Intrinsically disordered proteins · 2015Article
- Effect of pH on the hydrolytic kinetics of gamma-glutamyl transferase from Bacillus subtilis.TheScientificWorldJournal · 2014Article
- Pathogenesis of chronic hyperglycemia: from reductive stress to oxidative stress.Journal of diabetes research · 2014Review
- Dynamic localization of glucokinase and its regulatory protein in hypothalamic tanycytes.PloS one · 2014Article
- A phospho-BAD BH3 helix activates glucokinase by a mechanism distinct from that of allosteric activators.Nature structural & molecular biology · 2014Article
- Structural basis for regulation of human glucokinase by glucokinase regulatory protein.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Glucokinase catalyzes the ATP-dependent phosphorylation of glucose, a chemical transformation that represents the rate-limiting step of glycolytic metabolism in the liver and pancreas. Glucokinase is a central regulator of glucose homeostasis as evidenced by its association with two disease states, maturity onset diabetes of the young (MODY) and persistent hyperinsulinemia of infancy (PHHI). Mammalian glucokinase is subject to homotropic allosteric regulation by glucose-the steady-state velocity of glucose-6-phosphate production is not hyperbolic, but instead displays a sigmoidal response to increasing glucose concentrations. The positive cooperativity displayed by glucokinase is intriguing since the enzyme functions as a monomer under physiological conditions and contains only a single binding site for glucose. Despite the existence of several models of kinetic cooperativity in monomeric enzymes, a consensus has yet to be reached regarding the mechanism of allosteric regulation in glucokinase. Experimental evidence collected over the last 45 years by a number of investigators supports a link between cooperativity and slow conformational reorganizations of the glucokinase scaffold. In this review, we summarize advances in our understanding of glucokinase allosteric regulation resulting from recent X-ray crystallographic, pre-equilibrium kinetic and high-resolution nuclear magnetic resonance investigations. We conclude with a brief discussion of unanswered questions regarding the mechanistic basis of kinetic cooperativity in mammalian glucokinase.
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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.