ArticleArchives of biochemistry and biophysics2025
Identification of residues mediating homotropic regulation in human hexokinase 3 reveals a common allosteric interface shared with hexokinase 1.
Article in Archives of biochemistry and biophysics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Phylogenetic investigation of the 100 kDa hexokinase enzyme family with the topiary ancestral sequence reconstruction pipeline.Protein science : a publication of the Protein Society · 2026Article
- Characterization and Inhibition of Human Hexokinase Domain Containing Protein 1 Reveals an Enzyme with Unique Catalytic and Regulatory Traits.ACS chemical biology · 2025Article
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Authors and funding
2 authors.
Funding
Abstract
Vertebrate hexokinases (HKs) display a variety of allosteric phenomena, including activation and inhibition by both homotropic and heterotropic ligands. The extent to which these homologs share a common allosteric mechanism is unknown. A unique trait of the vertebrate hexokinase 3 (HK3) orthologs is substrate inhibition by glucose. Here, we demonstrate that the isolated, regulatory N-terminal domain of human HK3 contains a low affinity glucose binding site whose dissociation constant (3.2 ± 0.4 mM) approximates the K
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