ArticleIntrinsically disordered proteins2015
Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study.
Article in Intrinsically disordered proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- The Disordered Amino Terminus of the Circadian Enzyme Nocturnin Modulates Its NADP(H) Phosphatase Activity by Changing Protein Dynamics.Biochemistry · 2022Article
- Intrinsically Disordered Proteins: Critical Components of the Wetware.Chemical reviews · 2022Review
- Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.Journal of molecular biology · 2020Article
- Presence and structure-activity relationship of intrinsically disordered regions across mucins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils.The Journal of biological chemistry · 2019Article
- Active Site Breathing of Human Alkbh5 Revealed by Solution NMR and Accelerated Molecular Dynamics.Biophysical journal · 2018Article
- The relationship between folding and activity in UreG, an intrinsically disordered enzyme.Scientific reports · 2017Article
- Structural pliability adjacent to the kinase domain highlights contribution of FAK1 IDRs to cytoskeletal remodeling.Biochimica et biophysica acta. Proteins and proteomics · 2017Article
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Authors and funding
3 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Many human proteins are predicted to contain intrinsically disordered regions (IDRs), yet their occurrence in enzymes is notably rare. Human pancreatic glucokinase (GCK) is one of a small, but growing number of enzymes shown to possess an IDR. In this commentary, we summarize the results of recent biophysical studies that provide evidence for a functionally significant disorder-order transition within the IDR of GCK during the enzyme's catalytic cycle. High-resolution NMR studies indicate that kinetic cooperativity in GCK results from glucose-mediated millisecond conformational dynamics within the structurally heterogeneous and partially disordered small domain of this monomeric enzyme, whereby the precise timescale of these motions is critical for the manifestation of the kinetic cooperativity effect. GCK provides an excellent case study for understanding how structural and dynamic alterations within an IDR enable novel regulatory mechanisms. These studies also establish GCK as a model system for investigating the functional consequences of disorder and conformational heterogeneity in enzymatic systems in general.
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