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Updated: Sep 17, 2025
09:42
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
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Fuzziness in enzymatic catalysis
Sachin S Katti1, Tvesha Parikh2, Rachel J Godek2
1Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030, USA.
Current Opinion in Structural Biology
|June 28, 2025
Summary
Intrinsically disordered proteins utilize dynamic
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Intrinsically disordered proteins/regions (IDPs/IDRs) are crucial for cellular processes.
- Dynamic charge:charge interactions, termed 'fuzzy' interactions, are characteristic of IDPs/IDRs.
- These interactions are vital for enzymatic regulation and substrate recruitment in protein kinases and phosphatases.
Purpose of the Study:
- To review recent advancements in understanding fuzzy interactions.
- To elucidate the role of inter- and intramolecular fuzzy interactions in enzyme assembly, activation, and substrate recruitment.
- To highlight a novel mechanism of protein inhibition involving fuzzy interactions with active site metals.
Main Methods:
- Literature review of recent research on intrinsically disordered proteins and fuzzy interactions.
- Analysis of studies focusing on protein kinases, phosphatases, and their regulators/substrates.
- Examination of specific examples of fuzzy interactions in enzyme regulation and inhibition.
Main Results:
- Fuzzy interactions mediate enzyme assembly, activation, and substrate recruitment for kinases and phosphatases.
- Inter- and intramolecular fuzzy interactions are key to these regulatory processes.
- A unique inhibitory mechanism involving dynamic fuzzy interactions between protein phosphatases and active site metals has been identified.
Conclusions:
- Fuzzy interactions are fundamental to the function of intrinsically disordered proteins in enzyme regulation.
- These interactions provide a versatile mechanism for controlling kinase and phosphatase activity.
- The identified inhibitory mechanism offers new insights into protein regulation and potential therapeutic targets.
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