ArticleProtein science : a publication of the Protein Society2025
Structural mechanisms for cold-adapted activity of phosphoenolpyruvate carboxykinase.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Structural mechanisms for cold-adapted activity of phosphoenolpyruvate carboxykinase.Protein science : a publication of the Protein Society · 2025Article
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4 authors.
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Abstract
Temperature is a critical factor in enzyme function, as most enzymes are thermally activated. Across Earth's diverse environments (-20 to 120°C), enzymes have evolved to function optimally at their organism's growth temperature. Thermophilic enzymes must resist denaturation, while psychrophilic enzymes must maintain activity with limited thermal energy. Although principles underlying thermostability are well established, the mechanisms governing kinetic adaptation to temperature remain less understood. To investigate this, we characterized the kinetics and determined a comprehensive series of X-ray crystal structures of a psychrophilic, GTP-dependent phosphoenolpyruvate carboxykinase (PEPCK) bound to substrates and non-reactive mimics of the reaction coordinate. These structures were compared to those of a mesophilic PEPCK. PEPCK is a dynamic enzyme requiring substantial conformational changes during catalysis, particularly ordering of the active site Ω-loop lid. The psychrophilic enzyme exhibited a reduced catalytic efficiency (k
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