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Cold adapted enzymes
1Protein Crystallography Group, Department of Chemistry, Faculty of Science, University of Tromsø, N-9037 Tromsø, Norway. arne.smalas@chem.uit.no
Biotechnology Annual Review
|February 24, 2001
Summary
Enzymes from cold-adapted organisms show varied strategies for low-temperature function, often trading thermal stability for high catalytic efficiency. Structural analysis reveals no single feature explains this cold adaptation, with diverse molecular adjustments employed.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Reports on cold-adapted enzymes have surged, highlighting diverse low-temperature functional strategies.
- Cold-active enzymes often exhibit high catalytic efficiency but reduced thermal stability.
- Limited 3D structures hinder rationalization of cold adaptation mechanisms.
Purpose of the Study:
- To summarize structural characteristics of cold-adapted enzymes.
- To identify common structural features related to cold activity and stability.
- To explore adaptive strategies beyond increased molecular flexibility.
Main Methods:
- Comparative analysis of crystal structures (7), homology models (7), and amino acid sequences (24).
- Examination of structural features influencing stability (e.g., hydrogen bonds, ion-pairs, amino acid content, surface properties, helix stability, core packing).
Main Results:
- No single common structural feature explains the cold adaptation of enzymes.
- Each cold-adapted enzyme utilizes unique structural adjustments for flexibility, efficiency, and stability.
- A correlation exists between cold adaptation and reduced inter-domain/subunit interactions.
- Optimization of active site electrostatics contributes to increased catalytic activity.
Conclusions:
- Cold adaptation in enzymes is achieved through diverse, enzyme-specific structural modifications.
- Reduced inter-domain/subunit interactions and optimized active site electrostatics are key features.
- Understanding these varied strategies is crucial for enzyme engineering and biotechnology.