Psychrophilic Enzymes: From Folding to Function and Biotechnology
Psychrophiles thriving permanently at near-zero temperatures synthesize cold-active enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. Most p...
Saved in:
| Main Author: | |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2013-01-01
|
| Series: | Scientifica |
| Online Access: | http://dx.doi.org/10.1155/2013/512840 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832564430173372416 |
|---|---|
| author | Georges Feller |
| author_facet | Georges Feller |
| author_sort | Georges Feller |
| collection | DOAJ |
| description | Psychrophiles thriving permanently at near-zero temperatures synthesize cold-active enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state. Furthermore, a weak temperature dependence of activity ensures moderate reduction of the catalytic activity in the cold. In these naturally evolved enzymes, the optimization to low temperature activity is reached via destabilization of the structures bearing the active site or by destabilization of the whole molecule. This involves a reduction in the number and strength of all types of weak interactions or the disappearance of stability factors, resulting in improved dynamics of active site residues in the cold. These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate. Several open questions in the field are also highlighted. |
| format | Article |
| id | doaj-art-c260fd6d9d554f80b782afa129d442df |
| institution | Kabale University |
| issn | 2090-908X |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Scientifica |
| spelling | doaj-art-c260fd6d9d554f80b782afa129d442df2025-02-03T01:11:10ZengWileyScientifica2090-908X2013-01-01201310.1155/2013/512840512840Psychrophilic Enzymes: From Folding to Function and BiotechnologyGeorges Feller0Laboratory of Biochemistry, Centre for Protein Engineering, Institute of Chemistry, University of Liège, B6a, 4000 Liège, BelgiumPsychrophiles thriving permanently at near-zero temperatures synthesize cold-active enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state. Furthermore, a weak temperature dependence of activity ensures moderate reduction of the catalytic activity in the cold. In these naturally evolved enzymes, the optimization to low temperature activity is reached via destabilization of the structures bearing the active site or by destabilization of the whole molecule. This involves a reduction in the number and strength of all types of weak interactions or the disappearance of stability factors, resulting in improved dynamics of active site residues in the cold. These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate. Several open questions in the field are also highlighted.http://dx.doi.org/10.1155/2013/512840 |
| spellingShingle | Georges Feller Psychrophilic Enzymes: From Folding to Function and Biotechnology Scientifica |
| title | Psychrophilic Enzymes: From Folding to Function and Biotechnology |
| title_full | Psychrophilic Enzymes: From Folding to Function and Biotechnology |
| title_fullStr | Psychrophilic Enzymes: From Folding to Function and Biotechnology |
| title_full_unstemmed | Psychrophilic Enzymes: From Folding to Function and Biotechnology |
| title_short | Psychrophilic Enzymes: From Folding to Function and Biotechnology |
| title_sort | psychrophilic enzymes from folding to function and biotechnology |
| url | http://dx.doi.org/10.1155/2013/512840 |
| work_keys_str_mv | AT georgesfeller psychrophilicenzymesfromfoldingtofunctionandbiotechnology |