Jaenicke, Rainer (1993) Structure—Function Relationship of Hyperthermophilic Enzymes. In: Biocatalyst Design for Stability and Specificity. ACS Symposium Series (516). AMER CHEMICAL SOC, WASHINGTON, pp. 53-67. ISBN 9780841225183, 9780841213722
Full text not available from this repository.Abstract
The upper limit of thermal adaptation in the biosphere (almost-equal-to 110-degrees-C) coincides with the temperature where hydrophobic hydration vanishes and biomolecules start undergoing hydrothermal decomposition. Regarding T(max), hyperthermophilic microorganisms come close to this limit. Thermotoga maritima (T(opt) less-than-or-equal-to 90-degrees-C) has adapted its cellular inventory to T greater-than-or-equal-to 100-degrees-C. Enzymes purified to homogeneity show intrinsic stability up to almost-equal-to 110-degrees-C. Their overall properties at physiological temperature resemble those of their mesophilic counterparts: Mutative adaptation tends to maintain ''corresponding states'' regarding structure, flexibility and ligand binding. Physical, enzymatic and folding properties of glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase and amylase are discussed. Enhanced stability may be ascribed to improved packing and enhanced ligand and/or subunit interactions. Due to the minute adaptive changes in DELTAG no general strategy of thermophilism can be given.
| Item Type: | Book Section |
|---|---|
| Uncontrolled Keywords: | EUBACTERIUM THERMOTOGA-MARITIMA; LACTATE-DEHYDROGENASE; PROTEIN-STRUCTURE; STABILITY; TEMPERATURE; BIOMOLECULES |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Petra Gürster |
| Date Deposited: | 16 May 2024 06:41 |
| Last Modified: | 16 May 2024 06:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54162 |
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