SCHULTES, V and JAENICKE, R (1991) FOLDING INTERMEDIATES OF HYPERTHERMOPHILIC D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THERMOTOGA-MARITIMA ARE TRAPPED AT LOW-TEMPERATURE. FEBS LETTERS, 290 (1-2). pp. 235-238. ISSN 0014-5793,
Full text not available from this repository.Abstract
D-Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium, Thermotoga maritima, is extremely thermostable showing a thermal transition beyong 105-degrees-C. At low temperature, 'cold denaturation' becomes detectable only in the presence of destabilizing agents. Reconstitution after preceding denaturation depends on temperature. At 0-degrees-C, no significant recovery of activity is detectable, whereas between 30 and 100-degrees-C reactivation reaches up to 85%. Shifting the temperature from low values to the range of optimum reconstitution releases the trapped intermediate in a fast reaction. Evidence from ultra-centrifugal analysis and far-UV circular dichroism proves the intermediate to be partially assembled to the tetramer, with most of its native secondary structure restored in a fast reaction. Fluorescence emission exhibits at least biphasic kinetics with the rate-limiting step(s) reflecting local adjustments of aromatic residues involved in tertiary contacts in the native state of the enzyme.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; THERMOSTABILITY; PROTEIN; COLD DENATURATION; FOLDING INTERMEDIATE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; THERMOPHILE; THERMOTOGA-MARITIMA |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54860 |
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