PMID: 9655930Jul 10, 1998Paper

The pyruvate dehydrogenase complex from thermophilic organisms: thermal stability and re-association from the enzyme components

Biochimica Et Biophysica Acta
S Witzmann, H Bisswanger

Abstract

Examples of pyruvate dehydrogenase complexes, and of its probable precursors, the pyruvate ferredoxin oxidoreductases, both isolated from thermophilic organisms, are described. The pyruvate ferredoxin oxidoreductases are mostly characterized from thermophilic archaea like Sulfolobus solfataricus and Pyrococcus furiosus. They retain their catalytic activity up to 60 and 90 degreesC, respectively. Characteristic for the thermophilic nature is a biphasic temperature behavior, reflecting a more stable low temperature and a metastable high temperature form. Another feature is the strong binding of the cofactor thiamin diphosphate. Detailed analysis of thermostable pyruvate dehydrogenase complexes so far only exist for the enzymes from Bacillus stearothermophilus and Thermus flavus. In most respects, especially in the structural features, the enzyme complex from B. stearothermophilus resembles its mesophilic counterparts and only an elevated temperature maximum for the catalytic activity reveals the thermophilic nature. In contrast to this, the more thermostable enzyme complex from T. flavus shows a quite distinct behavior. One single protein chain (Mr=100 kDa) instead of an alpha2beta2 aggregate was found for the pyruvate dehydrogen...Continue Reading

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Citations

Jan 22, 2009·Extremophiles : Life Under Extreme Conditions·Felipe CavaJosé Berenguer
Sep 24, 2013·Metabolic Engineering·Borimas KrutsakornHisao Ohtake
Mar 4, 2014·Journal of Food Science and Technology·Masomeh GhassemAbdul Salam Babji

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