Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus

Article Abstract:

The pET11-d system helps express the gdhA gene encoding the hexameric glutamate dehydrogenase (GDH) from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli. Equal amounts of monomeric and hexameric forms constitute the recombinant GDH, as revealed by molecular exclusion chromatography. Heat treatment increases the GDH activity by inducing in vitro assembly of inactive monomers into hexamers in the recombinant GDH. Both recombinant enzyme and native enzyme from P. furiosus exhibit similar activity, but thermostability is lower for the recombinant GDH compared to native enzyme.

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In vitro reconstruction of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus

Article Abstract:

The main aim of the study is to obtain the recombinant form of Pyrococcus furiosus NAD(P)H:rubredoxin oxidoreductase (NROR), to reconstitute an in vitro recombinant superoxide reduction pathway and to show that NADPH can serve as an electron source for superoxide reduction to peroxide. It is demonstrated that the complete pathway from NAD(P)H to reduction of superoxide reductase (SOR) via NROR and rubredoxin can be reconstituted in an in vitro recombinant system.

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Changes in the catalytic properties of Pyrococcus furiosus thermostable amylase by mutagenesis of the substrate binding sites

Article Abstract:

The effects of the mutagenesis of the substrate binding sites on the various catalytic properties of Pyrococcus furiosus thermostable amylase (TA), a cyclodextrin-degrading (CD) enzyme, are analyzed.

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