Engineering thermostability in archaebacterial glyceraldehyde‐3‐phosphate dehydrogenase Hints for the important role of interdomain contacts in stabilizing protein conformation

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Abstract
Construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantil and the thermophilic Methanothermus fervidus by recombinant DNA techniques revealed that a short C-terminal fragment of the Mt.fervidus enzyme contributes largely to its thermostability. This C-terminal region appears to be homologous to the α6-helix of cubacterial and eukaryotie glyceraldehyde-3-phosphate dehydrogenases which is involved in the contacts between the two domains of the enzyme subunit. Site-directed mutagenesis experiments indicate that hydrophobic interaction play an important role in these contacts.