title: Engineering thermostability in archaebacterial glyceraldehyde-3-phosphate dehydrogenase. Hints for the important role of interdomain contacts in stabilizing protein conformation.
abstract: Construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantii 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 alpha 3-helix of eubacterial and eukaryotic 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 interactions play an important role in these contacts.
authors: Max-Planck-Institut für Biochemie, Martinsried, FRG.
authors: J
authors: J
authors: Biro
authors: S
authors: S
authors: Fabry
authors: W
authors: W
authors: Dietmaier
authors: C
authors: C
authors: Bogedain
authors: R
authors: R
authors: Hensel
mesh_terms: D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004252:DNA Mutational Analysis; D005818:Genetic Engineering; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000235:genetics*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D009841:Oligonucleotides / Q000235:genetics; D011489:Protein Denaturation; D013329:Structure-Activity Relationship
chemical_list: D009841:Oligonucleotides; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases