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

FEBS Letters

Hensel, Reinhard¹  Dietmaier, Wolfgang¹  Biro, Jutta¹  Bogedain, Christoph¹  Fabry, Stefan¹ 

[1] Max-Planck-Institut für Biochemie, D-8033 Martinsried, FRG

关键词: Thermostability;    Glyceraldehyde-3-phosphate dehydrogenase;    Site-directed mutagenesis;    Chimeric gene;    Hydrophobic interaction;    Archaebacteria;    DSM;    Deutsche Sammlung von Mikroorganismen und Zelikulturen GmbH (Braunschweig;    FRG);    GAPDH;    glyceraldehyde-3-phosphate dehydrogenase;    gap;    gene encoding GAPDH;    Mb;    Methanobacterium;    Mt;    Methanothermus;   

DOI  :  10.1016/0014-5793(90)81456-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown