Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima.

Abstract excerpt

The role of an ionic network of four charged amino acid side-chains in the thermostability of the enzyme D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima (TmGAPDH) has been assessed by site-directed mutagenesis, replacing the central residue of the ionic network, arginine 20, by either alanine (R20A) or asparagine (R20N). The purified mutant enzymes display no...

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