Chemical Function of Substituted Amino Acids in Glyceraldehyde-3-Phosphate Dehydrogenase
Final rept. 25 Sep 1987-15 Sep 1991
HOUSTON UNIV TX
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An investigation of the amino acids responsible for the thermostability of the T. aquaticus glyceraldehyde-3-phosphate dehydrogenase GAPDH was initiated. The gene encoding this enzyme was isolated from a genomic library and sequenced. The gene encoded a functional GAPDH by virtue of its ability to rescue a mutant bacterial strain whose own GAPDH gene was deleted. The heat-stability of the isolated enzyme is impressive, i.e., it retains 100 of its activity after 2 hours at 90 C while requiring 100 C to lose 50 of its activity. Defining the conditions for crystallization as well as the physicochemical properties of the purified GAPDH are currently ongoing.
- Medicine and Medical Research