Structural stabilities and activities
We show in this paper that triosephosphate isomerase (TIM) cloned and produced from two different hyperthermophile archaeal genomes catalyse the interconversion of glyceraldehyde-3-phosphate (G3P) and dihyroxyacetone phosphate (DHAP) at rates that are equal to, or exceed, the theoretically-predicted limits for this category of enzyme, when the temperature of assaying is close to the optimal temperatures of function of these enzymes. Thus, we call them ‘super-perfect’ enzymes, because TIM enzymes are known as perfect enzymes, which are the most efficient of enzymes known to man.