Interesting features of human TPI

3D Model

Triosephosphate isomerase (TPI) was found in 1934 by scientists who were studying the glycolysis pathway in yeast. TPI has been highly conserved and identified in almost every living organism (Meyerhof & Beck, 1944). TPI is an essential protein of the glycolysis pathway, which turns glucose into energy for cells. TPI converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P) and back. In humans, it is important that TPI works correctly, or illness may occur. Here we discuss five interesting features of human TPI that allow for proper catalysis. The features are Loop 6, Asparagine 11, Lysine 13, Histidine 95 and Glutamic acid 165. Shown bound in the active site is transition state analogue 2-phosphoglycolic acid (PGA). We refer to it as substrate and imply it is DHAP and G3P as it creates the same interactions with the active site.
(Mande et al., 1994).

References found in annotations 6 & 7 By Rebecca Jordan & Ayse Kekec