Exhibited by this model is the enzyme human trioesphosphate isomerase (TPI) bound to a phosphoglycolic acid (PGA) inhibitor in subunit 2 (cyan). The two identical chains of the TPI enzyme are expressed in different detail and colours which is further explained in the annotation. The TPI enzyme is a highly efficient catalyst involved in a key step of glycolysis, performing acid base catalysis to convert DHAP to GAP in a reversible reaction. References (please see the report for proper references): Wierenga, R. K., Kapetaniou, E. G., & Venkatesan, R. (2010). Triosephosphate isomerase: a highly evolved biocatalyst. Wierenga, R. . (2001). The TIM-barrel fold: a versatile framework for efficient enzymes. Mande, S. C., Mainfroid, V., Kalk, K. H., Goraj, K., Martial, J., & Hol, W. G. (1994). Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Kursula, I., & Wierenga, R. K. (2003). Crystal Structure of Triosephosphate Isomerase Complexed with 2-Phosphoglycolate at 0.83-Ã… Resolution.
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