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The enzymatic and crystallographic properties of the P168A variant of trypanosomal triosephosphate isomerase (TIM) are analyzed to investigate the importance of the fully conserved active site proline, Pro168, for the reaction mechanism of TIM. The results have shown that the presence of the proline side chain is required for transmitting the signal of ligand binding and loop 6 closure to the Glu167 side chain.

Throughout history, we have looked to nature to discover and copy pharmaceutical solutions to prevent and heal diseases. Due to the advances in metabolic engineering and the production of pharmaceutical proteins in different host cells, we have moved from mimicking nature to the delicate engineering of cells and proteins. We can now produce novel drug molecules, which are fusions of small chemical drugs and proteins. Currently we are at the brink of yet another step to venture beyond nature's border with the use of unnatural amino acids and manufacturing without the use of living cells using cell-free systems. In this review, we summarize the progress and limitations of the last decades in the development of pharmaceutical protein development, production in cells, and cell-free systems. We also discuss possible future directions of the field.