All enzymes need to interact with their substrates or ligands for their catalytic activity. Any larger fusion partners like GST linkde to the enzymes could reduce the interaction efficiency that results a lower enzymatic activity. In some cases, the fusion parners could completely block the interaction and cause the total activity loss. However, there are rarer cases that the recombinant GST fusion enzymes showed slight more activity due to GST enhanced folding during the recombinant expression.
GST forms dimers and this could either lead an increase or decrease in activity depending on whether the fused enzyme is active as a monomer or dimer. GST may impact the oligomerization of the enzyme and hence change catalytic efficiency (Kcat/Km) in unknown ways. If you need stringent enzymatic parameters it is better to cleave GST off of the protein, but this may not be practical in every case.
Thank you very much Dear Liu and Sujay. Could you send me some articles related this issue?
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