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Resumo(s)
Human carboxylesterase 2 (hCES2) is becoming more relevant due to its role in the hydrolysis of several drugs, pro-drugs and xenobiotics. However, its three dimensional structuture is yet to be resolved, and many of its properties are still unclear.
In this work, the impact of glycosylation in the enzymatic activity of an hCES2 variant, hCES2-10xHis, was evaluated. To achieve this objective, different methods were used, such as enzymatic deglycosylation and glycosylation inhibition through specific inhibitors or plasmid mutation.
It was concluded that glycosylation is necessary during hCES2 synthesis to maintain protein activity, but the presence of the glycans is not essential after the protein is completely matured.
Descrição
Dissertação para obtenção do Grau de Mestre em
Genética Molecular e Biomedicina
Palavras-chave
Carboxylesterase Glycosylation Deglycosylation PNGase F Tunicamycin Site directed mutagenesis
