Serine Carboxpeptidase II (SCP) is a proteolytic enzyme that cleaves the C-terminal residue of polypeptides. The enzymatic activity of SCP is conducive with a catalytic triad which functions at the active site. A similar enzyme, serine protease (serine endopeptidase) cleaves peptide bonds using an analogous catalytic mechanism via the catalytic triad. Protein structure in most cases dictates its enzymatic properties but this phenomenon is not observed between serine carboxypeptidase and serine protease. To determine if these proteins, similar in structure but different in function, model convergent evolution, kinetics of SCP must be studied. The SCP gene was amplified via PCR and ligated into the pGEM-T vector, a non-expression vector. The current goal of this project is to reisolate the SCP gene, ligate it into a pET-32c expression vector, and purify the protein. To-date, the SCP gene has been isolated from the pGEM-T vector using a restriction enzyme digestion and purification.

Coning methodology for serine carboypeptidase II

243rd National Meeting (2012)

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