Circularly permuted beta-lactamase from Staphylococcus aureus PC1

The structure and enzymatic functions of beta-lactamase from Staphylococcus aureus PC1 was evaluated through construction of two circularly permuted proteins, cp228 and cp254. Both have an eight residue long peptide that joins the N- and C- terminal helices of the native molecule with N-terminal residue located on positions 228 and 254, respectively. Cp228 has shown a decrease of activity towards beta-lactam antibiotics and a greater activity towards cefataxime.