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Circularly permuted beta-lactamase from Staphylococcus aureus PC1
- Source :
- Biochemistry. July 22, 1997, Vol. 36 Issue 29, p8767, 8 p.
- Publication Year :
- 1997
-
Abstract
- 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.
Details
- ISSN :
- 00062960
- Volume :
- 36
- Issue :
- 29
- Database :
- Gale General OneFile
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.19788985