Penicillin-degrading activities of peptides from pneumococcal penicillin-binding proteins.

Trypsin treatment of native penicillin-binding proteins (PBPs) 1a, 2b and 3 from Streptococcus pneumoniae resulted in the formation of stable peptides containing the beta-lactam-binding site with molecular masses ranging from 26 kDa to 36 kDa. Whereas the PBP 1a peptide (Ia) was enzymatically rather unstable, the PBP 2b peptide (IIb) and the PBP 3 peptide (III) were able to bind and release beta-lactams with similar rates compared to the intact PBP, the turnover rate of fragment II b was even twice as fast as that observed with PBP 2b. Analysis of the turnover products by thin-layer chromatography revealed that PBP 2b and 3 produced penicilloic acid as well as phenylacetylglycine. On the other hand, with the corresponding tryptic fragments only the hydrolysis product penicilloic acid was obtained.