Open AccessPenicillin‐degrading activities of peptides from pneumococcal penicillin‐binding proteins
Author(s) -
ELLERBROK Heinz,
HAKENBECK Regine
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb13779.x
Subject(s) - penicillin binding proteins , peptide , biochemistry , trypsin , penicillin , chemistry , streptococcus pneumoniae , hydrolysis , microbiology and biotechnology , biology , enzyme , antibiotics
Trypsin treatment of native penicillin‐binding proteins (PBPs) 1a, 2 b and 3 from Streptococcus pneumoniae resulted in the formation of stable peptides containing the β‐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 β‐lactams with similar rates compared to the intact PBP, the turnover rate of fragment IIb 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.