Sequences of the active-site peptides of three of the high-M sub(r) penicillin-binding proteins of Escherichia coli) K-12

The amino acid compositions of the radioactive peptides obtained from trypsin digestion of ( super(14)C)benzylpenicillin-labeled penicillin-binding proteins (PBPs) 1A, 1B, and 3 of Escherichia coli have been obtained. Complete digestion of these peptides with a combination of aminopeptidase M and ca...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1985-01, Vol.82 (7), p.1999-2003
Main Authors: Keck, W, Glauner, B, Schwarz, U, Broome-Smith, J K, Spratt, B G
Format: Article
Language:English
Subjects:
active sites
amino acid sequence
Escherichia coli
penicillin-binding protein
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Summary:The amino acid compositions of the radioactive peptides obtained from trypsin digestion of ( super(14)C)benzylpenicillin-labeled penicillin-binding proteins (PBPs) 1A, 1B, and 3 of Escherichia coli have been obtained. Complete digestion of these peptides with a combination of aminopeptidase M and carboxypeptidase Y showed that benzylpenicillin was bound to a serine residue in each of these proteins.
ISSN:0027-8424