Sequences of the active-site peptides of three of the high-Mr 
penicillin-binding proteins of Escherichia coli K-12

Keck, W; Glauner, B; Schwarz, U; Broome-Smith, JK; Spratt, BG

doi:10.1073/pnas.82.7.1999

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Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12

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Keck, W
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Glauner, B
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Schwarz, U
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Keck, W., Glauner, B., Schwarz, U., Broome-Smith, J., & Spratt, B. (1985). Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12. Proceedings of the National Academy of Sciences of the United States of America, 82(7), 1999-2003. doi:10.1073/pnas.82.7.1999.

Cite as: https://hdl.handle.net/21.11116/0000-000C-6D91-6

Abstract

The amino acid compositions of the radioactive peptides obtained from trypsin digestion of [14C]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. Comparison of the compositions of the penicillin-labeled peptides with the complete amino acid sequences of PBPs 1A, 1B, and 3 showed that the acylated serine occurs near the middle of each of the proteins, within the conserved sequence Gly-Ser-Xaa-Xaa-Lys-Pro. The sequence around the acylated serine of these high Mr PBPs shows little similarity to that around the acylated serine of the low-Mr PBPs (D-alanine carboxypeptidases) or of the class A or class C beta-lactamases, except that in all of these enzymes which interact with penicillin the acylated serine residue occurs within the sequence Ser-Xaa-Xaa-Lys.