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. 1985 Oct;164(1):456-60.
doi: 10.1128/jb.164.1.456-460.1985.

Identification of the active site in penicillin-binding protein 3 of Escherichia coli

R A Nicholas, J L Strominger, H Suzuki, Y Hirota

Identification of the active site in penicillin-binding protein 3 of Escherichia coli

R A Nicholas et al. J Bacteriol. 1985 Oct.

Abstract

We report the sequence of the active site tryptic peptide of penicillin-binding protein 3 from Escherichia coli. Purified penicillin-binding protein 3 was labeled with [14C]penicillin G and digested with trypsin, and the resulting radioactive peptides were isolated by a combination of gel filtration and high-pressure liquid chromatography. The major radioactive peak from high-pressure liquid chromatography was sequenced, and the peptide Thr-Ile-Thr-Asp-Val-Phe-Glu-Pro-Gly-Ser-Thr-Val-Lys, which comprises residues 298 to 310 in the amino acid sequence, was identified. This sequence is compared with the active site sequences from other penicillin-binding proteins and beta-lactamases.

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