Altering enzymatic activity: recruitment of carboxypeptidase activity into an RTEM beta-lactamase/penicillin-binding protein 5 chimera.

doi:10.1073/pnas.87.7.2823

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Article

Altering enzymatic activity: recruitment of carboxypeptidase activity into an RTEM beta-lactamase/penicillin-binding protein 5 chimera.

Proceedings of the National Academy of Sciences of the United States of America - 1 Apr 1990

Chang Y H, Labgold M R, Richards J H

Abstract excerpt

The D-Ala-D-Ala carboxypeptidases/transpeptidases (penicillin-binding proteins, PBPs) share considerable structural homology with class A beta-lactamases (EC 3.5.2.6), although these beta-lactamases have no observable D-Ala-D-Ala carboxypeptidase activity. With the objective of recruiting such activity into a beta-lactamase background, we have prepared a chimeric protein by inserting a 28-amino acid segment of...

Topics

Alanine
Amino Acid Sequence
Bacterial Proteins
Blotting, Western
Carrier Proteins
Chimera
Escherichia coli
Genes, Bacterial
Hexosyltransferases
Kinetics
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Muramoylpentapeptide Carboxypeptidase

Mutation

Penicillin-Binding Proteins

Peptidyl Transferases

Plasmids

Sequence Homology, Nucleic Acid

Substrate Specificity

Source

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Identifiers

PMID: 2181451
DOI: 10.1073/pnas.87.7.2823
PMCID: PMC53783

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2181451-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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