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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Nov;69(11):3355–3359. doi: 10.1073/pnas.69.11.3355

Role of the Penicillin-Sensitive Transpeptidation Reaction in Attachment of Newly Synthesized Peptidoglycan to Cell Walls of Micrococcus luteus

David Mirelman 1, Rivka Bracha 1, Nathan Sharon 1
PMCID: PMC389770  PMID: 4343965

Abstract

Cell-wall preparations of Micrococcus luteus (lysodeikticus) catalyze in vitro peptidoglycan synthesis from UDP N-acetyl-D-glucosamine, UDP N-acetylmuramic acid-pentapeptide, and glycine. Newly synthesized peptidoglycan is partially cross-linked by a transpeptidation reaction with concomitant release of C-terminal D-alanine. Penicillin not only strongly inhibits release of D-alanine (98% at 1 μg/ml), but also markedly inhibits incorporation of acetylglucosamine and N-acetylmuramic acid-pentapeptide into the preformed cell-wall peptidoglycan. The simplest explanation for the results is that incorporation of newly synthesized strands of peptidoglycan and their attachment to “older” cell-wall peptidoglycan proceeds mainly by transpeptidation and that transglycosylation is responsible only for part of the elongation of the pre-existing peptidoglycan. Another possibility is that incorporation occurs by transglycosylation, but it cannot continue without concurrent formation of peptide cross-bridges.

Keywords: bacterial cell-wall biosynthesis, transglycosylation, β-lactam antibiotics

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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