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Role of the penicillin-sensitive transpeptidation reaction in attachment of newly synthesized peptidoglycan to cell walls of Micrococcus luteus.

Authors
  • Mirelman, D
  • Bracha, R
  • Sharon, N
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
Nov 01, 1972
Volume
69
Issue
11
Pages
3355–3359
Identifiers
PMID: 4343965
Source
Medline
License
Unknown

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 mug/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.

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