d -Alanine Carboxypeptidase and Cell Wall Cross-Linking in Bacillus subtilis-Reference-Cited by-同舟云学术

d -Alanine Carboxypeptidase and Cell Wall Cross-Linking in Bacillus subtilis

Published:1974-02 Issue:2 Volume:117 Page:926-927
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Sharpe Arlene¹,Blumberg Peter M.¹,Strominger Jack L.¹

Affiliation:

1. The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138

Abstract

Inhibition of d -alanine carboxypeptidase in Bacillus subtilis by 95% caused no measurable change in the degree of cross-linking of the peptidoglycan.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.117.2.926-927.1974

Reference7 articles.

1. Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis;Blumberg P. M.;Proc. Nat. Acad. Sci. U.S.A.,1971

2. Symposium on the fine structure and replication of bacteria and their parts. III. Bacterial cell-wall replication followed by immunofluorescence;Cole R. M.;Bacteriol. Rev.,1965

3. N-acetylmuramyl-L-alanine amidase of Bacillus licheniformis and its L-form;Forsberg C. W.;J. Bacteriol.,1972

4. Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two o-alanine carboxypeptidases from Escherichia coli;Izaki K.;J. Biol. Chem.,1968

5. Biosynthesis of the peptidoglycan of bacterial cell walls. XIII. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of Escherichia coli;Izaki K.;J. Biol. Chem.,1968

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