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. 1979 Sep;139(3):770–774. doi: 10.1128/jb.139.3.770-774.1979

Escherichia coli murein-DD-endopeptidase insensitive to beta-lactam antibiotics.

W Keck, U Schwarz
PMCID: PMC218021  PMID: 383691

Abstract

A novel endopeptidase degrading the peptide cross-links in sacculi has been isolated from Escherichia coli and purified to homogeneity. The enzyme has a molecular weight of 30,000 and, in contrast to already known enzymes of similar specificity, remains fully active in the presence of beta-lactam antibiotics. In addition, it is exceptional in being inhibited by single-stranded deoxyribonucleic acid and by some polynucleotides. The possible role of the enzyme in cell division is discussed.

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Selected References

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

  1. Hartmann R., Höltje J. V., Schwarz U. Targets of penicillin action in Escherichia coli. Nature. 1972 Feb 25;235(5339):426–429. doi: 10.1038/235426a0. [DOI] [PubMed] [Google Scholar]
  2. Höltje J. V., Mirelman D., Sharon N., Schwarz U. Novel type of murein transglycosylase in Escherichia coli. J Bacteriol. 1975 Dec;124(3):1067–1076. doi: 10.1128/jb.124.3.1067-1076.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Izaki K., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli. J Biol Chem. 1968 Jun 10;243(11):3193–3201. [PubMed] [Google Scholar]
  4. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  5. Lugtenberg B., Meijers J., Peters R., van der Hoek P., van Alphen L. Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands. FEBS Lett. 1975 Oct 15;58(1):254–258. doi: 10.1016/0014-5793(75)80272-9. [DOI] [PubMed] [Google Scholar]
  6. Matsuhashi M., Takagaki Y., Maruyama I. N., Tamaki S., Nishimura Y., Suzuki H., Ogino U., Hirota Y. Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2976–2979. doi: 10.1073/pnas.74.7.2976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Mirelman D., Yashouv-Gan Y., Schwarz U. Peptidoglycan biosynthesis in a thermosensitive division mutant of Escherichia coli. Biochemistry. 1976 May 4;15(9):1781–1790. doi: 10.1021/bi00654a001. [DOI] [PubMed] [Google Scholar]
  8. Nguyen-Distèche M., Pollock J. J., Ghuysen J. M., Puig J., Reynolds P., Perkins H. R., Coyette J., Salton M. R. Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44. Eur J Biochem. 1974 Feb 1;41(3):457–463. doi: 10.1111/j.1432-1033.1974.tb03287.x. [DOI] [PubMed] [Google Scholar]
  9. PELZER H. MUCOPEPTIDHYDROLASEN IN ESCHERICHIA COLI B. II. QUANTITATIVE BESTIMMUNGSVERFAHREN UND SAEULENCHROMATOGRAPHISCHE TRENNUNG EINIGER MUCOPEPTIDHYDROLASEN. Z Naturforsch B. 1963 Nov;18:956–964. [PubMed] [Google Scholar]
  10. PRIMOSIGH J., PELZER H., MAASS D., WEIDEL W. Chemical characterization of mucopeptides released from the E. coli B cell wall by enzymic action. Biochim Biophys Acta. 1961 Jan 1;46:68–80. doi: 10.1016/0006-3002(61)90647-3. [DOI] [PubMed] [Google Scholar]
  11. RICH A., DAVIES D. R., CRICK F. H., WATSON J. D. The molecular structure of polyadenylic acid. J Mol Biol. 1961 Feb;3:71–86. doi: 10.1016/s0022-2836(61)80009-0. [DOI] [PubMed] [Google Scholar]
  12. Ricard M., Hirota Y. Process of cellular division in Escherichia coli: physiological study on thermosensitive mutants defective in cell division. J Bacteriol. 1973 Oct;116(1):314–322. doi: 10.1128/jb.116.1.314-322.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Schwarz U., Asmus A., Frank H. Autolytic enzymes and cell division of Escherichia coli. J Mol Biol. 1969 May 14;41(3):419–429. doi: 10.1016/0022-2836(69)90285-x. [DOI] [PubMed] [Google Scholar]
  14. Strominger J. L., Willoughby E., Kamiryo T., Blumberg P. M., Yocum R. R. Penicillin-sensitive enzymes and penicillin-binding components in bacterial cells. Ann N Y Acad Sci. 1974 May 10;235(0):210–224. doi: 10.1111/j.1749-6632.1974.tb43267.x. [DOI] [PubMed] [Google Scholar]
  15. Tamura T., Imae Y., Strominger J. L. Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli. J Biol Chem. 1976 Jan 25;251(2):414–423. [PubMed] [Google Scholar]
  16. Tomioka S., Matsuhashi M. Purification of penicillin-insensitive DD-endopeptidase, a new cell wall peptidoglycan-hydrolyzing enzyme in Escherichia coli, and its inhibition by deoxyribonucleic acids. Biochem Biophys Res Commun. 1978 Oct 30;84(4):978–984. doi: 10.1016/0006-291x(78)91679-0. [DOI] [PubMed] [Google Scholar]
  17. Verwer R. W., Nanninga N., Keck W., Schwarz U. Arrangement of glycan chains in the sacculus of Escherichia coli. J Bacteriol. 1978 Nov;136(2):723–729. doi: 10.1128/jb.136.2.723-729.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. WEIDEL W., PELZER H. BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS. Adv Enzymol Relat Areas Mol Biol. 1964;26:193–232. doi: 10.1002/9780470122716.ch5. [DOI] [PubMed] [Google Scholar]

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