Peptidoglycan Carboxypeptidase and Endopeptidase Activities of NCIB 9365 Free

Abstract

The D,D-carboxypeptidase of was exclusively associated with the proto-plast membrane. The enzyme had a pH optimum of 4.9 and was sensitive to thiol reagents. The D, D-carboxypeptidase was stimulated by most divalent cations, Pb and Cd providing the greatest degree of activation, but it was inhibited by Hg and Fe. A particulate L, D-carboxypeptidase was demonstrated in membrane preparations which were also able to catalyse a simple transpeptidation reaction employing D-alanine as the carboxyl acceptor. An endopeptidase activity capable of liberating D-alanyl-D-alanine from UDP-N-acetylmuramyl-L-Alanyl-y-γ-D-glutamy--2,6-diaminopimelyl-D-alanyl-D-alanine (UDP-MurNAc-pentapeptide) was present in the cytoplasm. This appeared to be the reverse reaction of the D-alanyl-D-alanine-adding enzyme responsible for the generation of the peptidoglycan precursor UDP-MurNAc-pentapeptide.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-111-2-327
1979-04-01
2024-03-29
Loading full text...

Full text loading...

/deliver/fulltext/micro/111/2/mic-111-2-327.html?itemId=/content/journal/micro/10.1099/00221287-111-2-327&mimeType=html&fmt=ahah

References

  1. BARNETH T.J. D-Alanine carboxypeptidases of Bacillus stearothermophilus: solubilization of particulate enzymes and mechanism of action of penicillin.. Biochimica et biophysica acta 1973; 304:332–352
    [Google Scholar]
  2. BLUMBERG P.M., STROMINGER J.L. Interaction of penicillin with the bacterial cell: penicillin binding proteins and penicillin-sensi tive enzymes. Bacteriological Reviews 1974; 38:291–335
    [Google Scholar]
  3. CARPENTER C.V., NEUHAUS F.C. Enzymatic synthesis of D-alanyl-malanine. Two binding modes for product on D-alaninemalanine ligase (ADP).. Biochemistry 1972; 11:2594–2598
    [Google Scholar]
  4. DIAZ-MAURIÑO T., NIETO M ., PERKINS H.R. Membrane-bound D,D-carboxypeptidases from Bacillus megaterium KM. Biochemical Journal 1974; 143:391–402
    [Google Scholar]
  5. DIXON M., WEBB E.C. Enzymes. 2nd edn 1964 pp Lonon: Longmans Green & Co.;
    [Google Scholar]
  6. EGAN A ., LAWRENCE P. J., STROMINGER J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. V. Co2+-dependent reversal of peptide bond formation. Journal of Biological Chemistry 1973; 248:3122–3130
    [Google Scholar]
  7. FARKAS W.R. The effects of plumbousion on protein biosynthesis in reticulocytes. Research Communications in Chemical Pathology and Pharmacology 1975; 10:127–148
    [Google Scholar]
  8. HUYSEN J.M., LÉYH-BOUILLE M., FRÈRJE. ,M ., , DUSART J., MARQUET A. PERKINS H.R., NIETO M. The penicillin receptor in Streptomyces. Annals of the New York Academy of Sciences 1974; 235:236–266
    [Google Scholar]
  9. GHUYSEN J.M. The concept of the penicillin target from 1965 until today. Journal of General Microbiology 1977; 101:13–33
    [Google Scholar]
  10. GONDRÉ G., FLOURET B, VAN HEIJENOORT J. Release of D-alanyl-D-alanine from the precursor of the cell wall peptidoglycan by a peptidase of Escherichia coli k12 . Biochimie 1973; 53:685–691
    [Google Scholar]
  11. IZAKI K., MATSUHASHI M., STROMINGEJR L . Biosynthesis of the peptidoglycan of bacterial cell walls. XIII. Peptidoglycan transpeptidase and D-alanine carboxypeptidase : penicillin- sensitive enzymatic reactions in strains of Escherichia coli . Journal of Biological Chemistry 1968; 243:3180–3192
    [Google Scholar]
  12. LOWRY O.H., ROSEBROUGH N.J., FARR A.L., RANDALL R.J. Protein measurementwith the Folin phenol reagent. Journal of Biological Chemistry 1951; 193:265–275
    [Google Scholar]
  13. MARQUET A., NIETO M., DIAZ-MAURIÑO. Membrane-bound D,D-carboxypeptidase and transpeptidase activities from Bacillus megaterium KM at pH 7.. European Journal of Biochemistry 1976; 68:581–589
    [Google Scholar]
  14. MIZUNO Y ., ITO E. Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D - glutamate: meso-2,6 - diaminopimelate ligase.. Journal of Biological Chemistry 1968; 243:2265–2672
    [Google Scholar]
  15. NATHENSON S. G., STROMINGER J.L ., ITO E. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. IV. Purification and properties of D-glutamic acid-adding enzyme. Journal of Biological Chemistry 1964; 239:1773–1776
    [Google Scholar]
  16. NGUYEN-DISTÈCHE M., GHUYSEN J.M., POLLOCK J. J., REYNOLDS P.E., PERKINS H.R., COYETTE J., SALTON M.R.J. Enzymes involved in wall peptide cross-linking in Escherichia coli K12, strain 44. European Journal of Biochemistry 1974; 41:447–455
    [Google Scholar]
  17. OPPENHEIM B., PATCHORNIK A. Formation of D-alanyl m-alanine and D-alanine from UDPMurNAc-L-Ala-D-isoGlu-L-Lys-D-Ala-D-Ala by extracts of Staphylococcus aureus and Streptococcus faecalis . FEBS Letters 1974; 45:172–175
    [Google Scholar]
  18. REYNOLDS P.E. Peptidoglycan synthesis in bacilli. I. Effect of temperature on the in vitro system from Bacillus megaterium and Bacillus stearothermophilus.. Biochimica et biophysica acta 1971; 237:239–254
    [Google Scholar]
  19. REYNOLDS P.E., BARNETT H.J. Transpeptidases and D,D-carboxypeptidases in bacilli. Annals of the New York Academy of Sciences 1974; 235:269–282
    [Google Scholar]
  20. SABBIONI E., GIRARDI F., MARAFANT E. Replacement of metal in metalloenzymes. A leadalkaline phosphatase. Biochemistry 1976; 15:271–276
    [Google Scholar]
  21. SHEPHERD S.T., CHASE H . A., REYNOLDS P. E. The separation and properties of two penicillin-binding proteins from Salmonella typhimurium . European Journal of Biochemistry 1977; 78:521–532
    [Google Scholar]
  22. STICKLAND L.H. The activation of phosphoglucomutase by metal ions.. Biochemical Journal 1949; 44:190–197
    [Google Scholar]
  23. TAMURA T. , IMAE Y., STROMINGER J.L. Purification to homogeneity and properties of two D-alanine carboxypeptidases 1 from Escherichia coli . Journal of Biological Chemistry 1976; 251:414–423
    [Google Scholar]
  24. UMBREIT J.N., STROMINGER J.L. DAlanine carboxypeptidase from Bacillus subtilis membranes. I. Purification and characterization.. Journal of Biological Chemistry 1973; 248:6759–6766
    [Google Scholar]
  25. VALLEE B.L., ULMER D.D. Biochemical effects of mercury, cadmium, and lead. Annual Review of Biochemistry 1972; 41:91–128
    [Google Scholar]
  26. WICKUS G.G., STROMINGER J.L. Penicillin-sensi tive transpeptidation during peptidoglycan biosynthesis in cell-free preparations from Bacillus megaterium. I. Incorporation of free diaminopimelic acid into peptidoglycan.. Journal of Biological Chemistry 1972; 247:5297–5306
    [Google Scholar]
  27. YOCUM R.R., BLUMBERG P.M., STROMING J. L. Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of Bacillus stearothermophilus . Journal of Biological Chemistry 1974; 249:4863–4871
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-111-2-327
Loading
/content/journal/micro/10.1099/00221287-111-2-327
Loading

Data & Media loading...

Most cited Most Cited RSS feed