Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria

Wietzerbin, Juana; Das, Bhupsh C.; Petit, Jean-François; Lederer, Edgar; Leyh-Bouille, Mélina; Ghuysen, Jean-Marie

doi:10.1021/bi00714a008

Article (Scientific journals)

Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria

Wietzerbin, Juana; Das, Bhupsh C.; Petit, Jean-François et al.

1974 • In Biochemistry, 13 (17), p. 3471-3476

Peer Reviewed verified by ORBi

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https://hdl.handle.net/2268/85178

DOI
10.1021/bi00714a008

PubMed
4210702

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Keywords :

alanine analysis; amino acids analysis; amino acids dicarboxylic analysis; carboxypeptidases; cell wall analysis; chemical phenomena; chemistry; dipeptides analysis isolation & purification; electrophoresis paper; glutamates analysis; hydrogen-ion concentration; hydrolysis; mass spectrometry; mitosporic fungi enzymology; muramidase; mycobacterium analysis; mcobacterium tuberculosis analysis; oligopeptides analysis solation & purification; peptides; peptidoglycan analysis; pimelic acids analysis; species specificity; stereoisomerism; streptomyces enzymology

Abstract :

[en] Cross-linking between peptide units in the wall peptidoglycan of Mycobacterium smegmatis 21732 ATCC is mediated through D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid linkages occurring in a ratio of about 2:1. The occurrence of D-alanyl-(D)-meso-diaminopimelic acid linkages was established by the action of the Streptomyces albus G DD-carboxypeptidase. The occurrence of meso-diaminopimelyl-meso-diaminopimelic acid linkages was established by isolation from partial acid hydro-lysates and characterization by mass spectrometric analyses of the dipeptide meso-diaminopimelyl-meso-diaminopimelic acid and the tripeptide meso-diaminopimelyl-meso-diaminopimelyl-meso-diaminopimelic acid. meso-Diaminopimelyl-meso-diami-nopimelic acid interpeptide linkages also occur in the wall peptidoglycan of M. tuberculosis BCG Pasteur strain.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Wietzerbin, Juana; Université Paris-Sud 11

Das, Bhupsh C.; Centre National de la Recherche Scientifique - CNRS

Petit, Jean-François; Université Paris-Sud 11

Lederer, Edgar; Université Paris-Sud 11

Leyh-Bouille, Mélina; Université de Liège - ULiège > Institut de Botanique > Service de Microbiologie

Ghuysen, Jean-Marie ; Université de Liège - ULiège > Institut de Botanique > Service de Microbiologie

Language :

English

Title :

Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria

Publication date :

13 August 1974

Journal title :

Biochemistry

ISSN :

0006-2960

eISSN :

1520-4995

Publisher :

American Chemical Society, Washington, United States - District of Columbia

Volume :

Issue :

Pages :

3471-3476

Peer reviewed :

Peer Reviewed verified by ORBi

Funders :

FRM - Fondation pour la Recherche Médicale
New York Cancer Research Institut
FRFC - Fonds de la Recherche Fondamentale Collective

Available on ORBi :

since 17 February 2011

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Bibliography

Adam, A., Petit, J. F., Wietzerbin-Falszpan, J., Sinay, P., Thomas, D. W., and Lederer, E. (1969), FEBS (Fed. Eur. Biochem. Soc.) Lett. 4, 87.
Azuma, I., Thomas, D. W., Adam, A., Ghuysen, J. M., Bonaly, R., Petit, J. F., and Lederer, E (1970), Biochim. Biophys. Acta 208, 444.
Bricas, E., Ghuysen, J. M., and Dezélée, P. (1967), Biochemistry 6, 2598.
Coyette, J., Perkins, H. R., Polacheck, L., Shockman, G. D., and Ghuysen, J. M. (1974), Eur. J. Biochem. (in press).
Cunto, G., Kanetsuna, F., and Imaeda, T. (1969), Biochim, Biophys. Acta 192, 358.
Ghuysen, J. M. (1968), Bacteriol. Rev. 32, 425.
Ghuysen, M. M., Tipper, D. J., and Strominger, J. L. (1966), Methods Enzymol. 8, 685.
Hash, J. H. (1963), Arch. Biochem. Biophys. 102, 379.
Kotani, S., Yanagida, L, Kato, K., and Matsuda, T. (1970), Biken J. 13, 249.
Lederer, E. (1971), Pure Appl. Chem. 25, 135.
Leyh-Bouille, M., Ghuysen, J. M., Bonaly, R., Nieto, M., Perkins, H. R., Schleifer, K. H., and Kandler, O. (1970), Biochemistry 9, 2961.
Schleifer, K. H., and Kandler, O. (1972), Bacteriol. Rev. 36, 407.
Wietzerbin-Falszpan, J., Das, B. C., Azuma, I., Adam, A., Petit, J. F., and Lederer, E. (1970), Biochem. Biophys. Res. Commun. 40, 57.
Wietzerbin-Falszpan, J., Das, B. C., Gros, C, Petit, J. F., and Lederer, E. (1973), Eur. J. Biochem. 32, 525.