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. 1974 Oct;120(1):173–184. doi: 10.1128/jb.120.1.173-184.1974

Appearance of a γ-d-Glutamyl-(l)Meso-Diaminopimelate Peptidoglycan Hydrolase During Sporulation in Bacillus sphaericus

M Guinand 1, G Michel 1, D J Tipper 1
PMCID: PMC245747  PMID: 4417809

Abstract

Particulate preparations from sporulating cells of Bacillus sphaericus 9602 contained an endopeptidase activity that hydrolyzed the γ-d-glutamyl-(l)meso-diaminopimelic acid linkages found in the spore cortical peptidoglycan of this organism. Diaminopimelic acid did not occur in the vegetative cell wall peptidoglycan, and the γ-d-glutamyl-l-lysine linkages found in this polymer were not hydrolyzed by the endopeptidase. The endopeptidase hydrolyzed (X)-l-alanyl-γ-d-glutamyl-(l)meso-diaminopimelyl(l)-d-alanyl-d-alanine only after removal of the terminal d-alanine residue. The preparations contained an acyl-d-alanyl-d-alanine carboxypeptidase I activity which converted such pentapeptides into substrates for the endopeptidase and which was inhibited 50% by 4 × 10−7 M benzylpenicillin. This activity also hydrolyzed the analogous pentapeptide substrates containing l-lysine. The preparations also contained an acyl-l-lysyl-d-alanine carboxypeptidase II activity that was not active on the meso-diaminopimelic acid-containing analogue. Neither this activity nor the endopeptidase was inhibited by 10−3 M benzylpenicillin. The specificities of the carboxypeptidases were consistent with the exclusive presence of l-lysine C-termini in the vegetative peptidoglycan and of meso-diaminopimelyl-d-alanine C-termini in the spore cortical peptidoglycan of B. sphaericus 9602.

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Selected References

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

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