Caracterisation d'une nouvelle endopeptidase specifique des liaisons gamma-d-glutamyl-l-lysine et gamma-d-glutamyl-(l)meso-diaminopimelate de substrats peptidoglycaniques, chez Bacillus sphaericus 9602 au cours de la sporulation

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Abstract
Characterisation of a New Endopeptidase from Sporulating Bacillus sphaericus which is Specfic for the γ‐d‐Glutamyl‐l‐lysine and γ‐d‐Glutamyl‐(l) meso‐dinminopimelate Linkages of Peptidoglycan Substrates A new peptidase which splits substrates related to the peptidic chains of peptidoglycans was found in the cell cytoplasm of sporulating Bacillus sphaericus. This is a γ‐d‐glutamyl‐l‐diaminoacid endopeptidase (endopeptidase II). It was shown to have substrate requirements different from those of the previously described γ‐d‐glutamyl‐(l) meso‐diaminopimelate endopeptidase (endopeptidase I). The substrates for endopeptidase II are peptides of the general type Unsubstituted N‐terminal l‐alanine was a strict requirement for endopeptidase II activity. Specific activities were variable with the nature and the substitution of the diaminoacid C‐terminal groups. The role of endopeptidase II in the biosynthesis of the spore cortex is discussed.

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