[Characterisation of a new endopeptidase from sporulating Bacillus sphaericus which is specific for the gamma-D-glutamyl-L-lysine and gamma-D-glutamyl-(L)meso-diaminopimelate linkages of peptidoglycan substrates (author's transl)].
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 gamma-D-glutamyl-L-diaminoacid endopeptidase (endopeptidase II). It was shown to have substrate requirements different from those of the previously described gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase (endopeptidase I). The substrates for endopeptidase II are peptides of the general type: formula: (see text). 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.
D001407:Bacillus / Q000201:enzymology*; D003960:Diaminopimelic Acid; D004151:Dipeptides; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005971:Glutamates; D007700:Kinetics; D008239:Lysine; D010457:Peptidoglycan; D013171:Spores, Bacterial / Q000201:enzymology; D013379:Substrate Specificity
D004151:Dipeptides; D005971:Glutamates; D010457:Peptidoglycan; D003960:Diaminopimelic Acid; D010450:Endopeptidases; D008239:Lysine
Caractérisation d'une nouvelle endopeptidase spécifique des liaisons gamma-D-glutamyl-L-lysine et gamma-D-glutamyl-(L)meso-diaminopimélate de substrats peptidoglycaniques, chez Bacillus sphaericus 9602 au cours de la sporulation.