[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)]

Eur J Biochem. 1979 Oct;100(1):189-96. doi: 10.1111/j.1432-1033.1979.tb02048.x.
[Article in French]

Abstract

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.

MeSH terms

  • Bacillus / enzymology*
  • Diaminopimelic Acid
  • Dipeptides
  • Endopeptidases / isolation & purification
  • Endopeptidases / metabolism*
  • Glutamates
  • Kinetics
  • Lysine
  • Peptidoglycan*
  • Spores, Bacterial / enzymology
  • Substrate Specificity

Substances

  • Dipeptides
  • Glutamates
  • Peptidoglycan
  • Diaminopimelic Acid
  • Endopeptidases
  • Lysine