A particulate D-alanine carboxypeptidase that can cleave the terminal residue of D-alanine from UDPMurNAc-L-ala-D-isoglu-L-lys-D-ala-D-ala was isolated from Streptococcus faecalis. The enzyme was inhibited by penicillin G non-competitively with a Ki of 0.8 μM. The carboxypeptidase was solubilized with Triton X-100 without loss of catalytic activity. In this form it could also be inhibited by penicillin G.
|Number of pages||10|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 8 Apr 1974|