D-alanine carboxypeptidase from Streptococcus faecalis
作者： Bina Oppenheim , R. Koren , A. Patchornik
DOI: 10.1016/0006-291X(74)90583-X
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摘要: Abstract A particulate D-alanine carboxypeptidase that can cleave the terminal residue of from UDPMurNAc-L-ala-D-isoglu-L-lys-D-ala-D-ala was isolated Streptococcus faecalis . The enzyme inhibited by penicillin G non-competitively with a Ki 0.8 μM. solubilized Triton X-100 without loss catalytic activity. In this form it could also be G.
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