D-alanine carboxypeptidase from Streptococcus faecalis

Bina Oppenheim, R. Koren, A. Patchornik

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)562-571
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume57
Issue number3
DOIs
StatePublished - 8 Apr 1974
Externally publishedYes

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