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Penicillin Sensitive Formation of D‐Alanine in a Particulate System from Staphylococcus Aureus
Author(s) -
Oppenheim B.,
Burstein Y.,
Patchornik A.
Publication year - 1972
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197200008
Subject(s) - peptidoglycan , chemistry , lipid ii , staphylococcus aureus , alanine , pentapeptide repeat , glycine , moiety , penicillin , biochemistry , cell wall , stereochemistry , microbiology and biotechnology , amino acid , antibiotics , bacteria , peptide , biology , genetics
Abstract A cell free system from Staphylococcus aureus 52A5 which incorporates UDPMurNAc‐L‐ala‐D‐isoglu‐L‐lys‐D‐ala‐ 14 C‐D‐ala into lipid intermediates and peptidoglycan is described. During peptidoglycan synthesis, glycine binding to the lipid intermediates and peptidoglycan is also demonstrated as well as release of the terminal D‐alanine from the pentapeptide moiety. This release of D‐alanine is strongly inhibited by penicillin G.