Abstract:
:A membrane fraction from Pseudomonas aeruginosa KM 338 was shown to catalyze in vitro peptidoglycan synthesis from uridine 5'-diphosphate-N-acetylmuramyl-l-alanyl-d- glutamyl-meso-diaminopimelyl-d-alanyl-d-alanine and uridine 5'-diphosphate-N-acetylglucosamine. Synthesized peptidoglycan was partially cross-linked by transpeptidation, which was accompanied by the release of d-alanine. This reaction was strongly inhibited by 25 and 50 mug of penicillin G and carbenicillin per ml respectively, whereas the intact cells were relatively resistant to penicillins (minimal inhibitory concentration of penicillin G and carbenicillin, 30 and 0.125 mg/ml, respectively). Soluble d-alanine carboxypeptidase present in P. aeruginosa KM 338 was studied as well, which was found almost completely inhibited by penicillin G and carbenicillin (10 mug/ml).
journal_name
Antimicrob Agents Chemotherjournal_title
Antimicrobial agents and chemotherapyauthors
Suginaka H,Ichikawa A,Kotani Sdoi
10.1128/aac.6.6.672subject
Has Abstractpub_date
1974-12-01 00:00:00pages
672-5issue
6eissn
0066-4804issn
1098-6596journal_volume
6pub_type
杂志文章abstract::Emergence of resistance to pentavalent antimonials has become a severe obstacle in the treatment of visceral leishmaniasis (VL) on the Indian subcontinent. The mechanisms operating in laboratory-generated strains are somewhat known, but the determinants of clinical antimony resistance are not well understood. By utili...
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