[Affinity of exocellular DD-carboxypeptidase/transpeptidase from Saccharopolyspora erythraea PZH TZ-575 to beta-lactam compounds].
The DD-carboxypeptidase/transpeptidases (DD-peptidases) involved in bacterial cell wall metabolism, catalyse the attack of C-terminal D-alanyl-D-alanine peptide bond of the peptydoglycan precursor. These enzymes are inactivated by beta-lactam antibiotics. DD-peptidase from Saccharopolyspora erythraea PZH TZ 64-575 was purified by the use of DEAE-cellulose, Sephadex G-100, Q-Sepharose resins and FPLC (Mono Q). After each step the effluent was concentrated by Amicon ultrafiltration. The purified enzyme showed DD-carboxypeptidase specific activity of 50.9 U/mg. The enzyme exhibited high affinity to beta-lactam compounds e.g. cefamandole, cefapirin, cefradin 1.5-2.6 x 10(-8) M. It was used to screen strains from the Culture Collection of the National Institute of Hygiene in Warsaw for the production of DD-peptidase inhibitors.
Solecka
J
J
Samodzielna Pracownia Promieniowców i Grzybów Niedoskonałych Państwowego Zakładu Higieny w Warszawie.
Kurzatkowski
W
W
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D002384:Catalysis; D004789:Enzyme Activation / Q000187:drug effects; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism; D016930:Saccharopolyspora / Q000187:drug effects / Q000201:enzymology*; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D047090:beta-Lactams; D002267:Muramoylpentapeptide Carboxypeptidase
Powinowactwo zewnatrzkomórkowej DD-karboksypeptydazy/transpeptydazy szczepu Saccharopolyspora erythraea PZH TZ 64-575 do zwiazków beta-laktamowych.