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The importance of the negative charge of β‐lactam compounds for the inactivation of the active‐site serine DD‐peptidase of Streptomyces R61
Author(s) -
Varetto Louis,
Frère Jean-Marie,
Ghuysen Jean-Marie
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81161-4
Subject(s) - chemistry , enzyme , carboxylate , stereochemistry , serine , lactam , active site , streptomyces , penicillin , covalent bond , cephalosporin , derivative (finance) , biochemistry , antibiotics , organic chemistry , biology , bacteria , financial economics , economics , genetics
The interaction between the Streptomyces R61 penicillin‐sensitive DD‐peptidase and deacetyl‐cephalosporin C or its lactone derivative has been studied at different pH values. The results show the importance of an enzyme group of p K ≌ 9 which might form an ion pair with the free carboxylate of the former compound. This electrostatic interaction is shown to contribute to the formation of the first, non‐covalent enzyme‐inactivator complex by a factor of at least 50.