Beta-lactamase activity of purified and partially characterized human renal dipeptidase.
نویسندگان
چکیده
منابع مشابه
The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-beta-lactamase enzyme CphA.
The Aeromonas hydrophila AE036 chromosome contains a cphA gene encoding a metallo-beta-lactamase which is highly active against carbapenem antibiotics such as imipenem. Here we show that the cphA gene product shares inhibitory similarities with a mammalian zinc peptidase, membrane dipeptidase (MDP; dehydropeptidase I). Both enzymes are able to hydrolyze imipenem and are inhibited by cilastatin....
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In vitro activity and beta-lactamase stability of cefmenoxime.
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In our previous papers1»2), we described the structure-activity relationships of 6-(heterocyclyl)methylene penam sulfones (1) as a new class of /3-lactamase inhibitors and proposed a mechanism of enzyme inactivation for series 1. In continuation of these studies with series 1, we pursued the closely related structures in series 2, since they should follow a similar mechanistic pathway and shoul...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)42642-1