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- W2046876730 abstract "Initially, cefotetan interacts with beta-lactamases to form a classical Michaelis complex characterized by a term Ki (the inhibition constant). In a second phase, this complex develops with time to form a new entity devoid of enzymic activity. This new entity may have the structure of an acyl enzyme with variable stability. In the case of TEM-1 and TEM-2 beta-lactamases, the process is progressively and totally reversible. The same phenomena were observed in varying degrees for Pitton's type 2 (PIT-2) penicillinase, OXA-1 and CARB-1. The Klebsiella oxytoca and Proteus vulgaris beta-lactamases are also inactivated by this same process. However, four other cephalosporinases appear to be unaffected by this mechanism." @default.
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- W2046876730 date "1983-01-01" @default.
- W2046876730 modified "2023-10-14" @default.
- W2046876730 title "Cefotetan and -lactamases: II. An unusual property: the inactivation of some -lactamases by cefotetan" @default.
- W2046876730 doi "https://doi.org/10.1093/jac/11.suppl_a.153" @default.
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