Labia R, Thabaut A, Morand A, Tiwari K, Sirot D, Sirot J
National Museum of Natural History, UA 401 CNRS, Paris, France.
Drugs Exp Clin Res. 1989;15(11-12):535-40.
The kinetic constants for "CAZ-5", a novel plasmid-mediated beta-lactamase with noticeable activity against third-generation cephalosporins and particularly ceftazidime have been determined. Two closely-related plasmid-mediated beta-lactamases have also been studied: SHV-2 and PIT-2 (also known as SHV-1). These enzymes were synthesized constitutively; they were highly sensitive to the action of the inhibitors clavulanic acid and sulbactam and they lacked activity against the cephamycins and imipenem. PIT-2/SHV-1 had poor hydrolytic activity against the third-generation cephalosporins, SHV-2 was markedly active against cefotaxime and related compounds, whereas the new enzyme, which was also active against these cephalosporins, had a noticeably greater activity against ceftazidime. Aztreonam was slowly hydrolysed by CAZ-5 beta-lactamase, but demonstrated an unusually high affinity for this enzyme.
已测定了“CAZ-5”(一种新型质粒介导的β-内酰胺酶,对第三代头孢菌素尤其是头孢他啶具有显著活性)的动力学常数。还研究了两种密切相关的质粒介导的β-内酰胺酶:SHV-2和PIT-2(也称为SHV-1)。这些酶是组成型合成的;它们对抑制剂克拉维酸和舒巴坦的作用高度敏感,并且对头孢霉素和亚胺培南缺乏活性。PIT-2/SHV-1对第三代头孢菌素的水解活性较差,SHV-2对头孢噻肟及相关化合物具有显著活性,而这种对这些头孢菌素也有活性的新酶对头孢他啶的活性明显更高。氨曲南被CAZ-5β-内酰胺酶缓慢水解,但对该酶表现出异常高的亲和力。