Murphy B P, Pratt R F
Department of Chemistry, Wesleyan University, Middletown, CT 06457.
Biochem J. 1988 Dec 1;256(2):669-72. doi: 10.1042/bj2560669.
A thionocephalosporin is shown to be a much poorer substrate of representative serine beta-lactamases of class A (RTEM-2) and class C (Enterobacter cloacae P99) and a much poorer inhibitor of the Streptomyces R61 DD-peptidase than is the analogous oxo beta-lactam. These results provide kinetic evidence for the existence of a catalytic oxyanion hole in these enzymes.
与类似的氧代β-内酰胺相比,硫代头孢菌素是A类(RTEM-2)和C类(阴沟肠杆菌P99)代表性丝氨酸β-内酰胺酶的更差底物,也是链霉菌R61 D-肽酶的更差抑制剂。这些结果为这些酶中催化性氧阴离子洞的存在提供了动力学证据。