克拉维酸与白色链霉菌G和马杜拉放线菌R39的β-内酰胺酶的相互作用。
Interaction of clavulanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39.
作者信息
Frère J M, Dormans C, Lenzini V M, Duyckaerts C
出版信息
Biochem J. 1982 Dec 1;207(3):429-36. doi: 10.1042/bj2070429.
Abstract
The reactions of beta-lactamases of Actinomadura R39 and Streptomyces albus G with clavulanate proceed along branched pathways. Both enzymes perform the hydrolysis of this beta-lactam with rather high efficiencies (kcat. = 18s-1 and 52s-1 respectively). If large clavulanate/enzyme ratios are used, complete inactivation of the enzymes is observed. At lower ratios, inactivation is only partial. Irreversible inactivation occurs after 400 and 20000 turnovers for the A. R39 and S. albus G enzymes respectively. With the A. R39 beta-lactamase, a transiently inhibited complex is also formed that remains undetectable with the S. albus G beta-lactamase. Kinetic models are presented and studied for the interaction between clavulanate and both enzymes. A tentative general reaction scheme is also discussed.
摘要
马杜拉放线菌R39和白色链霉菌G的β-内酰胺酶与棒酸的反应沿着分支途径进行。两种酶都以相当高的效率催化这种β-内酰胺的水解（催化常数分别为18s⁻¹和52s⁻¹）。如果使用大的棒酸/酶比例，会观察到酶的完全失活。在较低比例下，失活只是部分的。对于马杜拉放线菌R39和白色链霉菌G的酶，分别在400次和20000次周转后发生不可逆失活。对于马杜拉放线菌R39的β-内酰胺酶，还形成了一种瞬时抑制复合物，而白色链霉菌G的β-内酰胺酶则未检测到该复合物。提出并研究了棒酸与两种酶相互作用的动力学模型。还讨论了一个初步的通用反应方案。
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