β-碘青霉烷酸与白色链霉菌G和马杜拉放线菌R39的β-内酰胺酶的相互作用
Interaction of beta-iodopenicillanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39.
作者信息
Frère J M, Dormans C, Duyckaerts C, De Graeve J
出版信息
Biochem J. 1982 Dec 1;207(3):437-44. doi: 10.1042/bj2070437.
Abstract
The beta-lactamases of Streptomyces albus G and Actinomadura R39 are inactivated by beta-iodopenicillanate. However, in contrast with the beta-lactamase I from Bacillus cereus, they also efficiently catalyse the hydrolysis of the inactivator; with the S. albus G enzyme, kcat. is larger than 25s-1 and the number of turnovers before inactivation is 515. With the A. R39 enzyme, kcat. is larger than 50s-1 and the number of turnovers before inactivation is 80. After hydrolysis of the beta-lactam amide bond, the product rearranges into 2.3-dihydro-2,2-dimethyl-1,4-thiazine-3,6-dicarboxylate, which exhibits an absorption maximum at 305 nm.
摘要
白色链霉菌G和马杜拉放线菌R39的β-内酰胺酶可被β-碘青霉素酸灭活。然而，与蜡样芽孢杆菌的β-内酰胺酶I不同，它们也能高效催化灭活剂的水解；对于白色链霉菌G酶，kcat大于25s-1，灭活前的周转数为515。对于马杜拉放线菌R39酶，kcat大于50s-1，灭活前的周转数为80。β-内酰胺酰胺键水解后，产物重排为2,3-二氢-2,2-二甲基-1,4-噻嗪-3,6-二羧酸盐，其在305nm处有最大吸收。
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