噬菌体PBS2诱导枯草芽孢杆菌中的脱氧胞苷三磷酸脱氨酶。
Bacteriophage PBS2-induced deoxycytidine triphosphate deaminase in Bacillus subtilis.
作者信息
Price A R
出版信息
J Virol. 1974 Nov;14(5):1314-7. doi: 10.1128/JVI.14.5.1314-1317.1974.
Abstract
The dCTP deaminase induced by Bacillus subtilis bacteriophage PBS2, whose DNA contains uracil instead of thymine, requires metal ion and thiol activators and has a molecular weight of 125,000. The enzyme displays sigmoidal substrate saturation kinetics and inhibition by dUTP, consistent with the deaminase's proposed role of providing balanced levels of dUTP and dCTP for PBS2 uracil-DNA synthesis.
摘要
由枯草芽孢杆菌噬菌体PBS2诱导产生的dCTP脱氨酶，其DNA含有尿嘧啶而非胸腺嘧啶，该酶需要金属离子和硫醇激活剂，分子量为125,000。该酶表现出S形底物饱和动力学以及受dUTP抑制，这与该脱氨酶为PBS2尿嘧啶-DNA合成提供平衡水平的dUTP和dCTP的推测作用相一致。
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