大肠杆菌的环3',5'-腺苷单磷酸磷酸二酯酶
Cyclic 3',5'-adenosine monophosphate phosphodiesterase of Escherichia coli.
作者信息
Nielsen L D, Monard D, Rickenberg H V
出版信息
J Bacteriol. 1973 Nov;116(2):857-66. doi: 10.1128/jb.116.2.857-866.1973.
Abstract
The cyclic 3',5'-adenosine monophosphate (c-AMP) phosphodiesterase from Escherichia coli has been partially purified. The enzyme has an apparent molecular weight of 30,000, a Michaelis constant of 0.5 mM c-AMP, and a pH optimum of 7. The partially purified enzyme requires for activity the presence of a reducing compound and of either iron or a protein which seemingly acts as iron carrier.
摘要
来自大肠杆菌的环3',5'-腺苷单磷酸（c-AMP）磷酸二酯酶已被部分纯化。该酶的表观分子量为30,000，米氏常数为0.5 mM c-AMP，最适pH值为7。部分纯化的酶的活性需要一种还原化合物以及铁或一种似乎作为铁载体的蛋白质的存在。
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